EC 2.1.1.1 to EC 2.1.1.50
EC 2.1.1.51 to EC 2.1.1.100
EC 2.1.1.101 to EC 2.1.1.150
EC 2.1.1.151 to EC 2.1.1.200
EC 2.1.1.201 to EC 2.1.1.250
EC 2.1.1.251 to EC 2.1.1.300
Accepted name: cypemycin N-terminal methyltransferase
Reaction: 2 S-adenosyl-L-methionine + N-terminal L-alanine-[cypemycin] = 2 S-adenosyl-L-homocysteine + N-terminal N,N-dimethyl-L-alanine-[cypemycin]
Other name(s): CypM
Systematic name: S-adenosyl-L-methionine:N-terminal L-alanine-[cypemycin] N-methyltransferase
Comments: The enzyme, isolated from the bacterium Streptomyces sp. OH-4156, can methylate a variety of linear oligopeptides, cyclic peptides such as nisin and haloduracin, and the ε-amino group of lysine [2]. Cypemycin is a peptide antibiotic, a member of the linaridins, a class of posttranslationally modified ribosomally synthesized peptides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Claesen, J. and Bibb, M. Genome mining and genetic analysis of cypemycin biosynthesis reveal an unusual class of posttranslationally modified peptides. Proc. Natl. Acad. Sci. USA 107 (2010) 16297-16302. [PMID: 20805503]
2. Zhang, Q. and van der Donk, W.A. Catalytic promiscuity of a bacterial α-N-methyltransferase. FEBS Lett 586 (2012) 3391-3397. [PMID: 22841713]
Accepted name: 3-hydroxy-5-methyl-1-naphthoate 3-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 3-hydroxy-5-methyl-1-naphthoate = S-adenosyl-L-homocysteine + 3-methoxy-5-methyl-1-naphthoate
For diagram of reaction click here.
Other name(s): AziB2
Systematic name: S-adenosyl-L-methionine:3-hydroxy-5-methyl-1-naphthoate 3-O-methyltransferase
Comments: The enzyme from the bacterium Streptomyces sahachiroi is involved in the biosynthesis of 3-methoxy-5-methyl-1-naphthoate, a component of of the the antitumor antibiotic azinomycin B.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Ding, W., Deng, W., Tang, M., Zhang, Q., Tang, G., Bi, Y. and Liu, W. Biosynthesis of 3-methoxy-5-methyl naphthoic acid and its incorporation into the antitumor antibiotic azinomycin B. Mol. Biosyst. 6 (2010) 1071-1081. [PMID: 20485749]
Accepted name: 2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 2,7-dihydroxy-5-methyl-1-naphthoate = S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
For diagram of reaction click here.
Other name(s): NcsB1; neocarzinostatin O-methyltransferase
Systematic name: S-adenosyl-L-methionine:2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase
Comments: The enzyme from the bacterium Streptomyces carzinostaticus is involved in the biosynthesis of 2-hydroxy-7-methoxy-5-methyl-1-naphthoate. This compound is part of the enediyne chromophore of the antitumor antibiotic neocarzinostatin. In vivo the enzyme catalyses the regiospecific methylation at the 7-hydroxy group of its native substrate 2,7-dihydroxy-5-methyl-1-naphthoate. In vitro it also recognizes other dihydroxynaphthoic acids and catalyses their regiospecific O-methylation.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Luo, Y., Lin, S., Zhang, J., Cooke, H.A., Bruner, S.D. and Shen, B. Regiospecific O-methylation of naphthoic acids catalyzed by NcsB1, an O-methyltransferase involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin. J. Biol. Chem. 283 (2008) 14694-14702. [PMID: 18387946]
2. Cooke, H.A., Guenther, E.L., Luo, Y., Shen, B. and Bruner, S.D. Molecular basis of substrate promiscuity for the SAM-dependent O-methyltransferase NcsB1, involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin. Biochemistry 48 (2009) 9590-9598. [PMID: 19702337]
Accepted name: L-tyrosine C3-methyltransferase
Reaction: S-adenosyl-L-methionine + L-tyrosine = S-adenosyl-L-homocysteine + 3-methyl-L-tyrosine
For diagram of reaction click here.
Other name(s): SfmM2; SacF
Systematic name: S-adenosyl-L-methionine:L-tyrosine C3-methyltransferase
Comments: The enzyme from the bacterium Streptomyces lavendulae is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Tang, M.C., Fu, C.Y. and Tang, G.L. Characterization of SfmD as a heme peroxidase that catalyzes the regioselective hydroxylation of 3-methyltyrosine to 3-hydroxy-5-methyltyrosine in saframycin A biosynthesis. J. Biol. Chem. 287 (2012) 5112-5121. [PMID: 22187429]
Accepted name: 8-demethyl-8-α-L-rhamnosyltetracenomycin-C 2'-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 8-demethyl-8-α-L-rhamnosyltetracenomycin C = S-adenosyl-L-homocysteine + 8-demethyl-8-(2-O-methyl-α-L-rhamnosyl)tetracenomycin C
For diagram of reaction click here.
Glossary: 8-demethyl-8-α-L-rhamnosyltetracenomycin C = methyl (6aR,7S,10aR)-6a,7,10a,12-tetrahydroxy-8-methoxy-1-methyl-6,10,11-trioxo-3-α-L-rhamnosyloxy-6,6a,7,10,10a,11-hexahydrotetracene-2-carboxylate
Other name(s): ElmMI
Systematic name: S-adenosyl-L-methionine:8-demethyl-8-α-L-rhamnosyltetracenomycin-C 2'-O-methyltransferase
Comments: The enzyme from the bacterium Streptomyces olivaceus is involved in the biosynthesis of the polyketide elloramycin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Patallo, E.P., Blanco, G., Fischer, C., Brana, A.F., Rohr, J., Mendez, C. and Salas, J.A. Deoxysugar methylation during biosynthesis of the antitumor polyketide elloramycin by Streptomyces olivaceus. Characterization of three methyltransferase genes. J. Biol. Chem. 276 (2001) 18765-18774. [PMID: 11376004]
Accepted name: 8-demethyl-8-(2-methoxy-α-L-rhamnosyl)tetracenomycin-C 3'-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 8-demethyl-8-(2-O-methyl-α-L-rhamnosyl)tetracenomycin C = S-adenosyl-L-homocysteine + 8-demethyl-8-(2,3-di-O-methyl-α-L-rhamnosyl)tetracenomycin C
For diagram of reaction click here.
Glossary: 8-demethyl-8-α-L-rhamnosyltetracenomycin C = methyl (6aR,7S,10aR)-6a,7,10a,12-tetrahydroxy-8-methoxy-1-methyl-6,10,11-trioxo-3-α-L-rhamnosyloxy-6,6a,7,10,10a,11-hexahydrotetracene-2-carboxylate
Other name(s): ElmMII
Systematic name: S-adenosyl-L-methionine:8-demethyl-8-(2-methoxy-α-L-rhamnosyl)tetracenomycin-C 3'-O-methyltransferase
Comments: The enzyme from the bacterium Streptomyces olivaceus is involved in the biosynthesis of the polyketide elloramycin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Patallo, E.P., Blanco, G., Fischer, C., Brana, A.F., Rohr, J., Mendez, C. and Salas, J.A. Deoxysugar methylation during biosynthesis of the antitumor polyketide elloramycin by Streptomyces olivaceus. Characterization of three methyltransferase genes. J. Biol. Chem. 276 (2001) 18765-18774. [PMID: 11376004]
Accepted name: 8-demethyl-8-(2,3-dimethoxy-α-L-rhamnosyl)tetracenomycin-C 4'-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 8-demethyl-8-(2,3-di-O-methyl-α-L-rhamnosyl)tetracenomycin C = S-adenosyl-L-homocysteine + 8-demethyl-8-(2,3,4-tri-O-methyl-α-L-rhamnosyl)tetracenomycin C
For diagram of reaction click here.
Glossary: 8-demethyl-8-α-L-rhamnosyltetracenomycin C = methyl (6aR,7S,10aR)-6a,7,10a,12-tetrahydroxy-8-methoxy-1-methyl-6,10,11-trioxo-3-α-L-rhamnosyloxy-6,6a,7,10,10a,11-hexahydrotetracene-2-carboxylate
Other name(s): ElmMIII
Systematic name: S-adenosyl-L-methionine:8-demethyl-8-(2,3-di-O-methoxy-α-L-rhamnosyl)tetracenomycin-C 4'-O-methyltransferase
Comments: The enzyme from the bacterium Streptomyces olivaceus is involved in the biosynthesis of the polyketide elloramycin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Patallo, E.P., Blanco, G., Fischer, C., Brana, A.F., Rohr, J., Mendez, C. and Salas, J.A. Deoxysugar methylation during biosynthesis of the antitumor polyketide elloramycin by Streptomyces olivaceus. Characterization of three methyltransferase genes. J. Biol. Chem. 276 (2001) 18765-18774. [PMID: 11376004]
Accepted name: cytidylyl-2-hydroxyethylphosphonate methyltransferase
Reaction: 2 S-adenosyl-L-methionine + cytidine 5'-{[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate} + reduced acceptor = S-adenosyl-L-homocysteine + 5'-deoxyadenosine + L-methionine + cytidine 5'-({hydroxy[(S)2-hydroxypropyl]phosphonoyl}phosphate) + oxidized acceptor
For diagram of reaction, click here
Other name(s): Fom3; S-adenosyl-L-methionine:methylcob(III)alamin:2-hydroxyethylphosphonate methyltransferase (incorrect); 2-hydroxyethylphosphonate methyltransferase (incorrect)
Systematic name: S-adenosyl-L-methionine:cytidine 5'-{[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate} C-methyltransferase
Comments: Requires cobalamin. The enzyme, isolated from the bacterium Streptomyces wedmorensis, is involved in fosfomycin biosynthesis. It is a radical S-adenosyl-L-methionine (SAM) enzyme that contains a [4Fe-4S] center and a methylcob(III)alamin cofactor. The enzyme uses two molecues of SAM for the reaction. One molecule forms a 5'-deoxyadenosyl radical, while the other is used to methylate the cobalamin cofactor. The 5'-deoxyadenosyl radical abstracts a hydrogen from the C2 position of cytidine 5'-{[(2-hydroxyethyl)phosphonoyl]phosphate} forming a free radical that reacts with the methyl group on methylcob(III)alamin at the opposite side from SAM and the [4Fe-4S]cluster to produce a racemic mix of methylated products and cob(II)alamin. Both the [4Fe-4S]cluster and the cob(II)alamin need to be reduced by an unknown factor(s) before the enzyme could catalyse another cycle.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1. Woodyer, R.D., Li, G., Zhao, H. and van der Donk, W.A. New insight into the mechanism of methyl transfer during the biosynthesis of fosfomycin. Chem. Commun. (Camb.) (2007) 359-361. [PMID: 17220970]
2. Allen, K.D. and Wang, S.C. Initial characterization of Fom3 from Streptomyces wedmorensis: The methyltransferase in fosfomycin biosynthesis. Arch. Biochem. Biophys. 543 (2014) 67-73. [PMID: 24370735]
3. Sato, S., Kudo, F., Kim, S.Y., Kuzuyama, T. and Eguchi, T. Methylcobalamin-dependent radical SAM C-methyltransferase Fom3 recognizes cytidylyl-2-hydroxyethylphosphonate and catalyzes the nonstereoselective C-methylation in fosfomycin biosynthesis. Biochemistry 56 (2017) 3519-3522. [PMID: 28678474]
4. Blaszczyk, A.J. and Booker, S.J. A (re)discovery of the Fom3 substrate. Biochemistry 57 (2018) 891-892. [PMID: 29345912]
5. Sato, S., Kudo, F., Kuzuyama, T., Hammerschmidt, F. and Eguchi, T. C-methylation catalyzed by Fom3, a cobalamin-dependent radical S-adenosyl-L-methionine enzyme in fosfomycin biosynthesis, proceeds with inversion of configuration. Biochemistry 57 (2018) 4963-4966. [PMID: 29966085]
Accepted name: 18S rRNA (guanine1575-N7)-methyltransferase
Reaction: S-adenosyl-L-methionine + guanine1575 in 18S rRNA = S-adenosyl-L-homocysteine + N7-methylguanine1575 in 18S rRNA
Other name(s): 18S rRNA methylase Bud23; BUD23 (gene name)
Systematic name: S-adenosyl-L-methionine:18S rRNA (guanine1575-N7)-methyltransferase
Comments: The enzyme, found in eukaryotes, is involved in pre-rRNA processing. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. White, J., Li, Z., Sardana, R., Bujnicki, J.M., Marcotte, E.M. and Johnson, A.W. Bud23 methylates G1575 of 18S rRNA and is required for efficient nuclear export of pre-40S subunits. Mol. Cell Biol. 28 (2008) 3151-3161. [PMID: 18332120]
Accepted name: 25S rRNA (cytosine2870-C5)-methyltransferase
Reaction: S-adenosyl-L-methionine + cytosine2870 in 25S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA
Other name(s): NOP2 (gene name)
Systematic name: S-adenosyl-L-methionine:25S rRNA (cytosine2870-C5)-methyltransferase
Comments: The enzyme, found in eukaryotes, is specific for cytosine2870 of the 25S ribosomal RNA. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Sharma, S., Yang, J., Watzinger, P., Kotter, P. and Entian, K.D. Yeast Nop2 and Rcm1 methylate C2870 and C2278 of the 25S rRNA, respectively. Nucleic Acids Res. 41 (2013) 9062-9076. [PMID: 23913415]
Accepted name: 25S rRNA (cytosine2278-C5)-methyltransferase
Reaction: S-adenosyl-L-methionine + cytosine2278 in 25S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Other name(s): RCM1 (gene name)
Systematic name: S-adenosyl-L-methionine:25S rRNA (cytosine2278-C5)-methyltransferase
Comments: The enzyme, found in eukaryotes, is specific for 25S cytosine2278. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sharma, S., Yang, J., Watzinger, P., Kotter, P. and Entian, K.D. Yeast Nop2 and Rcm1 methylate C2870 and C2278 of the 25S rRNA, respectively. Nucleic Acids Res. 41 (2013) 9062-9076. [PMID: 23913415]
Accepted name: 25S rRNA (uracil2843-N3)-methyltransferase
Reaction: S-adenosyl-L-methionine + uracil2843 in 25S rRNA = S-adenosyl-L-homocysteine + N3-methyluracil2843 in 25S rRNA
Other name(s): BMT6
Systematic name: S-adenosyl-L-methionine:tRNA (uracil2843-N3)-methyltransferase
Comments: The enzyme, described from the yeast Saccharomyces cerevisiae, is involved in ribosome biogenesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sharma, S., Yang, J., Duttmann, S., Watzinger, P., Kotter, P. and Entian, K.D. Identification of novel methyltransferases, Bmt5 and Bmt6, responsible for the m3U methylations of 25S rRNA in Saccharomyces cerevisiae. Nucleic Acids Res. 42 (2014) 3246-3260. [PMID: 24335083]
Accepted name: 25S rRNA (uracil2634-N3)-methyltransferase
Reaction: S-adenosyl-L-methionine + uracil2634 in 25S rRNA = S-adenosyl-L-homocysteine + N3-methyluracil2634 in 25S rRNA
Other name(s): BMT5
Systematic name: S-adenosyl-L-methionine:tRNA (uracil2634-N3)-methyltransferase
Comments: The enzyme, described from the yeast Saccharomyces cerevisiae, is involved in ribosome biogenesis.
References:
1. Sharma, S., Yang, J., Duttmann, S., Watzinger, P., Kotter, P. and Entian, K.D. Identification of novel methyltransferases, Bmt5 and Bmt6, responsible for the m3U methylations of 25S rRNA in Saccharomyces cerevisiae. Nucleic Acids Res. 42 (2014) 3246-3260. [PMID: 24335083]
Accepted name: diphthine methyl ester synthase
Reaction: 4 S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] = 4 S-adenosyl-L-homocysteine + diphthine methyl ester-[translation elongation factor 2]
For diagram of reaction click here.
Glossary: diphthine methyl ester = 2-[(3S)-4-methoxy-4-oxo-3-(trimethylammonio)butyl]-L-histidine
Other name(s): S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); Dph5 (ambiguous)
Systematic name: S-adenosyl-L-methionine:2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] methyltransferase (diphthine methyl ester-[translation elongation factor 2]-forming)
Comments: This eukaryotic enzyme is part of the biosynthetic pathway of diphthamide. Different from the archaeal enzyme, which performs only 3 methylations, producing diphthine (cf. EC 2.1.1.98). The relevant histidine of elongation factor 2 is His715 in mammals and His699 in yeast. The order of the 4 methylations is not known.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Chen, J.-Y.C. and Bodley, J.W. Biosynthesis of diphthamide in Saccharomyces cerevisiae. Partial purification and characterization of a specific S-adenosylmethionine:elongation factor 2 methyltransferase. J. Biol. Chem. 263 (1988) 11692-11696. [PMID: 3042777]
2. Moehring, J.M. and Moehring, T.J. The post-translational trimethylation of diphthamide studied in vitro. J. Biol. Chem. 263 (1988) 3840-3844. [PMID: 3346227]
3. Lin, Z., Su, X., Chen, W., Ci, B., Zhang, S. and Lin, H. Dph7 catalyzes a previously unknown demethylation step in diphthamide biosynthesis. J. Am. Chem. Soc. 136 (2014) 6179-6182. [PMID: 24739148]
Accepted name: 27-O-demethylrifamycin SV methyltransferase
Reaction: S-adenosyl-L-methionine + 27-O-demethylrifamycin SV = S-adenosyl-L-homocysteine + rifamycin SV
Glossary: rifamycin SV = (7S,9E,11S,12R,13S,14R,15R,16R,17S,18S,19E,21Z)-2,15,17,27,29-pentahydroxy-11-methoxy-3,7,12,14,16,18,22-heptamethyl-6,23-dioxo-8,30-dioxa-24-azatetracyclo[23.3.1.14,7.05,28]triaconta-1(28),2,4,9, 19,21,25(29),26-octaen-13-yl acetate
Other name(s): AdoMet:27-O-demethylrifamycin SV methyltransferase
Systematic name: S-adenosyl-L-methionine:27-O-demethylrifamycin-SV 27-O-methyltransferase
Comments: The enzyme, characterized from the bacterium Amycolatopsis mediterranei, is involved in biosynthesis of the antitubercular drug rifamycin B.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Xu, J., Mahmud, T. and Floss, H.G. Isolation and characterization of 27-O-demethylrifamycin SV methyltransferase provides new insights into the post-PKS modification steps during the biosynthesis of the antitubercular drug rifamycin B by Amycolatopsis mediterranei S699. Arch. Biochem. Biophys. 411 (2003) 277-288. [PMID: 12623077]
Accepted name: mitomycin 6-O-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + 6-demethylmitomycin A = S-adenosyl-L-homocysteine + mitomycin A
(2) S-adenosyl-L-methionine + 6-demethylmitomycin B = S-adenosyl-L-homocysteine + mitomycin B
Glossary: mitomycin A = [(1aS,8S,8aR,8bS)-5-methyl-6,8a-dimethoxy-4,7-dioxo-1,1a,2,4,7,8,8a,8b-octahydroazirino[2',3':3,4]pyrrolo[1,2-a]indol-8-yl]methyl carbamate
mitomycin B = [(1aS,8S,8aR,8bS)-8a-hydroxy-5-methyl-6-methoxy-4,7-dioxo-1,1a,2,4,7,8,8a,8b-octahydroazirino[2',3':3,4]pyrrolo[1,2-a]indol-8-yl]methyl carbamate
Other name(s): MmcR; mitomycin 7-O-methyltransferase (incorrect); S-adenosyl-L-methionine:7-demethylmitomycin-A 7-O-methyltransferase (incorrect)
Systematic name: S-adenosyl-L-methionine:6-demethylmitomycin-A 6-O-methyltransferase
Comments: The enzyme, characterized from the bacterium Streptomyces lavendulae, is involved in the biosynthesis of the quinone-containing antibiotics mitomycin A and mitomycin B.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Gruschow, S., Chang, L.C., Mao, Y. and Sherman, D.H. Hydroxyquinone O-methylation in mitomycin biosynthesis. J. Am. Chem. Soc. 129 (2007) 6470-6476. [PMID: 17461583]
2. Singh, S., Chang, A., Goff, R.D., Bingman, C.A., Gruschow, S., Sherman, D.H., Phillips, G.N., Jr. and Thorson, J.S. Structural characterization of the mitomycin 7-O-methyltransferase. Proteins 79 (2011) 2181-2188. [PMID: 21538548]
Accepted name: sphingolipid C9-methyltransferase
Reaction: S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide = S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide
Systematic name: S-adenosyl-L-methionine:(4E,8E)-sphinga-4,8-dienine ceramide C-methyltransferase
Comments: The enzyme, characterized from the fungi Komagataella pastoris and Fusarium graminearum, acts only on ceramides and has no activity with free sphingoid bases or glucosylceramides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Ternes, P., Sperling, P., Albrecht, S., Franke, S., Cregg, J.M., Warnecke, D. and Heinz, E. Identification of fungal sphingolipid C9-methyltransferases by phylogenetic profiling. J. Biol. Chem. 281 (2006) 5582-5592. [PMID: 16339149]
2. Ramamoorthy, V., Cahoon, E.B., Thokala, M., Kaur, J., Li, J. and Shah, D.M. Sphingolipid C-9 methyltransferases are important for growth and virulence but not for sensitivity to antifungal plant defensins in Fusarium graminearum. Eukaryot Cell 8 (2009) 217-229. [PMID: 19028992]
Accepted name: [trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase
Reaction: S-adenosyl-L-methionine + [trehalose-6-phosphate synthase]-L-cysteine = S-adenosyl-L-homocysteine + [trehalose-6-phosphate synthase]-S-methyl-L-cysteine
Systematic name: S-adenosyl-L-methionine:[trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase
Comments: The enzyme, characterized from the yeast Saccharomyces cerevisiae, enhances the activity of EC 2.4.1.15, trehalose-6-phosphate synthase, resulting in elevating the levels of trehalose in the cell and contributing to stationary phase survival. In vitro the enzyme performs S-methylation of L-cysteine residues of various protein substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sengupta, S., Banerjee, S., Lahiri, S., Dutta, T., Dhar, T.K. and Ghosh, A.K. Purification, characterization, sequencing and molecular cloning of a novel cysteine methyltransferase that regulates trehalose-6-phosphate synthase from Saccharomyces cerevisiae. Biochim. Biophys. Acta 1840 (2014) 1861-1871. [PMID: 24412193]
Accepted name: type I protein arginine methyltransferase
Reaction: 2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-Nω,Nω-dimethyl-L-arginine (overall reaction)
(1a) S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nω-methyl-L-arginine
(1b) S-adenosyl-L-methionine + [protein]-Nω-methyl-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nω,Nω-dimethyl-L-arginine
Other name(s): PRMT1 (gene name); PRMT2 (gene name); PRMT3 (gene name); PRMT4 (gene name); PRMT6 (gene name); PRMT8 (gene name); RMT1 (gene name); CARM1 (gene name)
Systematic name: S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nω,Nω-dimethyl-L-arginine-forming)
Comments: This eukaryotic enzyme catalyses the sequential dimethylation of one of the terminal guanidino nitrogen atoms in arginine residues, resulting in formation of asymmetric dimethylarginine residues. Some forms (e.g. PRMT1) have a very wide substrate specificity, while others (e.g. PRMT4 and PRMT6) are rather specific. The enzyme has a preference for methylating arginine residues that are flanked by one or more glycine residues [1]. PRMT1 is responsible for the bulk (about 85%) of total protein arginine methylation activity in mammalian cells [2]. cf. EC 2.1.1.320, type II protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Gary, J.D. and Clarke, S. RNA and protein interactions modulated by protein arginine methylation. Prog. Nucleic Acid Res. Mol. Biol. 61 (1998) 65-131. [PMID: 9752719]
2. Tang, J., Gary, J.D., Clarke, S. and Herschman, H.R. PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. J. Biol. Chem. 273 (1998) 16935-16945. [PMID: 9642256]
3. Tang, J., Frankel, A., Cook, R.J., Kim, S., Paik, W.K., Williams, K.R., Clarke, S. and Herschman, H.R. PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells. J. Biol. Chem. 275 (2000) 7723-7730. [PMID: 10713084]
4. Frankel, A., Yadav, N., Lee, J., Branscombe, T.L., Clarke, S. and Bedford, M.T. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J. Biol. Chem. 277 (2002) 3537-3543. [PMID: 11724789]
Accepted name: type II protein arginine methyltransferase
Reaction: 2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-Nω,Nω'-dimethyl-L-arginine (overall reaction)
(1a) S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nω-methyl-L-arginine
(1b) S-adenosyl-L-methionine + [protein]-Nω-methyl-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nω,Nω'-dimethyl-L-arginine
Other name(s): PRMT5 (gene name); PRMT9 (gene name)
Systematic name: S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nω,Nω'-dimethyl-L-arginine-forming)
Comments: The enzyme catalyses the methylation of one of the terminal guanidino nitrogen atoms in arginine residues within proteins, forming monomethylarginine, followed by the methylation of the second terminal nitrogen atom to form a symmetrical dimethylarginine. The mammalian enzyme is active in both the nucleus and the cytoplasm, and plays a role in the assembly of snRNP core particles by methylating certain small nuclear ribonucleoproteins. cf. EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Branscombe, T.L., Frankel, A., Lee, J.H., Cook, J.R., Yang, Z., Pestka, S. and Clarke, S. PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins. J. Biol. Chem. 276 (2001) 32971-32976. [PMID: 11413150]
2. Wang, X., Zhang, Y., Ma, Q., Zhang, Z., Xue, Y., Bao, S. and Chong, K. SKB1-mediated symmetric dimethylation of histone H4R3 controls flowering time in Arabidopsis. EMBO J. 26 (2007) 1934-1941. [PMID: 17363895]
3. Lacroix, M., El Messaoudi, S., Rodier, G., Le Cam, A., Sardet, C. and Fabbrizio, E. The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5. EMBO Rep. 9 (2008) 452-458. [PMID: 18404153]
4. Chari, A., Golas, M.M., Klingenhager, M., Neuenkirchen, N., Sander, B., Englbrecht, C., Sickmann, A., Stark, H. and Fischer, U. An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs. Cell 135 (2008) 497-509. [PMID: 18984161]
5. Antonysamy, S., Bonday, Z., Campbell, R.M., Doyle, B., Druzina, Z., Gheyi, T., Han, B., Jungheim, L.N., Qian, Y., Rauch, C., Russell, M., Sauder, J.M., Wasserman, S.R., Weichert, K., Willard, F.S., Zhang, A. and Emtage, S. Crystal structure of the human PRMT5:MEP50 complex. Proc. Natl. Acad. Sci. USA 109 (2012) 17960-17965. [PMID: 23071334]
6. Hadjikyriacou, A., Yang, Y., Espejo, A., Bedford, M.T. and Clarke, S.G. Unique features of human protein arginine methyltransferase 9 (PRMT9) and its substrate RNA splicing factor SF3B2. J. Biol. Chem. 290 (2015) 16723-16743. [PMID: 25979344]
Accepted name: type III protein arginine methyltransferase
Reaction: S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nω-methyl-L-arginine
Other name(s): PRMT7 (gene name)
Systematic name: S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nω-methyl-L-arginine-forming)
Comments: Type III protein arginine methyltransferases catalyse the single methylation of one of the terminal nitrogen atoms of the guanidino group in an L-arginine residue within a protein. Unlike type I and type II protein arginine methyltransferases, which also catalyse this reaction, type III enzymes do not methylate the substrate any further. cf. EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.320, type II protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Miranda, T.B., Miranda, M., Frankel, A. and Clarke, S. PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity. J. Biol. Chem. 279 (2004) 22902-22907. [PMID: 15044439]
2. Gonsalvez, G.B., Tian, L., Ospina, J.K., Boisvert, F.M., Lamond, A.I. and Matera, A.G. Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins. J. Cell Biol. 178 (2007) 733-740. [PMID: 17709427]
3. Feng, Y., Hadjikyriacou, A. and Clarke, S.G. Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): the importance of acidic residues in the double E loop. J. Biol. Chem. 289 (2014) 32604-32616. [PMID: 25294873]
Accepted name: type IV protein arginine methyltransferase
Reaction: S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-N5-methyl-L-arginine
Other name(s): RMT2 (gene name)
Systematic name: S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-N5-methyl-L-arginine-forming)
Comments: This enzyme, characterized from the yeast Saccharomyces cerevisiae, methylates the the δ-nitrogen atom of arginine residues within proteins. Among its substrates are Arg67 of the ribosomal protein L12. cf. EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.320, type II protein arginine methyltransferase, and EC 2.1.1.321, type III protein arginine methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Niewmierzycka, A. and Clarke, S. S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase. J. Biol. Chem. 274 (1999) 814-824. [PMID: 9873020]
2. Chern, M.K., Chang, K.N., Liu, L.F., Tam, T.C., Liu, Y.C., Liang, Y.L. and Tam, M.F. Yeast ribosomal protein L12 is a substrate of protein-arginine methyltransferase 2. J. Biol. Chem. 277 (2002) 15345-15353. [PMID: 11856739]
3. Olsson, I., Berrez, J.M., Leipus, A., Ostlund, C. and Mutvei, A. The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup100. Exp Cell Res 313 (2007) 1778-1789. [PMID: 17448464]
Accepted name:(–)-pluviatolide 4-O-methyltransferase
Reaction: S-adenosyl-L-methionine + (–)-pluviatolide = S-adenosyl-L-homocysteine + (–)-bursehernin
For diagram of reaction click here.
Glossary:(–)-pluviatolide = (3R,4R)-4-(2H-1,3-benzodioxol-5-ylmethyl)-3-[(4-hydroxy-3-methoxyphenyl)methyl]oxolan-2-one
(–)-bursehernin = (3R,4R)-4-(2H-1,3-benzodioxol-5-ylmethyl)-3-[(3,4-dimethoxyphenyl)methyl]oxolan-2-one
Other name(s): OMT3 (gene name)
Systematic name: S-adenosyl-L-methionine:(–)-pluviatolide 4-O-methyltransferase
Comments: The enzyme, characterized from the plant Sinopodophyllum hexandrum, is involved in the biosynthetic pathway of podophyllotoxin, a non-alkaloid toxin lignan whose derivatives are important anticancer drugs.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Lau, W. and Sattely, E.S. Six enzymes from mayapple that complete the biosynthetic pathway to the etoposide aglycone. Science 349 (2015) 1224-1228. [PMID: 26359402]
Accepted name: dTDP-4-amino-2,3,4,6-tetradeoxy-D-glucose N,N-dimethyltransferase
Reaction: 2 S-adenosyl-L-methionine + dTDP-4-amino-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose = 2 S-adenosyl-L-homocysteine + dTDP-α-D-forosamine (overall reaction)
(1a) S-adenosyl-L-methionine + dTDP-4-amino-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose = S-adenosyl-L-homocysteine + dTDP-4-(methylamino)-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose
(1b) S-adenosyl-L-methionine + dTDP-4-(methylamino)-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose = 2 S-adenosyl-L-homocysteine + dTDP-α-D-forosamine
For diagram of reaction click here.
Glossary: dTDP-α-D-forosamine = dTDP-4-(dimethylamino)-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose
Other name(s): SpnS; TDP-4-amino-2,3,6-trideoxy-D-glucose N,N-dimethyltransferase
Systematic name: S-adenosyl-L-methionine:dTDP-4-amino-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose N,N-dimethyltransferase
Comments: The enzyme was isolated from the bacterium Saccharopolyspora spinosa, where it is involved in the biosynthesis of spinosyn A, an active ingredient of several commercial insecticides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Hong, L., Zhao, Z., Melancon, C.E., 3rd, Zhang, H. and Liu, H.W. In vitro characterization of the enzymes involved in TDP-D-forosamine biosynthesis in the spinosyn pathway of Saccharopolyspora spinosa, J. Am. Chem. Soc. 130 (2008) 4954-4967. [PMID: 18345667]
Accepted name: juvenile hormone-III synthase
Reaction: (1) S-adenosyl-L-methionine + (2E,6E)-farnesoate = S-adenosyl-L-homocysteine + methyl (2E,6E)-farnesoate
(2) S-adenosyl-L-methionine + juvenile hormone III acid = S-adenosyl-L-homocysteine + juvenile hormone III
Glossary: juvenile hormone III = methyl (2E,6E,10R)-10,11-epoxy-3,7,11-trimethyldodeca-2,6-dienoate
juvenile hormone III acid = (2E,6E,10R)-10,11-epoxy-3,7,11-trimethyldodeca-2,6-dienoate
Other name(s): farnesoic acid methyltransferase; juvenile hormone acid methyltransferase; JHAMT
Systematic name: S-adenosyl-L-methionine:(2E,6E)-farnesoate O-methyltransferase
Comments: The enzyme, found in insects, is involved in the synthesis of juvenile hormone III, a sesquiterpenoid that regulates several processes including embryonic development, metamorphosis, and reproduction, in many insect species.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Shinoda, T. and Itoyama, K. Juvenile hormone acid methyltransferase: a key regulatory enzyme for insect metamorphosis. Proc. Natl. Acad. Sci. USA 100 (2003) 11986-11991. [PMID: 14530389]
2. Defelipe, L.A., Dolghih, E., Roitberg, A.E., Nouzova, M., Mayoral, J.G., Noriega, F.G. and Turjanski, A.G. Juvenile hormone synthesis: "esterify then epoxidize" or "epoxidize then esterify"? Insights from the structural characterization of juvenile hormone acid methyltransferase. Insect Biochem. Mol. Biol. 41 (2011) 228-235. [PMID: 21195763]
3. Van Ekert, E., Heylen, K., Rouge, P., Powell, C.A., Shatters, R.G., Jr., Smagghe, G. and Borovsky, D. Aedes aegypti juvenile hormone acid methyl transferase, the ultimate enzyme in the biosynthetic pathway of juvenile hormone III, exhibits substrate control. J. Insect Physiol. 64 (2014) 62-73. [PMID: 24657668]
4. Van Ekert, E., Shatters, R.G., Jr., Rouge, P., Powell, C.A., Smagghe, G. and Borovsky, D. Cloning and expressing a highly functional and substrate specific farnesoic acid o-methyltransferase from the Asian citrus psyllid (Diaphorina citri Kuwayama). FEBS Open Bio 5 (2015) 264-275. [PMID: 25893162]
Accepted name: N-acetyl-demethylphosphinothricin P-methyltransferase
Reaction: 2 S-adenosyl-L-methionine + N-acetyl-demethylphosphinothricin + reduced acceptor = S-adenosyl-L-homocysteine + 5'-deoxyadenosine + L-methionine + N-acetyl-phosphinothricin + oxidized acceptor
Glossary: N-acetyl-demethylphosphinothricin = (2S)-2-acetamido-4-phosphinatobutanoate
Other name(s): phpK (gene name); bcpD (gene name); P-methylase
Systematic name: S-adenosyl-L-methionine:N-acetyl-demethylphosphinothricin P-methyltransferase
Comments: The enzyme was originally characterized from bacteria that produce the tripeptides bialaphos and phosalacine, which inhibit plant and bacterial glutamine synthetases. It is a radical S-adenosyl-L-methionine (SAM) enzyme that contains a [4Fe-4S] center and a methylcob(III)alamin cofactor. According to the proposed mechanism, the reduced iron-sulfur center donates an electron to SAM, resulting in homolytic cleavage of the carbon-sulfur bond to form a 5'-deoxyadenosyl radical that abstracts the hydrogen atom from the P-H bond of the substrate, forming a phosphinate-centered radical. This radical reacts with methylcob(III)alamin to produce the methylated product and cob(II)alamin, which is reduced by an unknown donor to cob(I)alamin. A potential route for restoring the latter back to methylcob(III)alamin is a nucleophilic attack on a second SAM molecule. The enzyme acts in vivo on N-acetyl-demethylphosphinothricin-L-alanyl-L-alanine or N-acetyl-demethylphosphinothricin-L-alanyl-L-leucine, the intermediates in the biosynthesis of bialaphos and phosalacine, respectively. This transformation produces the only example of a carbon-phosphorus-carbon linkage known to occur in nature.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Kamigiri, K., Hidaka, T., Imai, S., Murakami, T. and Seto, H. Studies on the biosynthesis of bialaphos (SF-1293) 12. C-P bond formation mechanism of bialaphos: discovery of a P-methylation enzyme. J. Antibiot. (Tokyo) 45 (1992) 781-787. [PMID: 1624380]
2. Hidaka, T., Hidaka, M., Kuzuyama, T. and Seto, H. Sequence of a P-methyltransferase-encoding gene isolated from a bialaphos-producing Streptomyces hygroscopicus. Gene 158 (1995) 149-150. [PMID: 7789803]
3. Werner, W.J., Allen, K.D., Hu, K., Helms, G.L., Chen, B.S. and Wang, S.C. In vitro phosphinate methylation by PhpK from Kitasatospora phosalacinea. Biochemistry 50 (2011) 8986-8988. [PMID: 21950770]
4. Allen, K.D. and Wang, S.C. Spectroscopic characterization and mechanistic investigation of P-methyl transfer by a radical SAM enzyme from the marine bacterium Shewanella denitrificans OS217. Biochim. Biophys. Acta 1844 (2014) 2135-2144. [PMID: 25224746]
5. Hu, K., Werner, W.J., Allen, K.D. and Wang, S.C. Investigation of enzymatic C-P bond formation using multiple quantum HCP nuclear magnetic resonance spectroscopy. Magn. Reson. Chem. 53 (2015) 267-272. [PMID: 25594737]
Accepted name: phenazine-1-carboxylate N-methyltransferase
Reaction: S-adenosyl-L-methionine + phenazine-1-carboxylate = S-adenosyl-L-homocysteine + 5-methyl-phenazine-1-carboxylate
For diagram of reaction click here.
Other name(s): phzM (gene name)
Systematic name: S-adenosyl-L-methionine:phenazine-1-carboxylate 5-N-methyltransferase
Comments: The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is involved in the biosynthesis of pyocyanin, a toxin produced and secreted by the organism. The enzyme is active in vitro only in the presence of EC 1.14.13.218, 5-methylphenazine-1-carboxylate 1-monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Parsons, J.F., Greenhagen, B.T., Shi, K., Calabrese, K., Robinson, H. and Ladner, J.E. Structural and functional analysis of the pyocyanin biosynthetic protein PhzM from Pseudomonas aeruginosa. Biochemistry 46 (2007) 1821-1828. [PMID: 17253782]
Accepted name: N-demethylindolmycin N-methyltransferase
Reaction: S-adenosyl-L-methionine + N-demethylindolmycin = S-adenosyl-L-homocysteine + indolmycin
Glossary: indolmycin = (5S)-5-[(1R)-1-(indol-3-yl)ethyl]-2-(methylamino)-1,3-oxazolin-4(5H)-one
Other name(s): ind7 (gene name)
Systematic name: S-adenosyl-L-methionine:N-demethylindolmycin N-methyltransferase
Comments: The enzyme, characterized from the bacterium Streptomyces griseus, catalyses the ultimate reaction in the biosynthesis of indolmycin, an antibacterial drug that inhibits the bacterial tryptophan—tRNA ligase (EC 6.1.1.2).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Du, Y.L., Alkhalaf, L.M. and Ryan, K.S. In vitro reconstitution of indolmycin biosynthesis reveals the molecular basis of oxazolinone assembly. Proc. Natl. Acad. Sci. USA 112 (2015) 2717-2722. [PMID: 25730866]
Accepted name: demethylphylloquinol methyltransferase
Reaction: S-adenosyl-L-methionine + demethylphylloquinol = S-adenosyl-L-homocysteine + phylloquinol
For diagram of reaction click here.
Glossary: demethylphylloquinol = 2-phytyl-1,4-naphthoquinol
phylloquinol = 2-methyl-3-phytyl-1,4-naphthoquinol = vitamin K1
Other name(s): menG (gene name); 2-phytyl-1,4-naphthoquinol methyltransferase
Systematic name: S-adenosyl-L-methionine:2-phytyl-1,4-naphthoquinol C-methyltransferase
Comments: The enzyme, found in plants and cyanobacteria, catalyses the final step in the biosynthesis of phylloquinone (vitamin K1), an electron carrier associated with photosystem I. The enzyme is specific for the quinol form of the substrate, and does not act on the quinone form [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Sakuragi, Y., Zybailov, B., Shen, G., Jones, A.D., Chitnis, P.R., van der Est, A., Bittl, R., Zech, S., Stehlik, D., Golbeck, J.H. and Bryant, D.A. Insertional inactivation of the menG gene, encoding 2-phytyl-1,4-naphthoquinone methyltransferase of Synechocystis sp. PCC 6803, results in the incorporation of 2-phytyl-1,4-naphthoquinone into the A1 site and alteration of the equilibrium constant between A1 and F(X) in photosystem I. Biochemistry 41 (2002) 394-405. [PMID: 11772039]
2. Lohmann, A., Schottler, M.A., Brehelin, C., Kessler, F., Bock, R., Cahoon, E.B. and Dormann, P. Deficiency in phylloquinone (vitamin K1) methylation affects prenyl quinone distribution, photosystem I abundance, and anthocyanin accumulation in the Arabidopsis AtmenG mutant. J. Biol. Chem. 281 (2006) 40461-40472. [PMID: 17082184]
3. Fatihi, A., Latimer, S., Schmollinger, S., Block, A., Dussault, P.H., Vermaas, W.F., Merchant, S.S. and Basset, G.J. A dedicated type II NADPH dehydrogenase performs the penultimate step in the biosynthesis of vitamin K1 in Synechocystis and Arabidopsis. Plant Cell 27 (2015) 1730-1741. [PMID: 26023160]
Accepted name: 5'-demethylyatein 5'-O-methyltransferase
Reaction: S-adenosyl-L-methionine + (–)-5'-demethylyatein = S-adenosyl-L-homocysteine + (-)-yatein
For diagram of reaction click here.
Glossary: (–)-5'-demethylyatein = (3R,4R)-4-(2,3-benzodioxol-5-ylmethyl)-3-(3-hydroxy-4,5-dimethoxybenzyl)dihydrofuran-2(3H)-one
(–)-yatein = (3R,4R)-4-(1,3-benzodioxol-5-ylmethyl)-3-(3,4,5-trimethoxybenzyl)dihydrofuran-2(3H)-one
Other name(s): OMT1 (gene name)
Systematic name: S-adenosyl-L-methionine:(–)-5'-demethylyatein 5'-O-methyltransferase
Comments: The enzyme, characterized from the plant Sinopodophyllum hexandrum, is involved in the biosynthetic pathway of podophyllotoxin, a non-alkaloid toxin lignan whose derivatives are important anticancer drugs.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Lau, W. and Sattely, E.S. Six enzymes from mayapple that complete the biosynthetic pathway to the etoposide aglycone. Science 349 (2015) 1224-1228. [PMID: 26359402]
Accepted name: bacteriochlorophyllide d C-121-methyltransferase
Reaction: S-adenosyl-L-methionine + 8-ethyl-12-methyl-3-vinylbacteriochlorophyllide d = S-adenosyl-L-homocysteine + 8,12-diethyl-3-vinylbacteriochlorophyllide d
For diagram of reaction click here.
Other name(s): bchR (gene name)
Systematic name: S-adenosyl-L-methionine:8-ethyl-12-methyl-3-vinylbacteriochlorophyllide-d C-121-methyltransferase
Comments: This enzyme, found in green sulfur bacteria (Chlorobiaceae) and green flimentous bacteria (Chloroflexaceae), is a radical S-adenosyl-L-methionine (AdoMet) enzyme and contains a [4Fe-4S] cluster. It adds a methyl group at the C-121 position of bacteriochlorophylls of the c, d and e types. This methylation plays a role in fine-tuning the structural arrangement of the bacteriochlorophyll aggregates in chlorosomes and therefore directly influences the chlorosomes absorption properties.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Gomez Maqueo Chew, A., Frigaard, N.U. and Bryant, D.A. Bacteriochlorophyllide c C-82 and C-121 methyltransferases are essential for adaptation to low light in Chlorobaculum tepidum. J. Bacteriol. 189 (2007) 6176-6184. [PMID: 17586634]
Accepted name: bacteriochlorophyllide d C-82-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + 8,12-diethyl-3-vinylbacteriochlorophyllide d = S-adenosyl-L-homocysteine + 12-ethyl-8-propyl-3-vinylbacteriochlorophyllide d
(2) S-adenosyl-L-methionine + 12-ethyl-8-propyl-3-vinylbacteriochlorophyllide d = S-adenosyl-L-homocysteine + 12-ethyl-8-isobutyl-3-vinylbacteriochlorophyllide d
For diagram of reaction click here.
Other name(s): bchQ (gene name)
Systematic name: S-adenosyl-L-methionine:8,12-diethyl-3-vinylbacteriochlorophyllide-d C-82-methyltransferase
Comments: This enzyme, found in green sulfur bacteria (Chlorobiaceae) and green flimentous bacteria (Chloroflexaceae), is a radical S-adenosyl-L-methionine (AdoMet) enzyme and contains a [4Fe-4S] cluster. It adds one or two methyl groups at the C-82 position of bacteriochlorophylls of the c, d and e types. These methylations play a role in fine-tuning the structural arrangement of the bacteriochlorophyll aggregates in chlorosomes and therefore directly influence chlorosomal absorption properties.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Gomez Maqueo Chew, A., Frigaard, N.U. and Bryant, D.A. Bacteriochlorophyllide c C-82 and C-121 methyltransferases are essential for adaptation to low light in Chlorobaculum tepidum. J. Bacteriol. 189 (2007) 6176-6184. [PMID: 17586634]
Accepted name: bacteriochlorophyllide d C-20 methyltransferase
Reaction: S-adenosyl-L-methionine + a bacteriochlorophyllide d = S-adenosyl-L-homocysteine + a bacteriochlorophyllide c
For diagram of reaction click here.
Other name(s): bchU (gene name)
Systematic name: S-adenosyl-L-methionine:bacteriochlorophyllide-d C-20 methyltransferase
Comments: The enzyme, found in green sulfur bacteria (Chlorobiaceae) and green flimentous bacteria (Chloroflexaceae), catalyses the methylation of the C-20 methine bridge position in bacteriochlorophyllide d, forming bacteriochlorophyllide c.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Maresca, J.A., Gomez Maqueo Chew, A., Ponsati, M.R., Frigaard, N.U., Ormerod, J.G. and Bryant, D.A. The bchU gene of Chlorobium tepidum encodes the c-20 methyltransferase in bacteriochlorophyll c biosynthesis. J. Bacteriol. 186 (2004) 2558-2566. [PMID: 15090495]
Accepted name: methanethiol S-methyltransferase
Reaction: S-adenosyl-L-methionine + methanethiol = S-adenosyl-L-homocysteine + dimethyl sulfide
Other name(s): mddA (gene name)
Systematic name: S-adenosyl-L-methionine:methanethiol S-methyltransferase
Comments: The enzyme, found in many bacterial taxa, is involved in a pathway that converts L-methionine to dimethyl sulfide.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Carrion, O., Curson, A.R., Kumaresan, D., Fu, Y., Lang, A.S., Mercade, E. and Todd, J.D. A novel pathway producing dimethylsulphide in bacteria is widespread in soil environments. Nat Commun 6 (2015) 6579. [PMID: 25807229]
Accepted name: 4-amino-anhydrotetracycline N4-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + 4-amino-4-de(dimethylamino)anhydrotetracycline = S-adenosyl-L-homocysteine + 4-methylamino-4-de(dimethylamino)anhydrotetracycline
(2) S-adenosyl-L-methionine + 4-methylamino-4-de(dimethylamino)anhydrotetracycline = S-adenosyl-L-homocysteine + anhydrotetracycline
For diagram of reaction click here.
Glossary: 4-amino-4-de(dimethylamino)anhydrotetracycline = (4S,4aS,12aS)-4-amino-3,10,11,12a-tetrahydroxy-6-methyl-1,12-dioxo-4a,5-dihydro-4H-tetracene-2-carboxamide
4-methylamino-4-de(dimethylamino)anhydrotetracycline = (4S,4aS,12aS)-3,10,11,12a-tetrahydroxy-6-methyl-4-(methylamino)-1,12-dioxo-4a,5-dihydro-4H-tetracene-2-carboxamide
anhydrotetracycline = (4S,4aS,12aS)-4-(dimethylamino)-3,10,11,12a-tetrahydroxy-6-methyl-1,12-dioxo-1,4,4a,5,12,12a-hexahydrotetracene-2-carboxamide
Other name(s): oxyT (gene name); ctcO (gene name)
Systematic name: S-adenosyl-L-methionine:(4S,4aS,12aS)-4-amino-3,10,11,12a-tetrahydroxy-6-methyl-1,12-dioxo-4a,5-dihydro-4H-tetracene-2-carboxamide Nα-methyltransferase
Comments: The enzyme, characterized from the bacterium Streptomyces rimosus, participates in the biosynthesis of tetracycline antibiotics.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Zhang, W., Watanabe, K., Cai, X., Jung, M.E., Tang, Y. and Zhan, J. Identifying the minimal enzymes required for anhydrotetracycline biosynthesis. J. Am. Chem. Soc. 130 (2008) 6068-6069. [PMID: 18422316]
Accepted name: norbelladine O-methyltransferase
Reaction: S-adenosyl-L-methionine + norbelladine = S-adenosyl-L-homocysteine + 4'-O-methylnorbelladine
For diagram of reaction click here.
Glossary: norbelladine = 4-({[2-(4-hydroxyphenyl)ethyl]amino}methyl)benzene-1,2-diol
4'-O-methylnorbelladine = 5-({[2-(4-hydroxyphenyl)ethyl]amino}methyl)-2-methoxyphenol
Other name(s): N4OMT1 (gene name)
Systematic name: S-adenosyl-L-methionine:norbelladine O-methyltransferase
Comments: The enzyme, characterized from the plants Nerine bowdenii and Narcissus pseudonarcissus (daffodil), participates in the biosynthesis of alkaloids produced by plants that belong to the Amaryllidaceae family.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Mann, J.D., Fales, H.M. and Mudd, S.H. Alkaloids and plant metabolism. VI. O-methylation in vitro of norbelladine, a precursor of Amaryllidaceae alkaloids. J. Biol. Chem. 238 (1963) 3820-3823. [PMID: 14109227]
2. Kilgore, M.B., Augustin, M.M., Starks, C.M., O'Neil-Johnson, M., May, G.D., Crow, J.A. and Kutchan, T.M. Cloning and characterization of a norbelladine 4'-O-methyltransferase involved in the biosynthesis of the Alzheimer’s drug galanthamine in Narcissus sp. aff. pseudonarcissus. PLoS One 9 (2014) e103223. [PMID: 25061748]
Accepted name: reticuline N-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + (S)-reticuline = S-adenosyl-L-homocysteine + (S)-tembetarine
(2) S-adenosyl-L-methionine + (S)-corytuberine = S-adenosyl-L-homocysteine + magnoflorine
For diagram of reaction click here or click here
Glossary: (S)-reticuline = (1S)-1-(3-hydroxy-4-methoxybenzyl)-6-methoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-7-ol
(S)-tembetarine = (1S)-1-(3-hydroxy-4-methoxybenzyl)-6-methoxy-2,2-dimethyl-1,2,3,4-tetrahydroisoquinolin-7-ol
(S)-corytuberine = (6aS)-2,10-dimethoxy-6-methyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-1,11-diol
(S)-magnoflorine = (6aS)-1,11-dihydroxy-2,10-dimethoxy-6,6-dimethyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinolinium
Other name(s): RNMT
Systematic name: S-adenosyl-L-methionine:(S)-reticuline N-methyltransferase
Comments: The enzyme from opium poppy (Papaver somniferum) can also methylate (R)-reticuline, tetrahydropapaverine, (S)-glaucine and (S)-bulbocapnine. It is involved in the biosynthesis of the quaternary benzylisoquinoline alkaloid magnoflorine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Morris, J.S. and Facchini, P.J. Isolation and characterization of reticuline N-methyltransferase involved in biosynthesis of the aporphine alkaloid magnoflorine in opium poppy. J. Biol. Chem. 291 (2016) 23416-23427. [PMID: 27634038]
Accepted name: desmethylxanthohumol 6'-O-methyltransferase
Reaction: S-adenosyl-L-methionine + desmethylxanthohumol = S-adenosyl-L-homocysteine + xanthohumol
For diagram of reaction click here.
Glossary: desmethylxanthohumol = 2′,4,4′,6′-tetrahydroxy-3-prenylchalcone = (2E)-3-(4-hydroxyphenyl)-1-[2,4,6-trihydroxy-3-(3-methylbut-2-en-1-yl)phenyl]prop-2-en-1-one
xanthohumol = (2E)-1-[2,4-dihydroxy-6-methoxy-3-(3-methylbut-2-en-1-yl)phenyl]-3-(4-hydroxyphenyl)prop-2-en-1-one
Other name(s): OMT1 (ambiguous)
Systematic name: S-adenosyl-L-methionine:desmethylxanthohumol 6'-O-methyltransferase
Comments: Found in hops (Humulus lupulus). The enzyme can also methylate xanthogalenol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Nagel, J., Culley, L.K., Lu, Y., Liu, E., Matthews, P.D., Stevens, J.F. and Page, J.E. EST analysis of hop glandular trichomes identifies an O-methyltransferase that catalyzes the biosynthesis of xanthohumol. Plant Cell 20 (2008) 186-200. [PMID: 18223037]
Accepted name: xanthohumol 4-O-methyltransferase
Reaction: S-adenosyl-L-methionine + xanthohumol = S-adenosyl-L-homocysteine + 4-O-methylxanthohumol
For diagram of reaction click here
Glossary: xanthohumol = 2',4,4'-trihydroxy-6'-methoxy-3-prenylchalcone = (2E)-1-[2,4-dihydroxy-6-methoxy-3-(3-methylbut-2-en-1-yl)phenyl]-3-(4-hydroxyphenyl)prop-2-en-1-one
4-O-methylxanthohumol =2',4'-dihydroxy-4,6'-dimethoxy-3-prenylchalcone = (2E)-1-[2,4-dihydroxy-6-methoxy-3-(3-methylbut-2-en-1-yl)phenyl]-3-(4-methoxyphenyl)prop-2-en-1-one
Other name(s): OMT2 (ambiguous); S-adenosyl-L-methionine:xanthohumol 4'-O-methyltransferase (incorrect); xanthohumol 4'-O-methyltransferase (incorrect)
Systematic name: S-adenosyl-L-methionine:xanthohumol 4-O-methyltransferase
Comments: The enzyme from hops (Humulus lupulus) has a broad substrate specificity. The best substrates in vitro are resveratrol, desmethylxanthohumol, naringenin chalcone and isoliquiritigenin.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:
References:
1. Nagel, J., Culley, L.K., Lu, Y., Liu, E., Matthews, P.D., Stevens, J.F. and Page, J.E. EST analysis of hop glandular trichomes identifies an O-methyltransferase that catalyzes the biosynthesis of xanthohumol. Plant Cell 20 (2008) 186-200. [PMID: 18223037]
Accepted name: 3-aminomethylindole N-methyltransferase
Reaction: 2 S-adenosyl-L-methionine + 3-(aminomethyl)indole = 2 S-adenosyl-L-homocysteine + gramine (overall reaction)
(1a) S-adenosyl-L-methionine + 3-(aminomethyl)indole = S-adenosyl-L-homocysteine + (1H-indol-3-yl)-N-methylmethanamine
(1b) S-adenosyl-L-methionine + (1H-indol-3-yl)-N-methylmethanamine = S-adenosyl-L-homocysteine + gramine
For diagram of reaction click here.
Glossary: 3-(aminomethyl)indole = (1H-indol-3-yl)methanamine
gramine = (1H-indol-3-ylmethyl)dimethylamine = (1H-indol-3-yl)-N,N-dimethylmethanamine
Other name(s): NMT (gene name)
Systematic name: S-adenosyl-L-methionine:3-(aminomethyl)indole N-methyltransferase (gramine-forming)
Comments: The enzyme, characterized from Hordeum vulgare (barley), catalyses two successive N-methylation reactions during the biosynthesis of gramine, a toxic indole alkaloid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Leland, T.J. and Hanson, A.D. Induction of a specific N-methyltransferase enzyme by long-term heat stress during barley leaf growth. Plant Physiol. 79 (1985) 451-457. [PMID: 16664431]
2. Larsson, K.A., Zetterlund, I., Delp, G. and Jonsson, L.M. N-Methyltransferase involved in gramine biosynthesis in barley: cloning and characterization. Phytochemistry 67 (2006) 2002-2008. [PMID: 16930646]
Accepted name: vanillate/3-O-methylgallate O-demethylase
Reaction: (1) vanillate + tetrahydrofolate = protocatechuate + 5-methyltetrahydrofolate
(2) 3-O-methylgallate + tetrahydrofolate = gallate + 5-methyltetrahydrofolate
Glossary: protocatechuate = 3,4-dihydroxybenzoate
vanillate = 4-hydroxy-3-methoxybenzoate
gallate = 3,4,5-trihydroxybenzoate
Other name(s): ligM (gene name)
Systematic name: vanillate:tetrahydrofolate O-methyltransferase
Comments: The enzyme, characterized from the bacterium Sphingomonas sp. SYK6, is involved in the degradation of lignin. The enzyme has similar activities with vanillate and 3-O-methylgallate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Nishikawa, S., Sonoki, T., Kasahara, T., Obi, T., Kubota, S., Kawai, S., Morohoshi, N. and Katayama, Y. Cloning and sequencing of the Sphingomonas (Pseudomonas) paucimobilis gene essential for the O demethylation of vanillate and syringate. Appl. Environ. Microbiol. 64 (1998) 836-842. [PMID: 9501423]
2. Masai, E., Sasaki, M., Minakawa, Y., Abe, T., Sonoki, T., Miyauchi, K., Katayama, Y. and Fukuda, M. A novel tetrahydrofolate-dependent O-demethylase gene is essential for growth of Sphingomonas paucimobilis SYK-6 with syringate. J. Bacteriol. 186 (2004) 2757-2765. [PMID: 15090517]
3. Abe, T., Masai, E., Miyauchi, K., Katayama, Y. and Fukuda, M. A tetrahydrofolate-dependent O-demethylase, LigM, is crucial for catabolism of vanillate and syringate in Sphingomonas paucimobilis SYK-6. J. Bacteriol. 187 (2005) 2030-2037. [PMID: 15743951]
Accepted name: anaerobilin synthase
Reaction: 2 S-adenosyl-L-methionine + protoheme + 2 reduced flavodoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + anaerobilin + Fe2+ + 2 oxidized flavodoxin
For diagram of reaction click here.
Glossary: anaerobilin = (4Z,10Z,14E)-8,12-bis(2-carboxyethyl)-3,7,13,18-tetramethyl-1,2,17-trivinyl-23,24-dihydrobilin
Other name(s): chuW (gene name)
Systematic name: S-adenosyl-L-methionine:protoheme C-methyltransferase (anaerobilin-producing)
Comments: The enzyme, studied from the bacterium Escherichia coli O157:H7, is a radical SAM (AdoMet) enzyme that is involved in heme degradation and iron utilization under anaerobic conditions. The enzyme uses two SAM molecules for the reaction. The first molecule is used to generate a 5'-deoxyadenosyl radical, which abstracts a hydrogen atom from the methyl group of the second SAM molecule. The newly formed methylene radical attacks the substrate, causing a rearrangement of the porphyrin ring that results in the liberation of iron.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. LaMattina, J.W., Nix, D.B. and Lanzilotta, W.N. Radical new paradigm for heme degradation in Escherichia coli O157:H7. Proc. Natl. Acad. Sci. USA 113 (2016) 12138-12143. [PMID: 27791000]
2. LaMattina, J.W., Delrossi, M., Uy, K.G., Keul, N.D., Nix, D.B., Neelam, A.R. and Lanzilotta, W.N. Anaerobic heme degradation: ChuY Is an anaerobilin reductase that exhibits kinetic cooperativity. Biochemistry 56 (2017) 845-855. [PMID: 28045510]
Accepted name: 8-amino-8-demethylriboflavin N,N-dimethyltransferase
Reaction: 2 S-adenosyl-L-methionine + 8-amino-8-demethylriboflavin = 2 S-adenosyl-L-homocysteine + roseoflavin (overall reaction)
(1a) S-adenosyl-L-methionine + 8-amino-8-demethylriboflavin = S-adenosyl-L-homocysteine + 8-demethyl-8-(methylamino)riboflavin
(1b) S-adenosyl-L-methionine + 8-demethyl-8-(methylamino)riboflavin = S-adenosyl-L-homocysteine + roseoflavin
Glossary: roseoflavin = 8-demethyl-8-(dimethylamino)riboflavin
Other name(s): rosA (gene name)
Systematic name: S-adenosyl-L-methionine:8-amino-8-demethylriboflavin N,N-dimethyltransferase
Comments: The enzyme, characterized from the soil bacterium Streptomyces davawensis, catalyses the last two steps in the biosynthesis of the antibiotic roseoflavin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Jankowitsch, F., Kuhm, C., Kellner, R., Kalinowski, J., Pelzer, S., Macheroux, P. and Mack, M. A novel N,N-8-amino-8-demethyl-D-riboflavin dimethyltransferase (RosA) catalyzing the two terminal steps of roseoflavin biosynthesis in Streptomyces davawensis. J. Biol. Chem. 286 (2011) 38275-38285. [PMID: 21911488]
2. Tongsook, C., Uhl, M.K., Jankowitsch, F., Mack, M., Gruber, K. and Macheroux, P. Structural and kinetic studies on RosA, the enzyme catalysing the methylation of 8-demethyl-8-amino-D-riboflavin to the antibiotic roseoflavin. FEBS J. 283 (2016) 1531-1549. [PMID: 26913589]
Accepted name: ornithine lipid N-methyltransferase
Reaction: 3 S-adenosyl-L-methionine + an ornithine lipid = 3 S-adenosyl-L-homocysteine + an N,N,N-trimethylornithine lipid (overall reaction)
(1a) S-adenosyl-L-methionine + an ornithine lipid = S-adenosyl-L-homocysteine + an N-methylornithine lipid
(1b) S-adenosyl-L-methionine + an N-methylornithine lipid = S-adenosyl-L-homocysteine + an N,N-dimethylornithine lipid
(1c) S-adenosyl-L-methionine + an N,N-dimethylornithine lipid = S-adenosyl-L-homocysteine + an N,N,N-trimethylornithine lipid
Glossary: an ornithine lipid = an Nα-[(3R)-3-(acyloxy)acyl]-L-ornithine
Other name(s): olsG (gene name)
Systematic name: S-adenosyl-L-methionine:ornithine lipid N-methyltransferase
Comments: The enzyme, characterized from the bacterium Singulisphaera acidiphila, catalyses three successive methylations of the terminal δ-nitrogen in ornithine lipids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Escobedo-Hinojosa, W.I., Vences-Guzman, M.A., Schubotz, F., Sandoval-Calderon, M., Summons, R.E., Lopez-Lara, I.M., Geiger, O. and Sohlenkamp, C. OlsG (Sinac_1600) is an ornithine lipid N-methyltransferase from the planctomycete Singulisphaera acidiphila. J. Biol. Chem. 290 (2015) 15102-15111. [PMID: 25925947]
Accepted name: psilocybin synthase
Reaction: 2 S-adenosyl-L-methionine + 4-hydroxytryptamine 4-phosphate = 2 S-adenosyl-L-homocysteine + psilocybin (overall reaction)
(1a) S-adenosyl-L-methionine + 4-hydroxytryptamine 4-phosphate = S-adenosyl-L-homocysteine + 4-hydroxy-N-methyltryptamine 4-phosphate
(1b) S-adenosyl-L-methionine + 4-hydroxy-N-methyltryptamine 4-phosphate = S-adenosyl-L-homocysteine + psilocybin
For diagram of reaction click here
Glossary: psilocybin = 3-[2-(dimethylamino)ethyl]-1H-indol-4-yl phosphate
Other name(s): PsiM
Systematic name: S-adenosyl-L-methionine:4-hydroxytryptamine-4-phosphate N,N-dimethyltransferase
Comments: Isolated from the fungus Psilocybe cubensis. The product, psilocybin, is a psychoactive compound.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Fricke, J., Blei, F. and Hoffmeister, D. Enzymatic synthesis of psilocybin. Angew. Chem. Int. Ed. Engl. 56 (2017) 12352-12355. [PMID: 28763571]
Accepted name: U6 snRNA m6A methyltransferase
Reaction: S-adenosyl-L-methionine + adenine in U6 snRNA = S-adenosyl-L-homocysteine + N6-methyladenine in U6 snRNA
Other name(s): METTL16 (gene name)
Systematic name: S-adenosyl-L-methionine:adenine in U6 snRNA methyltransferase
Comments: This enzyme, found in vertebrates, methylates a specific adenine in a hairpin structure of snRNA. The effects of the binding of the methyltransferase to its substrate is important for the regulation of the activity of an isoform of EC 2.5.1.6, methionine adenosyltransferase, that produces S-adenosyl-L-methionine [1,2]. The enzyme also binds (and maybe methylates) the lncRNAs XIST and MALAT1 as well as a number of pre-mRNAs at specific positions often found in the intronic regions [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Pendleton, K.E., Chen, B., Liu, K., Hunter, O.V., Xie, Y., Tu, B.P. and Conrad, N.K. The U6 snRNA m6A methyltransferase METTL16 regulates SAM synthetase intron retention. Cell 169 (2017) 824-835.e14. [PMID: 28525753]
2. Warda, A.S., Kretschmer, J., Hackert, P., Lenz, C., Urlaub, H., Hobartner, C., Sloan, K.E. and Bohnsack, M.T. Human METTL16 is a N6-methyladenosine (m6A) methyltransferase that targets pre-mRNAs and various non-coding RNAs. EMBO Rep. 18 (2017) 2004-2014. [PMID: 29051200]
EC 2.1.1.347
Accepted name: (+)-O-methylkolavelool synthase
Reaction: S-adenosyl-L-methionine + (+)-kolavelool = S-adenosyl-L-homocysteine + (+)-O-methylkolavelool
For diagram of reaction click here.
Other name(s): Haur_2147 (locus name)
Systematic name: S-adenosyl-L-methionine:(+)-kolavelool O-methyltransferase
Comments: Isolated from the bacterium Herpetosiphon aurantiacus.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Nakano, C., Oshima, M., Kurashima, N. and Hoshino, T. Identification of a new diterpene biosynthetic gene cluster that produces O-methylkolavelool in Herpetosiphon aurantiacus. Chembiochem 16 (2015) 772-781. [PMID: 25694050]
EC 2.1.1.348
Accepted name: mRNA m6A methyltransferase
Reaction: S-adenosyl-L-methionine + adenine in mRNA = S-adenosyl-L-homocysteine + N6-methyladenine in mRNA
Other name(s): METTL3 (gene name); METTL14 (gene name)
Systematic name: S-adenosyl-L-methionine:adenine in mRNA methyltransferase
Comments: This enzyme, found in eukaryotes, methylates adenines in mRNA with the consensus sequence RRACH.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
PDB,
CAS registry number:
References:
1. Liu, J., Yue, Y., Han, D., Wang, X., Fu, Y., Zhang, L., Jia, G., Yu, M., Lu, Z., Deng, X., Dai, Q., Chen, W. and He, C. A METTL3-METTL14 complex mediates mammalian nuclear RNA N6-adenosine methylation. Nat. Chem. Biol. 10 (2014) 93-95. [PMID: 24316715]
2. Wang, X., Huang, J., Zou, T. and Yin, P. Human m6A writers: Two subunits, 2 roles. RNA Biol. 14 (2017) 300-304. [PMID: 28121234]
EC 2.1.1.349
Accepted name: toxoflavin synthase
Reaction: (1) S-adenosyl-L-methionine + 1,6-didemethyltoxoflavin = S-adenosyl-L-homocysteine + reumycin
For diagram of reaction click here.
Glossary: reumycin = 1-demethyltoxoflavin
Other name(s): toxA (gene name)
Systematic name: S-adenosyl-L-methionine:1,6-didemethyltoxoflavin N1,N6-dimethyltransferase (toxoflavin-forming)
Comments: The enzyme is a dual-specificity methyltransferase that catalyses the last two steps of toxoflavin biosynthesis. Toxoflavin is a major virulence factor of several bacterial crop pathogens.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Fenwick, M.K., Philmus, B., Begley, T.P. and Ealick, S.E. Burkholderia glumae ToxA Is a dual-specificity methyltransferase that catalyzes the last two steps of toxoflavin biosynthesis. Biochemistry 55 (2016) 2748-2759. [PMID: 27070241]
EC 2.1.1.350
Accepted name: menaquinone C8-methyltransferase
Reaction: (1) 2 S-adenosyl-L-methionine + a menaquinone + reduced flavodoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + an 8-methylmenaquinone + oxidized flavodoxin
For diagram of reaction click here
Other name(s): mqnK (gene name); menK (gene name)
Systematic name: S-adenosyl-L-methionine:menaquinone C8-methyltransferase
Comments: The enzyme, found in a wide range of bacteria and archaea, is a radical SAM (AdoMet) enzyme that utilizes two molecules of S-adenosyl-L-methionine, one as the methyl group donor, and one for the creation of a 5'-deoxyadenosine radical that drives the reaction forward.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Hein, S., Klimmek, O., Polly, M., Kern, M. and Simon, J. A class C radical S-adenosylmethionine methyltransferase synthesizes 8-methylmenaquinone. Mol. Microbiol. 104 (2017) 449-462. [PMID: 28164386]
EC 2.1.1.351
Accepted name: nocamycin O-methyltransferase
Reaction: S-adenosyl-L-methionine + nocamycin E = S-adenosyl-L-homocysteine + nocamycin I
For diagram of reaction click here
Glossary: nocamycin E = (2R,3S,3aS,5R,6R,7S,9aS)-5-[(2R,3E,5E)-7-hydroxy-4-methyl-7-(2,4-dioxopyrroliden-3-ylidene)hepta-3,5-dien-2-yl]-2,6,9a-trimethyl-8-oxooctahydro-3a,7-epoxyfuro[3,2-b]oxocine-3-carboxylate
Other name(s): ncmP (gene name)
Systematic name: S-adenosyl-L-methionine:nocamycin E O-methyltransferase
Comments: The enzyme, isolated from the bacterium Saccharothrix syringae, is involved in the biosynthesis of nocamycin I and nocamycin II.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Mo, X., Gui, C. and Wang, Q. Elucidation of a carboxylate O-methyltransferase NcmP in nocamycin biosynthetic pathway. Bioorg. Med. Chem. Lett. 27 (2017) 4431-4435. [PMID: 28818448]
EC 2.1.1.352
Accepted name: 3-O-acetyl-4'-O-demethylpapaveroxine 4'-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 3-O-acetyl-4'-O-demethylpapaveroxine = S-adenosyl-L-homocysteine + 3-O-acetylpapaveroxine
Glossary: 3-O-acetyl-4'-O-demethylpapaveroxine = 6-{(S)-acetoxy[(5R)-4-hydroxy-6-methyl-5,6,7,8-tetrahydro[1,3]dioxolo[4,5-g]isoquinolin-5-yl]methyl}-2,3-dimethoxybenzaldehyde
For diagram of reaction click here.
Systematic name: S-adenosyl-L-methionine:3-O-acetyl-4'-O-demethylpapaveroxine 4'-O-methyltransferase
Comments: This activity is part of the noscapine biosynthesis pathway, as characterized in the plant Papaver somniferum (opium poppy). It is catalysed by heterodimeric complexes of the OMT2 gene product and the product of either OMT3 or 6OMT. OMT2 is the catalytic subunit in both complexes.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Li, Y. and Smolke, C.D. Engineering biosynthesis of the anticancer alkaloid noscapine in yeast. Nat Commun 7 (2016) 12137. [PMID: 27378283]
2. Park, M.R., Chen, X., Lang, D.E., Ng, K.KS. and Facchini, P.J. Heterodimeric O-methyltransferases involved in the biosynthesis of noscapine in opium poppy. Plant J. 95 (2018) 252-267. [PMID: 29723437]
EC 2.1.1.353
Accepted name: demethylluteothin O-methyltransferase
Reaction: S-adenosyl-L-methionine + demethylluteothin = S-adenosyl-L-homocysteine + luteothin
For diagram of reaction click here.
Glossary: luteothin = 2-[(3E,5E)-3,5-dimethyl-6-(4-nitrophenyl)hexa-3,5-dien-1-yl]-6-methoxy-3,5-dimethyl-4H-pyran-4-one
Other name(s): aurI (gene name)
Systematic name: S-adenosyl-L-methionine:demethylluteothin O-methyltransferase
Comments: The enzyme, characterized from the bacterium Streptomyces thioluteus, participates in the biosynthesis of the antibiotic aureothin. An orthologous enzyme in the bacteria Streptomyces orinoci and Streptomyces spectabilis catalyses a similar reaction in the biosynthesis of spectinabilin.
Links to other databases:
BRENDA,
EXPASY,
ExplorEnz,
KEGG,
MetaCyc,
CAS registry number:
References:
1. He, J., Muller, M. and Hertweck, C. Formation of the aureothin tetrahydrofuran ring by a bifunctional cytochrome P450 monooxygenase. J. Am. Chem. Soc. 126 (2004) 16742-16743. [PMID: 15612710]
2. Muller, M., He, J. and Hertweck, C. Dissection of the late steps in aureothin biosynthesis. Chembiochem 7 (2006) 37-39. [PMID: 16292785]
EC 2.1.1.354
Accepted name: [histone H3]-lysine4 N-trimethyltransferase
Reaction: 3 S-adenosyl-L-methionine + a [histone H3]-L-lysine4 = 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine4 (overall reaction)
Other name(s): KMT2H (gene name); KMT3C (gene name); KMT3D (gene name); KMT3E (gene name); PRDM9 (gene name); MLL5 (gene name); ASH1L (gene name); SMYD1 (gene name); SMYD2 (gene name); SMYD3 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine4 N6-trimethyltransferase
Comments: This entry describes several enzymes that successively methylate the L-lysine4 residue of histone H3 (H3K4), ultimately generating a trimethylated form. These modifications influence the binding of chromatin-associated proteins. In most cases the trimethylation of this position is associated with gene activation. EC 2.1.1.364, [histone H3]-lysine4 N-methyltransferase, describes enzymes that can catalyse only monomethylation of this substrate (the first sub-reaction of this entry); EC 2.1.1.370, [histone H3]-lysine4 N-dimethyltransferase, describes enzymes that catalyse only dimethylation of this substrate (the first two sub-reactions of this entry)
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References:
1. Nakamura, T., Mori, T., Tada, S., Krajewski, W., Rozovskaia, T., Wassell, R., Dubois, G., Mazo, A., Croce, C.M. and Canaani, E. ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation. Mol. Cell 10 (2002) 1119-1128. [PMID: 12453419]
2. Hamamoto, R., Furukawa, Y., Morita, M., Iimura, Y., Silva, F.P., Li, M., Yagyu, R. and Nakamura, Y. SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells. Nat. Cell Biol. 6 (2004) 731-740. [PMID: 15235609]
3. Blazer, L.L., Lima-Fernandes, E., Gibson, E., Eram, M.S., Loppnau, P., Arrowsmith, C.H., Schapira, M. and Vedadi, M. PR domain-containing protein 7 (PRDM7) is a histone 3 lysine 4 trimethyltransferase. J. Biol. Chem. 291 (2016) 13509-13519. [PMID: 27129774]
EC 2.1.1.355
Accepted name: [histone H3]-lysine9 N-trimethyltransferase
Reaction: 3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9 = 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9 (overall reaction)
Other name(s): KMT1A (gene name); KMT1B (gene name); KMT1C (gene name); KMT1D (gene name); KMT1F (gene name); MT8 (gene name); SUV39H1 (gene name); G9A (gene name); EHMT1 (gene name); PRDM2 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine9 N6-trimethyltransferase
Comments: This entry describes several enzymes that successively methylate the L-lysine9 residue of histone H3 (H3K9), ultimately generating a trimethylated form. These modifications influence the binding of chromatin-associated proteins. In general, the methylation of H3K9 leads to transcriptional repression of the affected target genes. cf. EC 2.1.1.367, [histone H3]-lysine9 N-methyltransferase, EC 2.1.1.368, [histone H3]-lysine9 N-dimethyltransferase, and EC 2.1.1.366, [histone H3]-N6,N6-dimethyl-lysine9 N-methyltransferase.
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References:
1. O'Carroll, D., Scherthan, H., Peters, A.H., Opravil, S., Haynes, A.R., Laible, G., Rea, S., Schmid, M., Lebersorger, A., Jerratsch, M., Sattler, L., Mattei, M.G., Denny, P., Brown, S.D., Schweizer, D. and Jenuwein, T. Isolation and characterization of Suv39h2, a second histone H3 methyltransferase gene that displays testis-specific expression. Mol. Cell Biol. 20 (2000) 9423-9433. [PMID: 11094092]
2. Schotta, G., Ebert, A., Krauss, V., Fischer, A., Hoffmann, J., Rea, S., Jenuwein, T., Dorn, R. and Reuter, G. Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation and heterochromatic gene silencing. EMBO J. 21 (2002) 1121-1131. [PMID: 11867540]
3. Tachibana, M., Sugimoto, K., Nozaki, M., Ueda, J., Ohta, T., Ohki, M., Fukuda, M., Takeda, N., Niida, H., Kato, H. and Shinkai, Y. G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. Genes Dev. 16 (2002) 1779-1791. [PMID: 12130538]
4. Schultz, D.C., Ayyanathan, K., Negorev, D., Maul, G.G. and Rauscher, F.J., 3rd. SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins. Genes Dev. 16 (2002) 919-932. [PMID: 11959841]
5. Kim, K.C., Geng, L. and Huang, S. Inactivation of a histone methyltransferase by mutations in human cancers. Cancer Res. 63 (2003) 7619-7623. [PMID: 14633678]
6. Wu, H., Min, J., Lunin, V.V., Antoshenko, T., Dombrovski, L., Zeng, H., Allali-Hassani, A., Campagna-Slater, V., Vedadi, M., Arrowsmith, C.H., Plotnikov, A.N. and Schapira, M. Structural biology of human H3K9 methyltransferases. PLoS One 5 (2010) e8570. [PMID: 20084102]
EC 2.1.1.356
Accepted name: [histone H3]-lysine27 N-trimethyltransferase
Reaction: 3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27 = 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27 (overall reaction)
Other name(s): KMT6A (gene name); KMT6B (gene name); EZH1 (gene name); EZH2 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine27 N6-trimethyltransferase
Comments: This entry describes enzymes that successively methylate the L-lysine27 residue of histone H3 (H3K27), ultimately generating a trimethylated form. These modifications influence the binding of chromatin-associated proteins. The methylation of lysine27 leads to transcriptional repression of the affected target genes. The enzyme associates with other proteins to form a complex that is essential for activity. The enzyme can also methylate some non-histone proteins. cf. EC 2.1.1.369, [histone H3]-lysine27 N-methyltransferase and EC 2.1.1.371, [histone H3]-lysine27 N-dimethyltransferase.
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References:
1. Cao, R., Wang, L., Wang, H., Xia, L., Erdjument-Bromage, H., Tempst, P., Jones, R.S. and Zhang, Y. Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 298 (2002) 1039-1043. [PMID: 12351676]
2. Kuzmichev, A., Nishioka, K., Erdjument-Bromage, H., Tempst, P. and Reinberg, D. Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. Genes Dev. 16 (2002) 2893-2905. [PMID: 12435631]
3. Kirmizis, A., Bartley, S.M., Kuzmichev, A., Margueron, R., Reinberg, D., Green, R. and Farnham, P.J. Silencing of human polycomb target genes is associated with methylation of histone H3 Lys 27. Genes Dev. 18 (2004) 1592-1605. [PMID: 15231737]
4. Schlesinger, Y., Straussman, R., Keshet, I., Farkash, S., Hecht, M., Zimmerman, J., Eden, E., Yakhini, Z., Ben-Shushan, E., Reubinoff, B.E., Bergman, Y., Simon, I. and Cedar, H. Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer. Nat. Genet. 39 (2007) 232-236. [PMID: 17200670]
5. Shen, X., Liu, Y., Hsu, Y.J., Fujiwara, Y., Kim, J., Mao, X., Yuan, G.C. and Orkin, S.H. EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency. Mol. Cell 32 (2008) 491-502. [PMID: 19026780]
6. Ezhkova, E., Lien, W.H., Stokes, N., Pasolli, H.A., Silva, J.M. and Fuchs, E. EZH1 and EZH2 cogovern histone H3K27 trimethylation and are essential for hair follicle homeostasis and wound repair. Genes Dev. 25 (2011) 485-498. [PMID: 21317239]
EC 2.1.1.357
Accepted name: histone H3 lysine36 N-dimethyltransferase
Reaction: 2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36 = 2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36 (overall reaction)
Other name(s): KMT3B (gene name); KMT3C (gene name); NSD2 (gene name); NSD3 (gene name); SETMAR (gene name); WHSC1 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine36 N6-dimethyltransferase
Comments: This entry describes a group of metazoan enzymes that catalyse two successive methylations of lysine 36 of histone H3 (H3K36), forming mono- and dimethylated forms. These modifications influence the binding of chromatin-associated proteins. The product can be further methylated to the trimethyl form by EC 2.1.1.358, histone H3 dimethyl-L-lysine36 N-methyltransferase. The yeast SET2 enzyme can catalyse all three methylations (see EC 2.1.1.359, histone H3 lysine36 N-trimethyltransferase).
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References:
1. Fnu, S., Williamson, E.A., De Haro, L.P., Brenneman, M., Wray, J., Shaheen, M., Radhakrishnan, K., Lee, S.H., Nickoloff, J.A. and Hromas, R. Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining. Proc. Natl Acad. Sci. USA 108 (2011) 540-545. [PMID: 21187428]
2. Kuo, A.J., Cheung, P., Chen, K., Zee, B.M., Kioi, M., Lauring, J., Xi, Y., Park, B.H., Shi, X., Garcia, B.A., Li, W. and Gozani, O. NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming. Mol. Cell 44 (2011) 609-620. [PMID: 22099308]
3. Qiao, Q., Li, Y., Chen, Z., Wang, M., Reinberg, D. and Xu, R.M. The structure of NSD1 reveals an autoregulatory mechanism underlying histone H3K36 methylation. J. Biol. Chem 286 (2011) 8361-8368. [PMID: 21196496]
4. Wagner, E.J. and Carpenter, P.B. Understanding the language of Lys36 methylation at histone H3. Nat. Rev. Mol. Cell. Biol. 13 (2012) 115-126. [PMID: 22266761]
[EC 2.1.1.358 Deleted entry: [histone H3]-dimethyl-L-lysine36 N-methyltransferase. Now known to have the activity of EC 2.1.1.359, [histone H3]-lysine36 N-trimethyltransferase. (EC 2.1.1.358 created 1976 as EC 2.1.1.43, modified 1982, modified 1983, part transferred 2019 to EC 2.1.1.358, deleted 2020)]
EC 2.1.1.359
Accepted name: histone H3 lysine36 N-trimethyltransferase
Reaction: 3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36 = 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36 (overall reaction)
Other name(s): SET2 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine36 N6-trimethyltransferase
Comments: The enzyme, characterized from yeast, catalyses the successive methylation of lysine36 of histone H3 (H3K36), forming the trimethylated form. These modifications influence the binding of chromatin-associated proteins. The enzyme couples the methylation reactions with transcriptional elongation through an interaction with the large subunit of RNA polymerase II. In mammals this activity is catalysed by two different enzymes, EC 2.1.1.357, histone H3 lysine36 N-dimethyltransferase and EC 2.1.1.358, histone H3 dimethyl-L-lysine36 N-methyltransferase.
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References:
1. Strahl, B.D., Grant, P.A., Briggs, S.D., Sun, Z.W., Bone, J.R., Caldwell, J.A., Mollah, S., Cook, R.G., Shabanowitz, J., Hunt, D.F. and Allis, C.D. Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression. Mol. Cell Biol. 22 (2002) 1298-1306. [PMID: 11839797]
2. Landry, J., Sutton, A., Hesman, T., Min, J., Xu, R.M., Johnston, M. and Sternglanz, R. Set2-catalyzed methylation of histone H3 represses basal expression of GAL4 in Saccharomyces cerevisiae. Mol. Cell Biol. 23 (2003) 5972-5978. [PMID: 12917322]
3. Morris, S.A., Shibata, Y., Noma, K., Tsukamoto, Y., Warren, E., Temple, B., Grewal, S.I. and Strahl, B.D. Histone H3 K36 methylation is associated with transcription elongation in Schizosaccharomyces pombe. Eukaryot Cell 4 (2005) 1446-1454. [PMID: 16087749]
4. Lin, L.J., Minard, L.V., Johnston, G.C., Singer, R.A. and Schultz, M.C. Asf1 can promote trimethylation of H3 K36 by Set2. Mol. Cell Biol. 30 (2010) 1116-1129. [PMID: 20048053]
EC 2.1.1.360
Accepted name: histone H3 lysine79 N-trimethyltransferase
Reaction: 3 S-adenosyl-L-methionine + a [histone H3]-L-lysine79 = 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79 (overall reaction)
Other name(s): DOT1L (gene name); KMT4 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine79 N6-trimethyltransferase
Comments: The enzyme successively methylates the L-lysine79 residue of histone H3 (H3K79), ultimately generating a trimethylated form. These modifications influence the binding of chromatin-associated proteins. This is the only known methylation event of a lysine residue within the core region of a histone, as all other such modifications occur at the tail.
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References:
1. Feng, Q., Wang, H., Ng, H.H., Erdjument-Bromage, H., Tempst, P., Struhl, K. and Zhang, Y. Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain. Curr. Biol. 12 (2002) 1052-1058. [PMID: 12123582]
2. Ng, H.H., Feng, Q., Wang, H., Erdjument-Bromage, H., Tempst, P., Zhang, Y. and Struhl, K. Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association. Genes Dev. 16 (2002) 1518-1527. [PMID: 12080090]
3. Min, J., Feng, Q., Li, Z., Zhang, Y. and Xu, R.M. Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. Cell 112 (2003) 711-723. [PMID: 12628190]
4. Steger, D.J., Lefterova, M.I., Ying, L., Stonestrom, A.J., Schupp, M., Zhuo, D., Vakoc, A.L., Kim, J.E., Chen, J., Lazar, M.A., Blobel, G.A. and Vakoc, C.R. DOT1L/KMT4 recruitment and H3K79 methylation are ubiquitously coupled with gene transcription in mammalian cells. Mol. Cell Biol. 28 (2008) 2825-2839. [PMID: 18285465]
EC 2.1.1.361
Accepted name: histone H4 lysine20 N-methyltransferase
Reaction: S-adenosyl-L-methionine + a [histone H4]-L-lysine20 = S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine-20
Other name(s): KMT5A (gene name); SET8 (gene name); PR-SET7 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H4]-L-lysine20 N6-methyltransferase
Comments: The enzyme catalyses the monomethylation of the L-lysine20 residue of histone H4 (H4K20). This event is usually followed by further methylation by EC 2.1.1.362, histone H4 N-methyl-L-lysine20 N-methyltransferase. This enzyme plays a pivotal role in DNA replication. Activity is high during the G2 and M phases, but declines significantly during G1 and S phases. Mutations in the enzyme have severe consequences, including DNA double-strand breaks, activation of DNA damage checkpoints, defective cell cycle progression, and reduced cell proliferation.
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References:
1. Fang, J., Feng, Q., Ketel, C.S., Wang, H., Cao, R., Xia, L., Erdjument-Bromage, H., Tempst, P., Simon, J.A. and Zhang, Y. Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase. Curr. Biol. 12 (2002) 1086-1099. [PMID: 12121615]
2. Nishioka, K., Rice, J.C., Sarma, K., Erdjument-Bromage, H., Werner, J., Wang, Y., Chuikov, S., Valenzuela, P., Tempst, P., Steward, R., Lis, J.T., Allis, C.D. and Reinberg, D. PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin. Mol. Cell 9 (2002) 1201-1213. [PMID: 12086618]
3. Jorgensen, S., Elvers, I., Trelle, M.B., Menzel, T., Eskildsen, M., Jensen, O.N., Helleday, T., Helin, K. and Sorensen, C.S. The histone methyltransferase SET8 is required for S-phase progression. J. Cell Biol. 179 (2007) 1337-1345. [PMID: 18166648]
4. Oda, H., Okamoto, I., Murphy, N., Chu, J., Price, S.M., Shen, M.M., Torres-Padilla, M.E., Heard, E. and Reinberg, D. Monomethylation of histone H4-lysine 20 is involved in chromosome structure and stability and is essential for mouse development. Mol. Cell Biol. 29 (2009) 2278-2295. [PMID: 19223465]
5. Jorgensen, S., Schotta, G. and Sorensen, C.S. Histone H4 lysine 20 methylation: key player in epigenetic regulation of genomic integrity. Nucleic Acids Res. 41 (2013) 2797-2806. [PMID: 23345616]
EC 2.1.1.362
Accepted name: histone H4 N-methyl-L-lysine20 N-methyltransferase
Reaction: S-adenosyl-L-methionine + a [histone H4]-N6-methyl-L-lysine20 = S-adenosyl-L-homocysteine + a [histone H4]-N6,N6-dimethyl-L-lysine20
Other name(s): KMT5B (gene name); KMT5C (gene name); SUV420H1 (gene name); SUV420H2 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H4]-N6-methyl-L-lysine20 N6-methyltransferase
Comments: This entry describes a group of enzymes that catalyse a single methylation of monomethylated lysine 20 of histone H4 (H4K20m1, generated by EC 2.1.1.361, histone H4 lysine20 N-methyltransferase), forming the dimethylated form. This modification is broadly distributed across the genome and is likely important for general chromatin-mediated processes. The double-methylated form of lysine20 in histone H4 is the most abundant methylation state of this residue and is found on ~80% of all histone H4 molecules. Full activity of the enzyme requires that the lysine at position 9 of histone H3 is trimethylated.
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References:
1. Schotta, G., Lachner, M., Sarma, K., Ebert, A., Sengupta, R., Reuter, G., Reinberg, D. and Jenuwein, T. A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin. Genes Dev. 18 (2004) 1251-1262. [PMID: 15145825]
2. Jorgensen, S., Schotta, G. and Sorensen, C.S. Histone H4 lysine 20 methylation: key player in epigenetic regulation of genomic integrity. Nucleic Acids Res. 41 (2013) 2797-2806. [PMID: 23345616]
3. Wu, H., Siarheyeva, A., Zeng, H., Lam, R., Dong, A., Wu, X.H., Li, Y., Schapira, M., Vedadi, M. and Min, J. Crystal structures of the human histone H4K20 methyltransferases SUV420H1 and SUV420H2. FEBS Lett. 587 (2013) 3859-3868. [PMID: 24396869]
4. Southall, S.M., Cronin, N.B. and Wilson, J.R. A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases. Nucleic Acids Res. 42 (2014) 661-671. [PMID: 24049080]
5. Weirich, S., Kudithipudi, S. and Jeltsch, A. Specificity of the SUV4-20H1 and SUV4-20H2 protein lysine methyltransferases and methylation of novel substrates. J. Mol. Biol. 428 (2016) 2344-2358. [PMID: 27105552]
EC 2.1.1.363
Accepted name: pre-sodorifen synthase
Reaction: S-adenosyl-L-methionine + (2E,6E)-farnesyl diphosphate = S-adenosyl-L-homocysteine + pre-sodorifen diphosphate
Glossary: pre-sodorifen diphosphate = [(2E)-3-methyl-5-[(1S,4R,5R)-1,2,3,4,5-pentamethylcyclopent-2-en-1-yl]pent-2-en-1-yl phosphonato]oxyphosphonate
Other name(s): sodC (gene name)
Systematic name: (2E,6E)-farnesyl diphosphate 10-C-methyltransferase (cyclyzing, pre-sodorifen diphosphate producing)
Comments: The enzyme, characterized from the bacterium Serratia plymuthica, participates in biosynthesis of sodorifen.
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References:
1. Domik, D., Magnus, N. and Piechulla, B. Analysis of a new cluster of genes involved in the synthesis of the unique volatile organic compound sodorifen of Serratia plymuthica 4Rx13. FEMS Microbiol. Lett. 363(14) (2016) fnw139. [PMID: 27231241]
2. Schmidt, R., Jager, V., Zuhlke, D., Wolff, C., Bernhardt, J., Cankar, K., Beekwilder, J., Ijcken, W.V., Sleutels, F., Boer, W., Riedel, K. and Garbeva, P. Fungal volatile compounds induce production of the secondary metabolite sodorifen in Serratia plymuthica PRI-2C. Sci Rep 7 (2017) 862. [PMID: 28408760]
3. von Reuss, S., Domik, D., Lemfack, M.C., Magnus, N., Kai, M., Weise, T. and Piechulla, B. Sodorifen biosynthesis in the rhizobacterium Serratia plymuthica involves methylation and cyclization of MEP-derived farnesyl pyrophosphate by a SAM-dependent C-methyltransferase. J. Am. Chem. Soc. 140 (2018) 11855-11862. [PMID: 30133268]
EC 2.1.1.364
Accepted name: [histone H3]-lysine4 N-methyltransferase
Reaction: S-adenosyl-L-methionine + a [histone H3]-L-lysine4 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine4
Other name(s): KMT7 (gene name); SETD7 (gene name); SET7/9 (gene name); KIAA1717 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine4 N6-methyltransferase
Comments: This entry describes enzymes that catalyse a single methylation of the L-lysine4 residue of histone H3 (H3K4), generating a monomethylated form. This modifications influence the binding of chromatin-associated proteins and result in gene activation or suppression. Some enzymes that catalyse this reaction continue to generate a trimethylated form; these enzymes are classified under EC 2.1.1.354, [histone H3]-lysine4 N-trimethyltransferase.
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References:
1. Wang, H., Cao, R., Xia, L., Erdjument-Bromage, H., Borchers, C., Tempst, P. and Zhang, Y. Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Mol. Cell 8 (2001) 1207-1217. [PMID: 11779497]
2. Nishioka, K., Chuikov, S., Sarma, K., Erdjument-Bromage, H., Allis, C.D., Tempst, P. and Reinberg, D. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev. 16 (2002) 479-489. [PMID: 11850410]
3. Wilson, J.R., Jing, C., Walker, P.A., Martin, S.R., Howell, S.A., Blackburn, G.M., Gamblin, S.J. and Xiao, B. Crystal structure and functional analysis of the histone methyltransferase SET7/9. Cell 111 (2002) 105-115. [PMID: 12372304]
4. Xiao, B., Jing, C., Wilson, J.R., Walker, P.A., Vasisht, N., Kelly, G., Howell, S., Taylor, I.A., Blackburn, G.M. and Gamblin, S.J. Structure and catalytic mechanism of the human histone methyltransferase SET7/9. Nature 421 (2003) 652-656. [PMID: 12540855]
5. Hu, P. and Zhang, Y. Catalytic mechanism and product specificity of the histone lysine methyltransferase SET7/9: an ab initio QM/MM-FE study with multiple initial structures. J. Am. Chem. Soc. 128 (2006) 1272-1278. [PMID: 16433545]
EC 2.1.1.365
Accepted name: MMP 1-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 3,3'-di-O-methyl-4α-mannobiose = S-adenosyl-L-homocysteine + 1,3,3'-tri-O-methyl-4α-mannobiose
Glossary: 3,3'-di-O-methyl-4α-mannobiose = 3-O-methyl-α-D-mannopyranosyl-(1→4)-3-O-methyl-α-D-mannopyranose
Other name(s): MeT1; 3-O-methylmannose polysaccharide 1-O-methyltransferase
Systematic name: S-adenosyl-L-methionine:3,3'-di-O-methyl-4α-mannobiose 1-O-methyltransferase
Comments: Requires Mg2+. The enzyme, characterized from the bacterium Mycolicibacterium hassiacum, participates in the biosynthesis of 3-O-methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in nontuberculous mycobacteria. The methylation catalysed by this enzyme was shown to block the reducing end of 3,3'-di-O-methyl-α-mannobiose, a probable early precursor of the 3-O-methylmannose polysaccharides.
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References:
1. Ripoll-Rozada, J., Costa, M., Manso, J.A., Maranha, A., Miranda, V., Sequeira, A., Ventura, M.R., Macedo-Ribeiro, S., Pereira, P.JB. and Empadinhas, N. Biosynthesis of mycobacterial methylmannose polysaccharides requires a unique 1-O-methyltransferase specific for 3-O-methylated mannosides. Proc. Natl. Acad. Sci. USA 116 (2019) 835-844. [PMID: 30606802]
EC 2.1.1.366
Accepted name: [histone H3]-N6,N6-dimethyl-lysine9 N-methyltransferase
Reaction: S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Other name(s): KMT1E (gene name); SETDB1 (gene name); KIAA0067 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-N6,N6-dimethyl-L-lysine9 N6-methyltransferase
Comments: The enzyme methylates only dimethylated lysine9 of histone H3 (H3K9), forming the trimethylated form. This modification influences the binding of chromatin-associated proteins. In general, the methylation of H3K9 leads to transcriptional repression of the affected target genes. The enzyme is highly upregulated in Huntington disease patients. cf. EC 2.1.1.367, [histone H3]-lysine9 N-methyltransferase, and EC 2.1.1.368, [histone H3]-lysine9 N-dimethyltransferase, and EC 2.1.1.355, [histone H3]-lysine9 N-trimethyltransferase.
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References:
1. Yang, L., Xia, L., Wu, D.Y., Wang, H., Chansky, H.A., Schubach, W.H., Hickstein, D.D. and Zhang, Y. Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor. Oncogene 21 (2002) 148-152. [PMID: 11791185]
2. Wang, H., An, W., Cao, R., Xia, L., Erdjument-Bromage, H., Chatton, B., Tempst, P., Roeder, R.G. and Zhang, Y. mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression. Mol. Cell 12 (2003) 475-487. [PMID: 14536086]
3. Pinheiro, I., Margueron, R., Shukeir, N., Eisold, M., Fritzsch, C., Richter, F.M., Mittler, G., Genoud, C., Goyama, S., Kurokawa, M., Son, J., Reinberg, D., Lachner, M. and Jenuwein, T. Prdm3 and Prdm16 are H3K9me1 methyltransferases required for mammalian heterochromatin integrity. Cell 150 (2012) 948-960. [PMID: 22939622]
EC 2.1.1.367
Accepted name: [histone H3]-lysine9 N-methyltransferase
Reaction: S-adenosyl-L-methionine + a [histone H3]-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
Other name(s): PRDM3 (gene name); PRDM16 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine9 N6-methyltransferase
Comments: This entry describes several enzymes that methylate the L-lysine-9 residue of histone H3 (H3K9) only once, generating a monomethylated form. These modifications influence the binding of chromatin-associated proteins. cf. EC 2.1.1.368, [histone H3]-lysine9 N-dimethyltransferase, EC 2.1.1.355, [histone H3]-lysine9 N-trimethyltransferase, and EC 2.1.1.366, [histone H3]-N6,N6-dimethyl-lysine9 N-methyltransferase.
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References:
1. Pinheiro, I., Margueron, R., Shukeir, N., Eisold, M., Fritzsch, C., Richter, F.M., Mittler, G., Genoud, C., Goyama, S., Kurokawa, M., Son, J., Reinberg, D., Lachner, M. and Jenuwein, T. Prdm3 and Prdm16 are H3K9me1 methyltransferases required for mammalian heterochromatin integrity. Cell 150 (2012) 948-960. [PMID: 22939622]
EC 2.1.1.368
Accepted name: [histone H3]-lysine9 N-dimethyltransferase
Reaction: 2 S-adenosyl-L-methionine + a [histone H3]-L-lysine9 = 2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9 (overall reaction)
Other name(s): SUVH1 (gene name); SUVR1 (gene name); SET32 (gene name); SDG32 (gene name); SET13 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine9 N6-dimethyltransferase
Comments: This entry describes several enzymes, characterized from plants, that successively methylate the L-lysine-9 residue of histone H3 (H3K9) twice, ultimately generating a dimethylated form. These modifications influence the binding of chromatin-associated proteins. In general, the methylation of H3K9 leads to transcriptional repression of the affected target genes. cf. EC 2.1.1.367, [histone H3]-lysine9 N-methyltransferase, EC 2.1.1.366, [histone H3]-N6,N6-dimethyl-lysine9 N-methyltransferase, and EC 2.1.1.355, [histone H3]-lysine9 N-trimethyltransferase.
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References:
1. Yu, Y., Dong, A. and Shen, W.H. Molecular characterization of the tobacco SET domain protein NtSET1 unravels its role in histone methylation, chromatin binding, and segregation. Plant J. 40 (2004) 699-711. [PMID: 15546353]
2. Shen, W.H. and Meyer, D. Ectopic expression of the NtSET1 histone methyltransferase inhibits cell expansion, and affects cell division and differentiation in tobacco plants. Plant Cell Physiol. 45 (2004) 1715-1719. [PMID: 15574848]
3. Naumann, K., Fischer, A., Hofmann, I., Krauss, V., Phalke, S., Irmler, K., Hause, G., Aurich, A.C., Dorn, R., Jenuwein, T. and Reuter, G. Pivotal role of AtSUVH2 in heterochromatic histone methylation and gene silencing in Arabidopsis. EMBO J. 24 (2005) 1418-1429. [PMID: 15775980]
EC 2.1.1.369
Accepted name: [histone H3]-lysine27 N-methyltransferase
Reaction: S-adenosyl-L-methionine + a [histone H3]-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
Other name(s): ATXR5 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine27 N6-methyltransferase
Comments: This entry describes enzymes that methylate the L-lysine-27 residue of histone H3 only once, generating a monomethylated form. This modification influences the binding of chromatin-associated proteins. The methylation of lysine-27 leads to transcriptional repression of the affected target genes. cf. EC 2.1.1.371, [histone H3]-lysine27 N-dimethyltransferase, and EC 2.1.1.356, [histone H3]-lysine27 N-trimethyltransferase.
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References:
1. Jacob, Y., Feng, S., LeBlanc, C.A., Bernatavichute, Y.V., Stroud, H., Cokus, S., Johnson, L.M., Pellegrini, M., Jacobsen, S.E. and Michaels, S.D. ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing. Nat. Struct. Mol. Biol. 16 (2009) 763-768. [PMID: 19503079]
EC 2.1.1.370
Accepted name: [histone H3]-lysine4 N-dimethyltransferase
Reaction: 2 S-adenosyl-L-methionine + a [histone H3]-L-lysine4 = 2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine4 (overall reaction)
Other name(s): NSD3 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine4 N6-dimethyltransferase
Comments: This entry describes enzymes that successively methylate the L-lysine4 residue of histone H3 (H3K4) twice, ultimately generating a dimethylated form. These modifications influence the binding of chromatin-associated proteins.The human NSD3 protein also catalyses the activity of EC 2.1.1.371, [histone H3]-lysine27 N-dimethyltransferase. cf. EC 2.1.1.364, [histone H3]-lysine4 N-methyltransferase, and EC 2.1.1.354, [histone H3]-lysine4 N-trimethyltransferase.
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References:
1. Kim, S.M., Kee, H.J., Eom, G.H., Choe, N.W., Kim, J.Y., Kim, Y.S., Kim, S.K., Kook, H., Kook, H. and Seo, S.B. Characterization of a novel WHSC1-associated SET domain protein with H3K4 and H3K27 methyltransferase activity. Biochem. Biophys. Res. Commun. 345 (2006) 318-323. [PMID: 16682010]
EC 2.1.1.371
Accepted name: [histone H3]-lysine27 N-dimethyltransferase
Reaction: 2 S-adenosyl-L-methionine + a [histone H3]-L-lysine27 = 2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27 (overall reaction)
Other name(s): NSD3 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine27 N6-dimethyltransferase
Comments: This entry describes enzymes that successively methylate the L-lysine27 residue of histone H3 (H3K27) twice, ultimately generating a dimethylated form. These modifications influence the binding of chromatin-associated proteins.The human NSD3 protein also catalyses the activity of EC2.1.1.370, [histone H3]-lysine4 N-dimethyltransferase. cf. EC 2.1.1.369, [histone H3]-lysine27 N-methyltransferase, and EC 2.1.1.356, [histone H3]-lysine27 N-trimethyltransferase.
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References:
1. Kim, S.M., Kee, H.J., Eom, G.H., Choe, N.W., Kim, J.Y., Kim, Y.S., Kim, S.K., Kook, H., Kook, H. and Seo, S.B. Characterization of a novel WHSC1-associated SET domain protein with H3K4 and H3K27 methyltransferase activity. Biochem. Biophys. Res. Commun. 345 (2006) 318-323. [PMID: 16682010]
EC 2.1.1.372
Accepted name: [histone H4]-lysine20 N-trimethyltransferase
Reaction: 3 S-adenosyl-L-methionine + a [histone H4]-L-lysine20 = 3 S-adenosyl-L-homocysteine + a [histone H4]-N6,N6,N6-trimethyl-L-lysine20 (overall reaction)
Other name(s): SET9 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H4]-L-lysine20 N6-trimethyltransferase
Comments: The enzyme, characterized from the fission yeast Schizosaccharomyces pombe, catalyses three successive methylations of the L-lysine-20 residue of histone H4 (H4K20), forming the trimethylated form. The methylation of this site is apparently not involved in the regulation of gene expression or heterochromatin function but participates in DNA damage response. cf. EC 2.1.1.361, [histone H4]-lysine20 N-methyltransferase, and EC 2.1.1.362, [histone H4]-N-methyl-L-lysine20 N-methyltransferase.
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References:
1. Sanders, S.L., Portoso, M., Mata, J., Bahler, J., Allshire, R.C. and Kouzarides, T. Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage. Cell 119 (2004) 603-614. [PMID: 15550243]
EC 2.1.1.373
Accepted name: 2-hydroxy-4-(methylsulfanyl)butanoate S-methyltransferase
Reaction: S-adenosyl-L-methionine + (2R)-2-hydroxy-4-(methylsulfanyl)butanoate = S-adenosyl-L-homocysteine + (2R)-4-(dimethylsulfaniumyl)-2-hydroxybutanoate
Other name(s): dsyB (gene name); methylthiohydroxybutyrate methyltransferase; MTHB methyltransferase
Systematic name: S-adenosyl-L-methionine:(2R)-2-hydroxy-4-(methylsulfanyl)butanoate S-methyltransferase
Comments: The enzyme, characterized from the marine bacterium Labrenzia aggregata, participates in the biosynthesis of dimethylsulfoniopropanoate (DMSP). A eukaryotic enzyme that shares little sequence similarity with the bacterial enzyme was identified in many marine phytoplankton species.
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References:
1. Summers, P.S., Nolte, K.D., Cooper, A.J.L., Borgeas, H., Leustek, T., Rhodes, D. and Hanson, A.D. Identification and stereospecificity of the first three enzymes of 3-dimethylsulfoniopropionate biosynthesis in a chlorophyte alga. Plant Physiol. 116 (1998) 369-378.
2. Curson, A.R., Liu, J., Bermejo Martinez, A., Green, R.T., Chan, Y., Carrion, O., Williams, B.T., Zhang, S.H., Yang, G.P., Bulman Page, P.C., Zhang, X.H. and Todd, J.D. Dimethylsulfoniopropionate biosynthesis in marine bacteria and identification of the key gene in this process. Nat. Microbiol. 2 (2017) 17009. [PMID: 28191900]
3. Kageyama, H., Tanaka, Y., Shibata, A., Waditee-Sirisattha, R. and Takabe, T. Dimethylsulfoniopropionate biosynthesis in a diatom Thalassiosira pseudonana: Identification of a gene encoding MTHB-methyltransferase. Arch. Biochem. Biophys. 645 (2018) 100-106. [PMID: 29574051]
4. Curson, A.RJ., Williams, B.T., Pinchbeck, B.J., Sims, L.P., Martinez, A.B., Rivera, P.PL., Kumaresan, D., Mercade, E., Spurgin, L.G., Carrion, O., Moxon, S., Cattolico, R.A., Kuzhiumparambil, U., Guagliardo, P., Clode, P.L., Raina, J.B. and Todd, J.D. DSYB catalyses the key step of dimethylsulfoniopropionate biosynthesis in many phytoplankton. Nat. Microbiol. 3 (2018) 430-439. [PMID: 29483657]
EC 2.1.1.374
Accepted name: 2-heptyl-1-hydroxyquinolin-4(1H)-one methyltransferase
Reaction: S-adenosyl-L-methionine + 2-heptyl-1-hydroxyquinolin-4(1H)-one = S-adenosyl-L-homocysteine + 2-heptyl-1-methoxyquinolin-4(1H)-one
Other name(s): htm (gene name)
Systematic name: S-adenosyl-L-methionine:2-heptyl-1-hydroxyquinolin-4(1H)-one methyltransferase
Comments: The enzyme, found in mycobacteria, is a member of a family of heterocyclic toxin methyltransferases. It is involved in defense against several antimicrobial natural compounds and drugs. 4-Hydroxyquinolin-2(1H)-one, 2-heptylquinolin-4(1H)-one, 2-heptyl-3-hydroxyquinolin-4(1H)-one (the "Pseudomonas quinolone signal", PQS) and the flavonol quercetin are also O-methylated, albeit with lower activity [2]. The enzyme also N-methylates the bactericidal compound 3-methyl-1-oxo-2-[3-oxo-3-(pyrrolidin-1-yl)propyl]-1,5-dihydrobenzo[4,5]imidazo[1,2-a]pyridine-4-carbonitrile [1].
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References:
1. Warrier, T., Kapilashrami, K., Argyrou, A., Ioerger, T.R., Little, D., Murphy, K.C., Nandakumar, M., Park, S., Gold, B., Mi, J., Zhang, T., Meiler, E., Rees, M., Somersan-Karakaya, S., Porras-De Francisco, E., Martinez-Hoyos, M., Burns-Huang, K., Roberts, J., Ling, Y., Rhee, K.Y., Mendoza-Losana, A., Luo, M. and Nathan, C.F. N-methylation of a bactericidal compound as a resistance mechanism in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 113 (2016) E4523-E4530. [PMID: 27432954]
2. Sartor, P., Bock, J., Hennecke, U., Thierbach, S. and Fetzner, S. Modification of the Pseudomonas aeruginosa toxin 2-heptyl-1-hydroxyquinolin-4(1H)-one and other secondary metabolites by methyltransferases from mycobacteria. FEBS J. (2020) . [PMID: 33064871]
EC 2.1.1.375
Accepted name: NNS virus cap methyltransferase
Reaction: 2 S-adenosyl-L-methionine + G(5')pppAACA-[mRNA] = 2 S-adenosyl-L-homocysteine + m7G(5')pppAmACA-[mRNA] (overall reaction)
Systematic name: S-adenosyl-L-methionine:G(5')pppAACA-[mRNA] N7,2'-O-methyltransferase
Comments: The enzyme from non-segmented negative strain (NNS) viruses (e.g. rhabdoviruses) catalyses two successive methylations. In higher eukaryotes the two methylations occur in the reverse order and are catalysed by two different enzymes (cf. EC 2.1.1.56, mRNA (guanine-N7)-methyltransferase, and EC 2.1.1.57, methyltransferase cap1) that do not required a specific motif.
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1. Rahmeh, A.A., Li, J., Kranzusch, P.J. and Whelan, S.P. Ribose 2'-O methylation of the vesicular stomatitis virus mRNA cap precedes and facilitates subsequent guanine-N-7 methylation by the large polymerase protein. J. Virol. 83 (2009) 11043-11050. [PMID: 19710136]
EC 2.1.1.376
Accepted name: glycine betaine—corrinoid protein Co-methyltransferase
Reaction: glycine betaine + a [Co(I) glycine betaine-specific corrinoid protein] = N,N-dimethylglycine + a [methyl-Co(III) glycine betaine-specific corrinoid protein]
Other name(s): mtgB (gene name); glycine betaine methyltransferase
Systematic name: glycine betaine:[Co(I) glycine betaine-specific corrinoid protein] Co-methyltransferase
Comments: The enzyme, which catalyses the transfer of a methyl group from glycine betaine to a glycine betaine-specific corrinoid protein (MtgC), is involved in methanogenesis from glycine betaine in some methanogenic archaea, and in glycine betaine degradation in some bacteria. Unlike similar enzymes involved in methanogenesis from methylated C1 compounds, this enzyme does not contain the unusual amino acid L-pyrrolysine.
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References:
1. Ticak, T., Kountz, D.J., Girosky, K.E., Krzycki, J.A. and Ferguson, D.J., Jr. A nonpyrrolysine member of the widely distributed trimethylamine methyltransferase family is a glycine betaine methyltransferase. Proc. Natl. Acad. Sci. USA 111 (2014) E4668-E4676. [PMID: 25313086]
2. Creighbaum, A.J., Ticak, T., Shinde, S., Wang, X. and Ferguson, D.J., Jr. Examination of the glycine betaine-dependent methylotrophic methanogenesis pathway: insights into anaerobic quaternary amine methylotrophy. Front. Microbiol. 10 (2019) 2572. [PMID: 31787957]
EC 2.1.1.377
Accepted name: [methyl-Co(III) glycine betaine-specific corrinoid protein]—coenzyme M methyltransferase
Reaction: a [methyl-Co(III) glycine betaine-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) glycine betaine-specific corrinoid protein]
Other name(s): mtaA (gene name)
Systematic name: methylated glycine betaine-specific corrinoid protein:CoM methyltransferase
Comments: The enzyme, which is involved in methanogenesis from glycine betaine, catalyses the transfer of a methyl group bound to the cobalt cofactor of glycine betaine-specific corrinoid protein to coenzyme M, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, which catalyses the final step in methanogenesis. The enzyme from the methanogenic archaeon Methanolobus vulcani B1d can also catalyse the activity of EC 2.1.1.246, [methyl-Co(III) methanol-specific corrinoid protein]—coenzyme M methyltransferase.
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References:
1. Creighbaum, A.J., Ticak, T., Shinde, S., Wang, X. and Ferguson, D.J., Jr. Examination of the glycine betaine-dependent methylotrophic methanogenesis pathway: insights into anaerobic quaternary amine methylotrophy. Front. Microbiol. 10 (2019) 2572. [PMID: 31787957]
EC 2.1.1.378
Accepted name: [methyl-Co(III) glycine betaine-specific corrinoid protein]—tetrahydrofolate methyltransferase
Reaction: a [methyl-Co(III) glycine betaine-specific corrinoid protein] + tetrahydrofolate = a [Co(I) glycine betaine-specific corrinoid protein] + 5-methyltetrahydrofolate
Other name(s): mtgA (gene name); DSY3157 (locus name)
Systematic name: [methyl-Co(III) glycine betaine-specific corrinoid protein]:tetrahydrofolate N-methyltransferase
Comments: This enzyme, characterized from the anaerobic bacterium Desulfitobacterium hafniense Y51, catalyses a similar reaction to that of EC 2.1.1.258, 5-methyltetrahydrofolate—corrinoid/iron-sulfur protein Co-methyltransferase, but in the opposite direction, transferring a methyl group from a methylated corrinoid protein to tetrahydrofolate. The corrinoid protein is specifically methylated by EC 2.1.1.376, glycine betaine—corrinoid protein Co-methyltransferase.
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References:
1. Ticak, T., Kountz, D.J., Girosky, K.E., Krzycki, J.A. and Ferguson, D.J., Jr. A nonpyrrolysine member of the widely distributed trimethylamine methyltransferase family is a glycine betaine methyltransferase. Proc. Natl. Acad. Sci. USA 111 (2014) E4668-E4676. [PMID: 25313086]
EC 2.1.1.379
Accepted name: [methyl coenzyme M reductase]-L-arginine C-5-methyltransferase
Reaction: 2 S-adenosyl-L-methionine + a [methyl coenzyme-M reductase]-L-arginine + reduced acceptor = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + a [methyl coenzyme-M reductase]-(5S)-C-methyl-L-arginine + acceptor
Other name(s): methanogenesis marker protein 10; Mmp10
Systematic name: S-adenosyl-L-methionine:[methyl coenzyme M reductase]-L-arginine C-5-(S)-methyltransferase
Comments: The enzyme, present in methanogenic archaea, catalyses a modification of an L-arginine residue at the active site of EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase (better known as methyl-coenzyme M reductase), which catalyses the last and methane-releasing step of methanogenesis. The enzyme is a radical AdoMet (radical SAM) enzyme and contains a [4Fe-4S] cluster and a Coα-[α-(5-hydroxybenzimidazolyl)]-cobamide cofactor. The methyl group, which is derived from S-adenosyl-L-methionine, is transferred to the cob(I)amide cofactor, forming methylcob(III)amide as an intermediate carrier, before being transferred to the arginine residue.
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References:
1. Deobald, D., Adrian, L., Schone, C., Rother, M. and Layer, G. Identification of a unique radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase. Sci. Rep. 8 (2018) 7404. [PMID: 29743535]
2. Radle, M.I., Miller, D.V., Laremore, T.N. and Booker, S.J. Methanogenesis marker protein 10 (Mmp10) from Methanosarcina acetivorans is a radical S-adenosylmethionine methylase that unexpectedly requires cobalamin. J. Biol. Chem. 294 (2019) 11712-11725. [PMID: 31113866]
3. Lyu, Z., Shao, N., Chou, C.W., Shi, H., Patel, R., Duin, E.C. and Whitman, W.B. Posttranslational methylation of arginine in methyl coenzyme M reductase has a profound impact on both methanogenesis and growth of Methanococcus maripaludis. J. Bacteriol. 202 (2020) . [PMID: 31740491]
EC 2.1.1.380
Accepted name: 3-amino-4-hydroxybenzoate 4-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 3-amino-2,4-dihydroxybenzoate = S-adenosyl-L-homocysteine + 3-amino-2-hydroxy-4-methoxybenzoate
For diagram of reaction, click here
Glossary: cremeomycin = 6-carboxy-2-diazonio-3-methoxyphenolate
Other name(s): creN (gene name)
Systematic name: S-adenosyl-L-methionine:3-amino-4-hydroxybenzoate 4-O-methyltransferase
Comments: The enzyme, characterized from the bacterium Streptomyces cremeus, is involved in cremeomycin biosynthesis.
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References:
1. Waldman, A.J., Pechersky, Y., Wang, P., Wang, J.X. and Balskus, E.P. The cremeomycin biosynthetic gene cluster encodes a pathway for diazo formation. Chembiochem 16 (2015) 2172-2175. [PMID: 26278892]
EC 2.1.1.381
Accepted name: arginine Nω-methyltransferase
Reaction: S-adenosyl-L-methionine + L-arginine = S-adenosyl-L-homocysteine + Nω-methyl-L-arginine
Other name(s): sznE (gene name); stzE (gene name)
Systematic name: S-adenosyl-L-methionine:L-arginine Nω-methyltransferase
Comments: The enzyme, characterized from the bacterium Streptomyces achromogenes subsp. streptozoticus, participates in the biosynthesis of the glucosamine-nitrosourea antibiotic streptozotocin.
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References:
1. Ng, T.L., Rohac, R., Mitchell, A.J., Boal, A.K. and Balskus, E.P. An N-nitrosating metalloenzyme constructs the pharmacophore of streptozotocin. Nature 566 (2019) 94-99. [PMID: 30728519]
2. He, H.Y., Henderson, A.C., Du, Y.L. and Ryan, K.S. Two-enzyme pathway links l-arginine to nitric oxide in N-nitroso biosynthesis. J. Am. Chem. Soc. 141 (2019) 4026-4033. [PMID: 30763082]
EC 2.1.1.382
Accepted name: methoxylated aromatic compound—corrinoid protein Co-methyltransferase
Reaction: a methoxylated aromatic compound + a [Co(I) methoxylated-aromatic-compound-specific corrinoid protein] = a [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein] + a phenol
Other name(s): mtoB (gene name); mtvB (gene name); vdmB (gene name)
Systematic name: methoxylated aromatic compound:cobamide Co-methyltransferase
Comments: This entry stands for a family of enzymes that have been characterized from acetogenic bacteria and archaeal species. Different members of this family have different substrate specificity. In the methanogenic archaeon Methermicoccus shengliensis the enzyme participates in methanogenesis from methoxylated aromatic compounds, while in acetogenic bacteria and in non-methanogenic archaea it participates in methoxydotrophic growth. Most of the enzymes have a wide specificity and were shown to act on a large number of methoxylated aromatic compounds, carrying a methoxy group at positions 2, 3 or 4 of the aromatic ring. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state; during methylation the cobalt is oxidized to the Co(III) state.
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References:
1. Kaufmann, F., Wohlfarth, G. and Diekert, G. O-demethylase from Acetobacterium dehalogenans—substrate specificity and function of the participating proteins. Eur. J. Biochem. 253 (1998) 706-711. [PMID: 9654069]
2. Engelmann, T., Kaufmann, F. and Diekert, G. Isolation and characterization of a veratrol:corrinoid protein methyl transferase from Acetobacterium dehalogenans. Arch. Microbiol. 175 (2001) 376-383. [PMID: 11409548]
3. Naidu, D. and Ragsdale, S.W. Characterization of a three-component vanillate O-demethylase from Moorella thermoacetica. J. Bacteriol. 183 (2001) 3276-3281. [PMID: 11344134]
4. Pierce, E., Xie, G., Barabote, R.D., Saunders, E., Han, C.S., Detter, J.C., Richardson, P., Brettin, T.S., Das, A., Ljungdahl, L.G. and Ragsdale, S.W. The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum). Environ. Microbiol. 10 (2008) 2550-2573. [PMID: 18631365]
5. Kurth, J.M., Nobu, M.K., Tamaki, H., de Jonge, N., Berger, S., Jetten, M.SM., Yamamoto, K., Mayumi, D., Sakata, S., Bai, L., Cheng, L., Nielsen, J.L., Kamagata, Y., Wagner, T. and Welte, C.U. Methanogenic archaea use a bacteria-like methyltransferase system to demethoxylate aromatic compounds. ISME J. 15 (2021) 3549-3565. [PMID: 34145392]
6. Welte, C.U., de Graaf, R., Dalcin Martins, P., Jansen, R.S., Jetten, M.SM. and Kurth, J.M. A novel methoxydotrophic metabolism discovered in the hyperthermophilic archaeon Archaeoglobus fulgidus. Environ. Microbiol. 23 (2021) 4017-4033. [PMID: 33913565]
EC 2.1.1.383
Accepted name: L-carnitine—corrinoid protein Co-methyltransferase
Reaction: L-carnitine + a [Co(I) quaternary-amine-specifc corrinoid protein] = a [methyl-Co(III) quaternary-amine-specific corrinoid protein] + L-norcarnitine
Glossary: L-norcarnitine = (3R)-4-(dimethylamino)-3-hydroxybutanoate
Other name(s): mtcB (gene name)
Systematic name: L-carnitine:[Co(I) quaternary-amine-specifc corrinoid protein] Co-methyltransferase
Comments: The enzyme, characterized from the bacterium Eubacterium limosum, is a component of a system that transfers a methyl group from L-carnitine to tetrahydrofolate, as part of an L-carnitine degradation pathway. The resulting 5-methyltetrahydrofolate is processed to acetyl-CoA via the Wood—Ljungdahl pathway.
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BRENDA,
EXPASY,
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MetaCyc,
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References:
1. Kountz, D.J., Behrman, E.J., Zhang, L. and Krzycki, J.A. MtcB, a member of the MttB superfamily from the human gut acetogen Eubacterium limosum, is a cobalamin-dependent carnitine demethylase. J. Biol. Chem. 295 (2020) 11971-11981. [PMID: 32571881]
EC 2.1.1.384
Accepted name: [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein]—tetrahydromethanopterin methyltransferase
Reaction: [a methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein] + tetrahydromethanopterin = N5-methyltetrahydromethanopterin + a [Co(I) methoxylated-aromatic-compound-specific corrinoid protein]
Other name(s): mtoA (gene name)
Systematic name: [methylated methoxylated-aromatic-compound-specific corrinoid protein]:tetrahydromethanopterin methyltransferase
Comments: The enzyme has been characterized from several archaeal species. In the methanogenic archaeon Methermicoccus shengliensis the enzyme participates in methanogenesis from methoxylated aromatic compounds, while in the non-methanogenic Archaeoglobus fulgidus it participates in methoxydotrophic growth. The enzyme catalyses the transfer of a methyl group bound to the cobalt cofactor of a dedicated corrinoid protein (MtoC) to tetrahydromethanopterin or tetrahydrosarcinapterin. cf. EC 2.1.1.385, [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein]—tetrahydrofolate methyltransferase.
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EXPASY,
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MetaCyc,
CAS registry number:
References:
1. Kurth, J.M., Nobu, M.K., Tamaki, H., de Jonge, N., Berger, S., Jetten, M.SM., Yamamoto, K., Mayumi, D., Sakata, S., Bai, L., Cheng, L., Nielsen, J.L., Kamagata, Y., Wagner, T. and Welte, C.U. Methanogenic archaea use a bacteria-like methyltransferase system to demethoxylate aromatic compounds. ISME J. (2021) 3549-3565.
2. Welte, C.U., de Graaf, R., Dalcin Martins, P., Jansen, R.S., Jetten, M.SM. and Kurth, J.M. A novel methoxydotrophic metabolism discovered in the hyperthermophilic archaeon Archaeoglobus fulgidus. Environ. Microbiol. (2021) .
EC 2.1.1.385
Accepted name: [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein]—tetrahydrofolate methyltransferase
Reaction: [a methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein] + tetrahydrofolate = N5-methyltetrahydrofolate + a [Co(I) methoxylated-aromatic-compound-specific corrinoid protein]
Other name(s): mtvA (gene name)
Systematic name: [methylated methoxylated-aromatic-compound-specific corrinoid protein]:tetrahydrofolaten methyltransferase
Comments: The enzyme, found in acetogenic bacteria, participates in a pathway for the degradation of methoxylated aromatic compounds (methoxydotrophic growth). The enzyme catalyses the transfer of a methyl group bound to the cobalt cofactor of a dedicated corrinoid protein (MtvC) to tetrahydrofolate. cf. EC 2.1.1.384, [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein]—tetrahydromethanopterin methyltransferase.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Kaufmann, F., Wohlfarth, G. and Diekert, G. O-demethylase from Acetobacterium dehalogenans—substrate specificity and function of the participating proteins. Eur. J. Biochem. 253 (1998) 706-711. [PMID: 9654069]
2. Naidu, D. and Ragsdale, S.W. Characterization of a three-component vanillate O-demethylase from Moorella thermoacetica. J. Bacteriol. 183 (2001) 3276-3281. [PMID: 11344134]
3. Pierce, E., Xie, G., Barabote, R.D., Saunders, E., Han, C.S., Detter, J.C., Richardson, P., Brettin, T.S., Das, A., Ljungdahl, L.G. and Ragsdale, S.W. The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum). Environ. Microbiol. 10 (2008) 2550-2573. [PMID: 18631365]
EC 2.1.1.386
Accepted name: small RNA 2'-O-methyltransferase
Reaction: S-adenosyl-L-methionine + an [sRNA]-3'-end ribonucleotide = S-adenosyl-L-homocysteine + an [sRNA]-3'-end 2'-O-methylated ribonucleotide
Glossary: sRNA = small RNA
Other name(s): HENMT1 (gene name); HEN1 (gene name)
Systematic name: S-adenosyl-L-methionine:[sRNA]-3'-end ribonucleotide 2'-O-methyltransferase
Comments: The enzyme adds a 2'-O-methyl group to the ribose of the last nucleotide in several types of small RNAs (sRNAs), protecting the 3'-end of sRNAs from uridylation activity and subsequent degradation.
Links to other databases:
BRENDA,
EXPASY,
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References:
1. Park, W., Li, J., Song, R., Messing, J. and Chen, X. CARPEL FACTORY, a Dicer homolog, and HEN1, a novel protein, act in microRNA metabolism in Arabidopsis thaliana. Curr. Biol. 12 (2002) 1484-1495. [PMID: 12225663]
2. Yu, B., Yang, Z., Li, J., Minakhina, S., Yang, M., Padgett, R.W., Steward, R. and Chen, X. Methylation as a crucial step in plant microRNA biogenesis. Science 307 (2005) 932-935. [PMID: 15705854]
3. Kirino, Y. and Mourelatos, Z. 2'-O-methyl modification in mouse piRNAs and its methylase. Nucleic Acids Symp Ser (Oxf) (2007) 417-418. [PMID: 18029764]
4. Huang, Y., Ji, L., Huang, Q., Vassylyev, D.G., Chen, X. and Ma, J.B. Structural insights into mechanisms of the small RNA methyltransferase HEN1. Nature 461 (2009) 823-827. [PMID: 19812675]
5. Peng, L., Zhang, F., Shang, R., Wang, X., Chen, J., Chou, J.J., Ma, J., Wu, L. and Huang, Y. Identification of substrates of the small RNA methyltransferase Hen1 in mouse spermatogonial stem cells and analysis of its methyl-transfer domain. J. Biol. Chem. 293 (2018) 9981-9994. [PMID: 29703750]
EC 2.1.1.387
Accepted name: 5-dehydro-6-demethoxy-6-hydroxyfumagillol O-methyltransferase
Reaction: S-adenosyl-L-methionine + 5-dehydro-6-demethoxy-6-hydroxyfumagillol = S-adenosyl-L-homocysteine + 5-dehydrofumagillol
For diagram of reaction click here
Glossary: fumagillol = (3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-1-oxaspiro[2.5]octan-6-ol
Other name(s): Fma-MT; fmaD (gene name); af390-400 (gene name)
Systematic name: S-adenosyl-L-methionine:5-dehydro-6-demethoxy-6-hydroxyfumagillol 6-O-methyltransferase
Comments: The enzyme, characterized from the mold Aspergillus fumigatus, participates in the biosynthesis of the meroterpenoid fumagillin.
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References:
1. Lin, H.C., Tsunematsu, Y., Dhingra, S., Xu, W., Fukutomi, M., Chooi, Y.H., Cane, D.E., Calvo, A.M., Watanabe, K. and Tang, Y. Generation of complexity in fungal terpene biosynthesis: discovery of a multifunctional cytochrome P450 in the fumagillin pathway. J. Am. Chem. Soc. 136 (2014) 4426-4436. [PMID: 24568283]
EC 2.1.1.388
Accepted name: proline betaine—corrinoid protein Co-methyltransferase
Reaction: L-proline betaine + a [Co(I) quaternary-amine-specific corrinoid protein] = a [methyl-Co(III) quaternary-amine-specific corrinoid protein] + N-methyl-L-proline
Glossary: L-proline betaine = (2S)-1,1-dimethylpyrrolidinium-2-carboxylate
Other name(s): mtpB (gene name)
Systematic name: L-proline betaine:[Co(I) quaternary-amine-specific corrinoid protein] Co-methyltransferase
Comments: The enzyme, characterized from the bacterium Eubacterium limosum, is a component of a system that transfers a methyl group from L-proline betaine to tetrahydrofolate, as part of an L-proline betaine degradation pathway. The resulting 5-methyltetrahydrofolate is processed to acetyl-CoA via the Wood—Ljungdahl pathway.
Links to other databases:
BRENDA,
EXPASY,
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MetaCyc,
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References:
1. Picking, J.W., Behrman, E.J., Zhang, L. and Krzycki, J.A. MtpB, a member of the MttB superfamily from the human intestinal acetogen Eubacterium limosum, catalyzes proline betaine demethylation. J. Biol. Chem. 294 (2019) 13697-13707. [PMID: 31341018]
EC 2.1.1.389
Accepted name: [methyl-Co(III) quaternary-amine-specific corrinoid protein]—tetrahydrofolate methyltransferase
Reaction: [a methyl-Co(III) quaternary-amine-specific corrinoid protein] + tetrahydrofolate = N5-methyltetrahydrofolate + a [Co(I) quaternary-amine-specific corrinoid protein]
Other name(s): mtqA (gene name) (ambiguous); [methyl-Co(III) MtqC corrinoid protein]—tetrahydrofolate methyltransferase
Systematic name: [methylated quaternary-amine-specific corrinoid protein]:tetrahydrofolate methyltransferase
Comments: The enzyme, characterized from the acetogenic gut bacterium Eubacterium limosum, participates in a pathway for the degradation of some quaternary amine compounds (L-proline betaine and L-carnitine). The enzyme catalyses the transfer of a methyl group bound to the cobalt cofactor of a dedicated corrinoid protein (bacterial MtqC) to tetrahydrofolate. The resulting 5-methyltetrahydrofolate is processed to acetyl-CoA via the Wood—Ljungdahl pathway.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Picking, J.W., Behrman, E.J., Zhang, L. and Krzycki, J.A. MtpB, a member of the MttB superfamily from the human intestinal acetogen Eubacterium limosum, catalyzes proline betaine demethylation. J. Biol. Chem. 294 (2019) 13697-13707. [PMID: 31341018]
2. Kountz, D.J., Behrman, E.J., Zhang, L. and Krzycki, J.A. MtcB, a member of the MttB superfamily from the human gut acetogen Eubacterium limosum, is a cobalamin-dependent carnitine demethylase. J. Biol. Chem. 295 (2020) 11971-11981. [PMID: 32571881]
EC 2.1.1.390
Accepted name: gentamicin X2 methyltransferase
Reaction: gentamicin X2 + 2 S-adenosyl-L-methionine + reduced acceptor = geneticin + 5'-deoxyadenosine + L-methionine + S-adenosyl-L-homocysteine + oxidized acceptor (overall reaction)
Glossary: geneticin = G418 = (1R,2S,3S,4R,6S)-4,6-diamino-3-{[3-deoxy-4-C-methyl-3-(methylamino)-β-L-arabinopyranosyl]oxy}-2-hydroxycyclohexyl 2-amino-2,7-dideoxy-D-glycero-α-D-gluco-heptopyranoside
Other name(s): genK (gene name); gntK (gene name); gentamicin C-methyltransferase (ambiguous)
Systematic name: S-adenosyl-L-methionine:gentamicin X2 C6'-methyltransferase
Comments: The enzyme, isolated from the bacterium Micromonospora echinospora, has a single [4Fe-4S] cluster per monomer. It is a radical S-adenosyl-L-methionine (SAM) enzyme with a methylcob(III)alamin cofactor. The enzyme uses two molecues of SAM for the reaction. One molecule forms a 5'-deoxyadenosyl radical, while the other is used to methylate the cobalamin cofactor. It catalyses methylation of the 6'-carbon of gentamicin X2 (GenX2) to produce genetricin (G418) during the biosynthesis of gentamicins. The 6'-pro-R-hydrogen atom of GenX2 is stereoselectively abstracted by the 5'-deoxyadenosyl radical and methylation occurs with retention of configuration at C6'. The regeneration of cob(I)alamin from cob(III)alamin is carried out with an as yet unidentified electron donor.
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References:
1. Kim, J.Y., Suh, J.W., Kang, S.H., Phan, T.H., Park, S.H. and Kwon, H.J. Gene inactivation study of gntE reveals its role in the first step of pseudotrisaccharide modifications in gentamicin biosynthesis. Biochem Biophys Res Commun 372 (2008) 730-734. [PMID: 18533111]
2. Hong, W. and Yan, L. Identification of gntK, a gene required for the methylation of purpurosamine C-6' in gentamicin biosynthesis. J. Gen. Appl. Microbiol. 58 (2012) 349-356. [PMID: 23149679]
3. Kim, H.J., McCarty, R.M., Ogasawara, Y., Liu, Y.N., Mansoorabadi, S.O., LeVieux, J. and Liu, H.W. GenK-catalyzed C-6' methylation in the biosynthesis of gentamicin: isolation and characterization of a cobalamin-dependent radical SAM enzyme. J. Am. Chem. Soc. 135 (2013) 8093-8096. [PMID: 23679096]
4. Kim, H.J., Liu, Y.N., McCarty, R.M. and Liu, H.W. Reaction catalyzed by GenK, a cobalamin-dependent radical S-adenosyl-l-methionine methyltransferase in the biosynthetic pathway of gentamicin, proceeds with retention of configuration. J. Am. Chem. Soc. 139 (2017) 16084-16087. [PMID: 29091410]
EC 2.1.1.391
Accepted name: demethylgadusol O-methyltransferase
Reaction: S-adenosyl-L-methionine + demethylgadusol = S-adenosyl-L-homocysteine + gadusol
Glossary: demethylgadusol = (4R,5R)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohex-2-en-1-one
Other name(s): gadusol synthase; desmethyl gadusol O-methyltransferase
Systematic name: S-adenosyl-L-methionine:demethylgadusol 2-O-methyltransferase
Comments: The enzyme, present in egg-laying vertebrates, is involved in biosynthesis of the UV absorbing compound gadusol. It is a bifunctional enzyme that also catalyses EC 1.3.1.126, 2-epi-5-epi-valiolone dehydrogenase.
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References:
1. Osborn, A.R., Almabruk, K.H., Holzwarth, G., Asamizu, S., LaDu, J., Kean, K.M., Karplus, P.A., Tanguay, R.L., Bakalinsky, A.T. and Mahmud, T. De novo synthesis of a sunscreen compound in vertebrates. Elife 4 (2015) . [PMID: 25965179]
(2) S-adenosyl-L-methionine + reumycin = S-adenosyl-L-homocysteine + toxoflavin
toxoflavin = 1,6-dimethylpyrimido[5,4-e][1,2,4]triazine-5,7(1H,6H)-dione
(2) 2 S-adenosyl-L-methionine + a 2-demethylmenaquinone + reduced flavodoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + a 2-demethyl-8-methylmenaquinone + oxidized flavodoxin
nocamycin I = methyl (2R,3S,3aS,5R,6R,7S,9aS)-5-[(2R,3E,5E)-7-hydroxy-4-methyl-7-(2,4-dioxopyrroliden-3-ylidene)hepta-3,5-dien-2-yl]-2,6,9a-trimethyl-8-oxooctahydro-3a,7-epoxyfuro[3,2-b]oxocine-3-carboxylate
3-O-acetylpapaveroxine = 6-{(S)-acetoxy[(5R)-4-methoxy-6-methyl-5,6,7,8-tetrahydro[1,3]dioxolo[4,5-g]isoquinolin-5-yl]methyl}-2,3-dimethoxybenzaldehyde
aureothin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E)-2-methyl-3-(4-nitrophenyl)prop-2-en-1-ylidene]oxolan-2-yl]-4H-pyran-4-one
spectinabilin = neoaureothin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E,4E,6E)-2,4,6-trimethyl-7-(4-nitrophenyl)hepta-2,4,6-trien-1-ylidene]oxolan-2-yl]-4H-pyran-4-one
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine4 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine4
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine4 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine4
(1c) S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine4 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine4
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
(1c) S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
(1c) S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
(1c) S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine79 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine79
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine79 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine79
(1c) S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine79 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine-79
sodorifen = (1S,2S,4R,5S,8s)-1,2,4,5,6,7,8-heptamethyl-3-methylenebicyclo[3.2.1]oct-6-ene
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine4 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine4
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine4 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine4
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
(1a) S-adenosyl-L-methionine + a [histone H4]-L-lysine20 = S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
(1b) S-adenosyl-L-methionine + a [histone H4]-N6-methyl-L-lysine20 = S-adenosyl-L-homocysteine + a [histone H4]-N6,N6-dimethyl-L-lysine20
(1c) S-adenosyl-L-methionine + a [histone H4]-N6,N6-dimethyl-L-lysine20 = S-adenosyl-L-homocysteine + a [histone H4]-N6,N6,N6-trimethyl-L-lysine20
(1a) S-adenosyl-L-methionine + G(5')pppAACA-[mRNA] = S-adenosyl-L-homocysteine + G(5')pppAmACA-[mRNA]
(1b) S-adenosyl-L-methionine + G(5')pppAmACA-[mRNA] = S-adenosyl-L-homocysteine + m7G(5')pppAmACA-[mRNA]
(1a) S-adenosyl-L-methionine + cob(I)alamin = S-adenosyl-L-homocysteine + methylcob(III)alamin
(1b) methylcob(III)alamin + gentamicin X2 + S-adenosyl-L-methionine = cob(III)alamin + geneticin + 5'-deoxyadenosine + L-methionine
(1c) cob(III)alamin + reduced acceptor = cob(I)alamin + oxidized acceptor
gadusol = (4R,5R)-3,4,5-trihydroxy-5-(hydroxymethyl)-2-methoxycyclohex-2-en-1-one
Continued with EC 2.1.2.1 to EC 2.2.1.4
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