EC 2.1.1.1 to EC 2.1.1.50EC 2.1.1.151 to EC 2.1.1.200 EC 2.1.1.201 to EC 2.1.1.250 See separate file for EC 2.1.1.301 to EC 2.1.1.396.
EC 2.1.1.51 to EC 2.1.1.100
EC 2.1.1.101 to EC 2.1.1.150
EC 2.1.1.301 to EC 2.1.1.396
Accepted name: methylated-thiol—coenzyme M methyltransferase
Reaction: methanethiol + CoM = methyl-CoM + hydrogen sulfide (overall reaction)
(1a) methanethiol + a [Co(I) methylated--thiol-specific corrinoid protein] = a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
(1b) a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + coenzyme M = methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein]
Glossary: CoM = coenzyme M = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated)
Other name(s): mtsA (gene name)
Systematic name: methylated-thiol:coenzyme M methyltransferase
Comments: The enzyme, which is involved in methanogenesis from methylated thiols, such as methane thiol, dimethyl sulfide, and 3-S-methylmercaptopropionate, catalyses two successive steps - the transfer of a methyl group from the substrate to the cobalt cofactor of a methylated-thiol-specific corrinoid protein (MtsB), and the subsequent transfer of the methyl group from the corrinoid protein to coenzyme M. With most other methanogenesis substrates this process is carried out by two different enzymes (for example, EC 2.1.1.90, methanol—corrinoid protein Co-methyltransferase, and EC 2.1.1.246, methylated methanol-specific corrinoid protein:coenzyme M methyltransferase). The cobalt is oxidized during methylation from the Co(I) state to the Co(III) state, and is reduced back to the Co(I) form during demethylation.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Paul, L. and Krzycki, J.A. Sequence and transcript analysis of a novel Methanosarcina barkeri methyltransferase II homolog and its associated corrinoid protein homologous to methionine synthase. J. Bacteriol. 178 (1996) 6599-6607. [PMID: 8932317]
2. Tallant, T.C. and Krzycki, J.A. Methylthiol:coenzyme M methyltransferase from Methanosarcina barkeri, an enzyme of methanogenesis from dimethylsulfide and methylmercaptopropionate. J. Bacteriol. 179 (1997) 6902-6911. [PMID: 9371433]
3. Tallant, T.C., Paul, L. and Krzycki, J.A. The MtsA subunit of the methylthiol:coenzyme M methyltransferase of Methanosarcina barkeri catalyses both half-reactions of corrinoid-dependent dimethylsulfide: coenzyme M methyl transfer. J. Biol. Chem. 276 (2001) 4485-4493. [PMID: 11073950]
Accepted name: tetramethylammonium—corrinoid protein Co-methyltransferase
Reaction: tetramethylammonium + a [(Co(I) tetramethylammonium-specific corrinoid protein] = a [methyl-Co(III) tetramethylammonium-specific corrinoid protein] + trimethylamine
Other name(s): mtqB (gene name); tetramethylammonium methyltransferase
Systematic name: tetramethylammonium:5-hydroxybenzimidazolylcobamide Co-methyltransferase
Comments: The enzyme, which catalyses the transfer of a methyl group from tetramethylammonium to a tetramethylammonium-specific corrinoid protein (MtqC), is involved in methanogenesis from tetramethylammonium. 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. The methylated corrinoid protein is substrate for EC 2.1.1.253, methylated tetramethylammonium-specific corrinoid protein:coenzyme M methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Asakawa, S., Sauer, K., Liesack, W. and Thauer, R.K. Tetramethylammonium:coenzyme M methyltransferase system from methanococcoides s. Arch. Microbiol. 170 (1998) 220-226. [PMID: 9732435]
Accepted name: [methyl-Co(III) tetramethylammonium-specific corrinoid protein]—coenzyme M methyltransferase
Reaction: a [methyl-Co(III) tetramethylammonium-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) tetramethylammonium-specific corrinoid protein]
Glossary: CoM = coenzyme M = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated)
Other name(s): methyltransferase 2 (ambiguous); mtqA (gene name)
Systematic name: methylated tetramethylammonium-specific corrinoid protein:Coenzyme M methyltransferase
Comments: The enzyme, which is involved in methanogenesis from tetramethylammonium, catalyses the transfer of a methyl group from a corrinoid protein (see EC 2.1.1.252, tetramethylammonium—corrinoid protein Co-methyltransferase), where it is bound to the cobalt cofactor, to coenzyme M, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Asakawa, S., Sauer, K., Liesack, W. and Thauer, R.K. Tetramethylammonium:coenzyme M methyltransferase system from methanococcoides s. Arch. Microbiol. 170 (1998) 220-226. [PMID: 9732435]
Accepted name: erythromycin 3"-O-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + erythromycin C = S-adenosyl-L-homocysteine + erythromycin A
(2) S-adenosyl-L-methionine + erythromycin D = S-adenosyl-L-homocysteine + erythromycin B
For diagram of reaction click here.
Other name(s): EryG
Systematic name: S-adenosyl-L-methionine:erythromycin C 3"-O-methyltransferase
Comments: The enzyme methylates the 3 position of the mycarosyl moiety of erythromycin C, forming the most active form of the antibiotic, erythromycin A. It can also methylate the precursor erythromycin D, forming erythromycin B, which is then converted to erythromycin A by EC 1.14.13.154, erythromycin 12-hydroxylase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Paulus, T.J., Tuan, J.S., Luebke, V.E., Maine, G.T., DeWitt, J.P. and Katz, L. Mutation and cloning of eryG, the structural gene for erythromycin O-methyltransferase from Saccharopolyspora erythraea, and expression of eryG in Escherichia coli. J. Bacteriol. 172 (1990) 2541-2546. [PMID: 2185226]
2. Summers, R.G., Donadio, S., Staver, M.J., Wendt-Pienkowski, E., Hutchinson, C.R. and Katz, L. Sequencing and mutagenesis of genes from the erythromycin biosynthetic gene cluster of Saccharopolyspora erythraea that are involved in L-mycarose and D-desosamine production. Microbiology 143 (1997) 3251-3262. [PMID: 9353926]
Accepted name: geranyl diphosphate 2-C-methyltransferase
Reaction: S-adenosyl-L-methionine + geranyl diphosphate = S-adenosyl-L-homocysteine + (E)-2-methylgeranyl diphosphate
For diagram of reaction click here and mechanism click here.
Other name(s): SCO7701; GPP methyltransferase; GPPMT; 2-methyl-GPP synthase; MGPPS; geranyl pyrophosphate methyltransferase
Systematic name: S-adenosyl-L-methionine:geranyl-diphosphate 2-C-methyltransferase
Comments: This enzyme, along with EC 4.2.3.118, 2-methylisoborneol synthase, produces 2-methylisoborneol, an odiferous compound produced by soil microorganisms with a strong earthy/musty odour.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Wang, C.M. and Cane, D.E. Biochemistry and molecular genetics of the biosynthesis of the earthy odorant methylisoborneol in Streptomyces coelicolor. J. Am. Chem. Soc. 130 (2008) 8908-8909. [PMID: 18563898]
2. Ariyawutthiphan, O., Ose, T., Tsuda, M., Gao, Y., Yao, M., Minami, A., Oikawa, H. and Tanaka, I. Crystallization and preliminary X-ray crystallographic study of a methyltransferase involved in 2-methylisoborneol biosynthesis in Streptomyces lasaliensis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 (2011) 417-420. [PMID: 21393856]
3. Komatsu, M., Tsuda, M., Omura, S., Oikawa, H. and Ikeda, H. Identification and functional analysis of genes controlling biosynthesis of 2-methylisoborneol. Proc. Natl. Acad. Sci. USA 105 (2008) 7422-7427. [PMID: 18492804]
4. Giglio, S., Chou, W.K., Ikeda, H., Cane, D.E. and Monis, P.T. Biosynthesis of 2-methylisoborneol in cyanobacteria. Environ. Sci. Technol. 45 (2011) 992-998. [PMID: 21174459]
Accepted name: tRNA (guanine6-N2)-methyltransferase
Reaction: S-adenosyl-L-methionine + guanine6 in tRNA = S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA
Other name(s): methyltransferase Trm14; m2G6 methyltransferase
Systematic name: S-adenosyl-L-methionine:tRNA (guanine6-N2)-methyltransferase
Comments: The enzyme specifically methylates guanine6 at N2 in tRNA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Menezes, S., Gaston, K.W., Krivos, K.L., Apolinario, E.E., Reich, N.O., Sowers, K.R., Limbach, P.A. and Perona, J.J. Formation of m2G6 in Methanocaldococcus jannaschii tRNA catalyzed by the novel methyltransferase Trm14. Nucleic Acids Res. 39 (2011) 7641-7655. [PMID: 21693558]
Accepted name: tRNA (pseudouridine54-N1)-methyltransferase
Reaction: S-adenosyl-L-methionine + pseudouridine54 in tRNA = S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNA
Other name(s): TrmY; m1Ψ methyltransferase
Systematic name: S-adenosyl-L-methionine:tRNA (pseudouridine54-N1)-methyltransferase
Comments: While this archaeal enzyme is specific for the 54 position and does not methylate pseudouridine at position 55, the presence of pseudouridine at position 55 is necessary for the efficient methylation of pseudouridine at position 54 [2,3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Chen, H.Y. and Yuan, Y.A. Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase. J. Mol. Cell. Biol. 2 (2010) 366-374. [PMID: 21098051]
2. Wurm, J.P., Griese, M., Bahr, U., Held, M., Heckel, A., Karas, M., Soppa, J. and Wohnert, J. Identification of the enzyme responsible for N1-methylation of pseudouridine 54 in archaeal tRNAs. RNA 18 (2012) 412-420. [PMID: 22274954]
3. Chatterjee, K., Blaby, I.K., Thiaville, P.C., Majumder, M., Grosjean, H., Yuan, Y.A., Gupta, R. and de Crecy-Lagard, V. The archaeal COG1901/DUF358 SPOUT-methyltransferase members, together with pseudouridine synthase Pus10, catalyze the formation of 1-methylpseudouridine at position 54 of tRNA. RNA 18 (2012) 421-433. [PMID: 22274953]
Accepted name: 5-methyltetrahydrofolate—corrinoid/iron-sulfur protein Co-methyltransferase
Reaction: a [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
Other name(s): acsE (gene name)
Systematic name: 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase
Comments: Catalyses the transfer of a methyl group from the N5 group of methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein. Involved, together with EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin) and EC 2.3.1.169, CO-methylating acetyl-CoA synthase, in the reductive acetyl coenzyme A (Wood-Ljungdahl) pathway of autotrophic carbon fixation in various bacteria and archaea.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Roberts, D.L., Zhao, S., Doukov, T. and Ragsdale, S.W. The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum. J. Bacteriol. 176 (1994) 6127-6130. [PMID: 7928975]
2. Doukov, T., Seravalli, J., Stezowski, J.J. and Ragsdale, S.W. Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase. Structure 8 (2000) 817-830. [PMID: 10997901]
3. Doukov, T.I., Hemmi, H., Drennan, C.L. and Ragsdale, S.W. Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases. J. Biol. Chem. 282 (2007) 6609-6618. [PMID: 17172470]
Accepted name: [fructose-bisphosphate aldolase]-lysine N-methyltransferase
Reaction: 3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine = 3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
Other name(s): rubisco methyltransferase; ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase; ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit εN-methyltransferase; S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine 6-N-methyltransferase
Systematic name: S-adenosyl-L-methionine:[fructose-bisphosphate aldolase]-lysine N6-methyltransferase
Comments: The enzyme methylates a conserved lysine in the C-terminal part of higher plant fructose-bisphosphate aldolase (EC 4.1.2.13). The enzyme from pea (Pisum sativum) also methylates Lys-14 in the large subunits of hexadecameric higher plant ribulose-bisphosphate-carboxylase (EC 4.1.1.39) [2], but that from Arabidopsis thaliana does not.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Magnani, R., Nayak, N.R., Mazarei, M., Dirk, L.M. and Houtz, R.L. Polypeptide substrate specificity of PsLSMT. A set domain protein methyltransferase. J. Biol. Chem. 282 (2007) 27857-27864. [PMID: 17635932]
2. Mininno, M., Brugiere, S., Pautre, V., Gilgen, A., Ma, S., Ferro, M., Tardif, M., Alban, C. and Ravanel, S. Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants. J. Biol. Chem. 287 (2012) 21034-21044. [PMID: 22547063]
Accepted name: rRNA small subunit pseudouridine methyltransferase Nep1
Reaction: S-adenosyl-L-methionine + pseudouridine1191 in yeast 18S rRNA = S-adenosyl-L-homocysteine + N1-methylpseudouridine1191 in yeast 18S rRNA
Other name(s): Nep1; nucleolar essential protein 1
Systematic name: S-adenosyl-L-methionine:18S rRNA (pseudouridine1191-N1)-methyltransferase
Comments: This enzyme, which occurs in both prokaryotes and eukaryotes, recognizes specific pseudouridine residues (Ψ) in small subunits of ribosomal RNA based on the local RNA structure. It recognizes Ψ914 in 16S rRNA from the archaeon Methanocaldococcus jannaschii, Ψ1191 in yeast 18S rRNA, and Ψ1248 in human 18S rRNA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Taylor, A.B., Meyer, B., Leal, B.Z., Kötter, P., Schirf, V., Demeler, B., Hart, P.J., Entian, K.-D. and Wöhnert, J. The crystal structure of Nep1 reveals an extended SPOUT-class methyltransferase fold and a pre-organized SAM-binding site. Nucleic Acids Res. 36 (2008) 1542-1554. [PMID: 18208838]
2. Wurm, J.P., Meyer, B., Bahr, U., Held, M., Frolow, O., Kötter, P., Engels, J.W., Heckel, A., Karas, M., Entian, K.-D. and Wöhnert, J. The ribosome assembly factor Nep1 responsible for Bowen-Conradi syndrome is a pseudouridine-N1-specific methyltransferase. Nucleic Acids Res. 38 (2010) 2387-2398. [PMID: 20047967]
3. Meyer, B., Wurm, J.P., Kötter, P., Leisegang, M.S., Schilling, V., Buchhaupt, M., Held, M., Bahr, U., Karas, M., Heckel, A., Bohnsack, M.T., Wöhnert, J. and Entian, K.-D. The Bowen-Conradi syndrome protein Nep1 (Emg1) has a dual role in eukaryotic ribosome biogenesis, as an essential assembly factor and in the methylation of Ψ1191 in yeast 18S rRNA. Nucleic Acids Res. 39 (2011) 1526-1537. [PMID: 20972225]
Accepted name: 4-dimethylallyltryptophan N-methyltransferase
Reaction: S-adenosyl-L-methionine + 4-prenyl-L-tryptophan = S-adenosyl-L-homocysteine + 4-prenyl-L-abrine
For diagram of reaction click here.
Glossary: 4-prenyl-L-tryptophan = 4-(3-methylbut-2-enyl)-L-tryptophan = 4-dimethylallyl-L-tryptophan (ambiguous);
4-prenyl-L-abrine = 4-(3-methylbut-2-enyl)-L-abrine = 4-dimethylallyl-L-abrine (ambiguous)
Other name(s): fgaMT (gene name); easF (gene name)
Systematic name: S-adenosyl-L-methionine:4-(3-methylbut-2-enyl)-L-tryptophan N-methyltransferase
Comments: The enzyme catalyses a step in the pathway leading to biosynthesis of ergot alkaloids in certain fungi.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Rigbers, O. and Li, S.M. Ergot alkaloid biosynthesis in Aspergillus fumigatus. Overproduction and biochemical characterization of a 4-dimethylallyltryptophan N-methyltransferase. J. Biol. Chem. 283 (2008) 26859-26868. [PMID: 18678866]
Accepted name: squalene methyltransferase
Reaction: 2 S-adenosyl-L-methionine + squalene = 2 S-adenosyl-L-homocysteine + 3,22-dimethyl-1,2,23,24-tetradehydro-2,3,22,23-tetrahydrosqualene (overall reaction)
(1a) S-adenosyl-L-methionine + squalene = S-adenosyl-L-homocysteine + 3-methyl-1,2-didehydro-2,3-dihydrosqualene
(1b) S-adenosyl-L-methionine + 3-methyl-1,2-didehydro-2,3-dihydrosqualene = S-adenosyl-L-homocysteine + 3,22-dimethyl-1,2,23,24-tetradehydro-2,3,22,23-tetrahydrosqualene
For diagram of reaction click here.
Other name(s): TMT-1; TMT-2
Systematic name: S-adenosyl-L-methionine:squalene C-methyltransferase
Comments: Two isoforms differing in their specificity were isolated from the green alga Botryococcus braunii BOT22. TMT-1 gave more of the dimethylated form whereas TMT2 gave more of the monomethylated form.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Niehaus, T.D., Kinison, S., Okada, S., Yeo, Y.S., Bell, S.A., Cui, P., Devarenne, T.P. and Chappell, J. Functional identification of triterpene methyltransferases from Botryococcus braunii race B. J. Biol. Chem. 287 (2012) 8163-8173. [PMID: 22241476]
Accepted name: botryococcene C-methyltransferase
Reaction: 2 S-adenosyl-L-methionine + C30 botryococcene = 2 S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene (overall reaction)
(1a) S-adenosyl-L-methionine + C30 botryococcene = S-adenosyl-L-homocysteine + 3-methyl-1,2-didehydro-2,3-dihydrobotryococcene
(1b) S-adenosyl-L-methionine + 3-methyl-1,2-didehydro-2,3-dihydrobotryococcene = S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene
(2a) S-adenosyl-L-methionine + C30 botryococcene = S-adenosyl-L-homocysteine + 20-methyl-21,22-didehydro-20,21-dihydrobotryococcene
(2b) S-adenosyl-L-methionine + 20-methyl-21,22-didehydro-20,21-dihydrobotryococcene = S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene
For diagram of reaction click here.
Glossary: C30 botryococcene = (10S,13R)-10-ethenyl-2,6,10,13,17,21-hexamethyldocosa-2,5,11,16,20-pentaene
3-methyl-1,2-didehydro-2,3-dihydrobotryococcene = showacene
20-methyl-21,22-didehydro-20,21-dihydrobotryococcene = isoshowacene
Other name(s): TMT-3
Systematic name: S-adenosyl-L-methionine:botryococcene C-methyltransferase
Comments: Isolated from the green alga Botryococcus braunii BOT22. Shows a very weak activity with squalene.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Niehaus, T.D., Kinison, S., Okada, S., Yeo, Y.S., Bell, S.A., Cui, P., Devarenne, T.P. and Chappell, J. Functional identification of triterpene methyltransferases from Botryococcus braunii race B. J. Biol. Chem. 287 (2012) 8163-8173. [PMID: 22241476]
Accepted name: 23S rRNA (guanine2069-N7)-methyltransferase
Reaction: S-adenosyl-L-methionine + guanine2069 in 23S rRNA = S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
Other name(s): rlmK (gene name); 23S rRNA m7G2069 methyltransferase
Systematic name: S-adenosyl-L-methionine:23S rRNA (guanine2069-N7)-methyltransferase
Comments: The enzyme specifically methylates guanine2069 at position N7 in 23S rRNA. In γ-proteobacteria the enzyme also catalyses EC 2.1.1.173, 23S rRNA (guanine2445-N2)-methyltransferase, while in β-proteobacteria the activities are carried out by separate proteins [1]. The enzyme from the γ-proteobacterium Escherichia coli has RNA unwinding activity as well [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Kimura, S., Ikeuchi, Y., Kitahara, K., Sakaguchi, Y., Suzuki, T. and Suzuki, T. Base methylations in the double-stranded RNA by a fused methyltransferase bearing unwinding activity. Nucleic Acids Res. 40 (2012) 4071-4085. [PMID: 22210896]
Accepted name: tellurite methyltransferase
Reaction: S-adenosyl-L-methionine + tellurite = S-adenosyl-L-homocysteine + methanetelluronate
Other name(s): TehB
Systematic name: S-adenosyl-L-methionine:tellurite methyltransferase
Comments: The enzyme is involved in the detoxification of tellurite. It can also methylate selenite and selenium dioxide.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Liu, M., Turner, R.J., Winstone, T.L., Saetre, A., Dyllick-Brenzinger, M., Jickling, G., Tari, L.W., Weiner, J.H. and Taylor, D.E. Escherichia coli TehB requires S-adenosylmethionine as a cofactor to mediate tellurite resistance. J. Bacteriol. 182 (2000) 6509-6513. [PMID: 11053398]
2. Choudhury, H.G., Cameron, A.D., Iwata, S. and Beis, K. Structure and mechanism of the chalcogen-detoxifying protein TehB from Escherichia coli. Biochem. J. 435 (2011) 85-91. [PMID: 21244361]
Accepted name: 23S rRNA (adenine2030-N6)-methyltransferase
Reaction: S-adenosyl-L-methionine + adenine2030 in 23S rRNA = S-adenosyl-L-homocysteine + N6-methyladenine2030 in 23S rRNA
Other name(s): YhiR protein; rlmJ (gene name); m6A2030 methyltransferase
Systematic name: S-adenosyl-L-methionine:23S rRNA (adenine2030-N6)-methyltransferase
Comments: The recombinant RlmJ protein is most active in methylating deproteinized 23S ribosomal subunit, and does not methylate the completely assembled 50S subunits [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Golovina, A.Y., Dzama, M.M., Osterman, I.A., Sergiev, P.V., Serebryakova, M.V., Bogdanov, A.A. and Dontsova, O.A. The last rRNA methyltransferase of E. coli revealed: the yhiR gene encodes adenine-N6 methyltransferase specific for modification of A2030 of 23S ribosomal RNA. RNA 18 (2012) 1725-1734. [PMID: 22847818]
Accepted name: flavonoid 3',5'-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + a 3'-hydroxyflavonoid = S-adenosyl-L-homocysteine + a 3'-methoxyflavonoid
(2) S-adenosyl-L-methionine + a 5'-hydroxy-3'-methoxyflavonoid = S-adenosyl-L-homocysteine + a 3',5'-dimethoxyflavonoid
For diagram of reaction click here.
Glossary: delphinidin = 3,3',4',5,5',7-hexahydroxyflavylium
cyanidin = 3,3',4',5,7-pentahydroxyflavylium
myricetin = 3,3',4',5,5',7-hexahydroxyflavone
quercetin = 3,3',4',5,7-pentahydroxyflavone
Other name(s): AOMT; CrOMT2
Systematic name: S-adenosyl-L-methionine:flavonoid 3'-O-methyltransferase
Comments: Isolated from Vitis vinifera (grape) [2]. Most active with delphinidin 3-glucoside but also acts on cyanidin 3-glucoside, cyanidin, myricetin, quercetin and quercetin 3-glucoside. The enzyme from Catharanthus roseus was most active with myricetin [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Cacace, S., Schröder, G., Wehinger, E., Strack, D., Schmidt, J. and Schröder, J. A flavonol O-methyltransferase from Catharanthus roseus performing two sequential methylations. Phytochemistry 62 (2003) 127-137. [PMID: 12482447]
2. Hugueney, P., Provenzano, S., Verries, C., Ferrandino, A., Meudec, E., Batelli, G., Merdinoglu, D., Cheynier, V., Schubert, A. and Ageorges, A. A novel cation-dependent O-methyltransferase involved in anthocyanin methylation in grapevine. Plant Physiol. 150 (2009) 2057-2070. [PMID: 19525322]
Accepted name: tRNAThr (cytosine32-N3)-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + cytosine32 in tRNAThr = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
(2) S-adenosyl-L-methionine + cytosine32 in tRNASer = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
Other name(s): ABP140; Trm140p
Systematic name: S-adenosyl-L-methionine:tRNAThr (cytosine32-N3)-methyltransferase
Comments: The enzyme from Saccharomyces cerevisiae specifically methylates cytosine32 in tRNAThr and in tRNASer.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Noma, A., Yi, S., Katoh, T., Takai, Y., Suzuki, T. and Suzuki, T. Actin-binding protein ABP140 is a methyltransferase for 3-methylcytidine at position 32 of tRNAs in Saccharomyces cerevisiae. RNA 17 (2011) 1111-1119. [PMID: 21518805]
2. D'Silva, S., Haider, S.J. and Phizicky, E.M. A domain of the actin binding protein Abp140 is the yeast methyltransferase responsible for 3-methylcytidine modification in the tRNA anti-codon loop. RNA 17 (2011) 1100-1110. [PMID: 21518804]
Accepted name: dimethylsulfoniopropionate demethylase
Reaction: S,S-dimethyl-β-propiothetin + tetrahydrofolate = 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
For diagram of reaction click here.
Glossary: S,S-dimethyl-β-propiothetin = 3-(S,S-dimethylsulfonio)propanoate
Other name(s): dmdA (gene name); dimethylsulfoniopropionate-dependent demethylase A
Systematic name: S,S-dimethyl-β-propiothetin:tetrahydrofolate S-methyltransferase
Comments: The enzyme from the marine bacteria Pelagibacter ubique and Ruegeria pomeroyi are specific towards S,S-dimethyl-β-propiothetin. They do not demethylate glycine-betaine [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Jansen, M. and Hansen, T.A. Tetrahydrofolate serves as a methyl acceptor in the demethylation of dimethylsulfoniopropionate in cell extracts of sulfate-reducing bacteria. Arch. Microbiol. 169 (1998) 84-87. [PMID: 9396840]
2. Reisch, C.R., Moran, M.A. and Whitman, W.B. Dimethylsulfoniopropionate-dependent demethylase (DmdA) from Pelagibacter ubique and Silicibacter pomeroyi. J. Bacteriol. 190 (2008) 8018-8024. [PMID: 18849431]
3. Schuller, D.J., Reisch, C.R., Moran, M.A., Whitman, W.B. and Lanzilotta, W.N. Structures of dimethylsulfoniopropionate-dependent demethylase from the marine organism Pelagibacter ubique. Protein Sci. 21 (2012) 289-298. [PMID: 22162093]
Accepted name: (+)-6a-hydroxymaackiain 3-O-methyltransferase
Reaction: S-adenosyl-L-methionine + (+)-6a-hydroxymaackiain = S-adenosyl-L-homocysteine + (+)-pisatin
Glossary: (+)-6a-hydroxymaackiain = (6aR,12aR)-6H-[1,3]dioxolo[5,6][1]benzofuro[3,2-c]chromene-3,6a(12aH)-diol
(+)-pisatin = (6aR,12aR)-3-methoxy-6H-[1,3]dioxolo[5,6][1]benzofuro[3,2-c]chromen-6a(12aH)-ol
Other name(s): HM3OMT; HMM2
Systematic name: S-adenosyl-L-methionine:(+)-6a-hydroxymaackiain 3-O-methyltransferase
Comments: The protein from the plant Pisum sativum (garden pea) methylates (+)-6a-hydroxymaackiain at the 3-position. It also methylates 2,7,4'-trihydroxyisoflavanone on the 4'-position (cf. EC 2.1.1.212, 2,7,4-trihydroxyisoflavanone 4-O-methyltransferase) with lower activity.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Preisig, C.L., Matthews, D.E. and Vanetten, H.D. Purification and characterization of S-adenosyl-L-methionine:6a-hydroxymaackiain 3-O-methyltransferase from Pisum sativum. Plant Physiol. 91 (1989) 559-566. [PMID: 16667069]
2. Wu, Q., Preisig, C.L. and VanEtten, H.D. Isolation of the cDNAs encoding (+)6a-hydroxymaackiain 3-O-methyltransferase, the terminal step for the synthesis of the phytoalexin pisatin in Pisum sativum. Plant Mol. Biol. 35 (1997) 551-560. [PMID: 9349277]
3. Liu, C.J., Deavours, B.E., Richard, S.B., Ferrer, J.L., Blount, J.W., Huhman, D., Dixon, R.A. and Noel, J.P. Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses. Plant Cell 18 (2006) 3656-3669. [PMID: 17172354]
4. Akashi, T., VanEtten, H.D., Sawada, Y., Wasmann, C.C., Uchiyama, H. and Ayabe, S. Catalytic specificity of pea O-methyltransferases suggests gene duplication for (+)-pisatin biosynthesis. Phytochemistry 67 (2006) 2525-2530. [PMID: 17067644]
Accepted name: cobalt-precorrin-4 methyltransferase
Reaction: S-adenosyl-L-methionine + cobalt-precorrin-4 = S-adenosyl-L-homocysteine + cobalt-precorrin-5A
For diagram of reaction click here.
Other name(s): CbiF
Systematic name: S-adenosyl-L-methionine:cobalt-precorrin-4 11-methyltransferase
Comments: This enzyme, which participates in the anaerobic (early cobalt insertion) cobalamin biosynthesis pathway, catalyses the methylation of C-11 in cobalt-precorrin-4 to form cobalt-precorrin-5A. See EC 2.1.1.133, precorrin-4 C11-methyltransferase, for the equivalent enzyme that participates in the aerobic cobalamin biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Raux, E., Schubert, H.L., Woodcock, S.C., Wilson, K.S. and Warren, M.J. Cobalamin (vitamin B12) biosynthesis--cloning, expression and crystallisation of the Bacillus megaterium S-adenosyl-L-methionine-dependent cobalt-precorrin-4 transmethylase CbiF. Eur. J. Biochem. 254 (1998) 341-346. [PMID: 9660189]
2. Schubert, H.L., Wilson, K.S., Raux, E., Woodcock, S.C. and Warren, M.J. The X-ray structure of a cobalamin biosynthetic enzyme, cobalt-precorrin-4 methyltransferase. Nat. Struct. Biol. 5 (1998) 585-592. [PMID: 9665173]
3. Kajiwara, Y., Santander, P.J., Roessner, C.A., Perez, L.M. and Scott, A.I. Genetically engineered synthesis and structural characterization of cobalt-precorrin 5A and -5B, two new intermediates on the anaerobic pathway to vitamin B12: definition of the roles of the CbiF and CbiG enzymes. J. Am. Chem. Soc. 128 (2006) 9971-9978. [PMID: 16866557]
Accepted name: cobalt-factor III methyltransferase
Reaction: S-adenosyl-L-methionine + cobalt-factor III + reduced acceptor = S-adenosyl-L-homocysteine + cobalt-precorrin-4 + acceptor
For diagram of reaction click here.
Other name(s): CbiH60 (gene name)
Systematic name: S-adenosyl-L-methionine:cobalt-factor III 17-methyltransferase (ring contracting)
Comments: Isolated from the bacterium Bacillus megaterium. The enzyme, which participates in the anaerobic (early cobalt insertion) pathway of adenosylcobalamin biosynthesis, catalyses a crucial reaction where the tetrapyrrole ring contracts as a result of methylation of C-17. Contains a [4Fe-4S] cluster. It can also convert cobalt-precorrin-3 to cobalt-precorrin-4. The reductant may be thioredoxin. See EC 2.1.1.131, precorrin-3B C17-methyltransferase, for the corresponding enzyme that participates in the aerobic cobalamin biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Moore, S.J., Biedendieck, R., Lawrence, A.D., Deery, E., Howard, M.J., Rigby, S.E. and Warren, M.J. Characterization of the enzyme CbiH60 involved in anaerobic ring contraction of the cobalamin (vitamin B12) biosynthetic pathway. J. Biol. Chem. 288 (2013) 297-305. [PMID: 23155054]
Accepted name: benzoate O-methyltransferase
Reaction: S-adenosyl-L-methionine + benzoate = S-adenosyl-L-homocysteine + methyl benzoate
Other name(s): BAMT; S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase
Systematic name: S-adenosyl-L-methionine:benzoate O-methyltransferase
Comments: While the enzyme from the plant Zea mays is specific for benzoate [6], the enzymes from Arabidopsis species and Clarkia breweri also catalyse the reaction of EC 2.1.1.274, salicylate 1-O-methyltransferase [1,5]. In snapdragon (Antirrhinum majus) two isoforms are found, one specific for benzoate [2,3] and one that is also active towards salicylate [4]. The volatile product is an important scent compound in some flowering species [2].
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:
References:
1. Ross, J.R., Nam, K.H., D'Auria, J.C. and Pichersky, E. S-adenosyl-L-methionine:salicylic acid carboxyl methyltransferase, an enzyme involved in floral scent production and plant defense, represents a new class of plant methyltransferases. Arch. Biochem. Biophys. 367 (1999) 9-16. [PMID: 10375393]
2. Dudareva, N., Murfitt, L.M., Mann, C.J., Gorenstein, N., Kolosova, N., Kish, C.M., Bonham, C. and Wood, K. Developmental regulation of methyl benzoate biosynthesis and emission in snapdragon flowers. Plant Cell 12 (2000) 949-961. [PMID: 10852939]
3. Murfitt, L.M., Kolosova, N., Mann, C.J. and Dudareva, N. Purification and characterization of S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase, the enzyme responsible for biosynthesis of the volatile ester methyl benzoate in flowers of Antirrhinum majus. Arch. Biochem. Biophys. 382 (2000) 145-151. [PMID: 11051108]
4. Negre, F., Kolosova, N., Knoll, J., Kish, C.M. and Dudareva, N. Novel S-adenosyl-L-methionine:salicylic acid carboxyl methyltransferase, an enzyme responsible for biosynthesis of methyl salicylate and methyl benzoate, is not involved in floral scent production in snapdragon flowers. Arch. Biochem. Biophys. 406 (2002) 261-270. [PMID: 12361714]
5. Chen, F., D'Auria, J.C., Tholl, D., Ross, J.R., Gershenzon, J., Noel, J.P. and Pichersky, E. An Arabidopsis thaliana gene for methylsalicylate biosynthesis, identified by a biochemical genomics approach, has a role in defense. Plant J. 36 (2003) 577-588. [PMID: 14617060]
6. Köllner, T.G., Lenk, C., Zhao, N., Seidl-Adams, I., Gershenzon, J., Chen, F. and Degenhardt, J. Herbivore-induced SABATH methyltransferases of maize that methylate anthranilic acid using s-adenosyl-L-methionine. Plant Physiol. 153 (2010) 1795-1807. [PMID: 20519632]
Accepted name: salicylate 1-O-methyltransferase
Reaction: S-adenosyl-L-methionine + salicylate = S-adenosyl-L-homocysteine + methyl salicylate
Glossary: methyl salicylate = methyl 2-hydroxybenzoate
Other name(s): SAMT; S-adenosyl-L-methionine:salicylic acid carboxyl methyltransferase; salicylate carboxymethyltransferase
Systematic name: S-adenosyl-L-methionine:salicylate 1-O-methyltransferase
Comments: The enzyme, which is found in flowering plants, also has the activity of EC 2.1.1.273, benzoate O-methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, PDB, CAS registry number:
References:
1. Ross, J.R., Nam, K.H., D'Auria, J.C. and Pichersky, E. S-Adenosyl-L-methionine:salicylic acid carboxyl methyltransferase, an enzyme involved in floral scent production and plant defense, represents a new class of plant methyltransferases. Arch. Biochem. Biophys. 367 (1999) 9-16. [PMID: 10375393]
2. Negre, F., Kolosova, N., Knoll, J., Kish, C.M. and Dudareva, N. Novel S-adenosyl-L-methionine:salicylic acid carboxyl methyltransferase, an enzyme responsible for biosynthesis of methyl salicylate and methyl benzoate, is not involved in floral scent production in snapdragon flowers. Arch. Biochem. Biophys. 406 (2002) 261-270. [PMID: 12361714]
3. Chen, F., D'Auria, J.C., Tholl, D., Ross, J.R., Gershenzon, J., Noel, J.P. and Pichersky, E. An Arabidopsis thaliana gene for methylsalicylate biosynthesis, identified by a biochemical genomics approach, has a role in defense. Plant J. 36 (2003) 577-588. [PMID: 14617060]
4. Zubieta, C., Ross, J.R., Koscheski, P., Yang, Y., Pichersky, E. and Noel, J.P. Structural basis for substrate recognition in the salicylic acid carboxyl methyltransferase family. Plant Cell 15 (2003) 1704-1716. [PMID: 12897246]
Accepted name: gibberellin A9 O-methyltransferase
Reaction: S-adenosyl-L-methionine + gibberellin A9 = S-adenosyl-L-homocysteine + methyl gibberellin A9
Glossary: gibberellin A9 = (1R,4aR,4bR,7R,9aR,10S,10aR)-1-methyl-8-methylene-13-oxododecahydro-4a,1-(epoxymethano)-7,9a-methanobenzo[a]azulene-10-carboxylic acid
methyl gibberellin A9 = methyl (1R,4aR,4bR,7R,9aR,10S,10aR)-1-methyl-8-methylene-13-oxododecahydro-4a,1-(epoxymethano)-7,9a-methanobenzo[a]azulene-10-carboxylate
Other name(s): GAMT1
Systematic name: S-adenosyl-L-methionine:gibberellin A9 O-methyltransferase
Comments: The enzyme also methylates gibberellins A20 (95%), A3 (80%), A4 (69%) and A34 (46%) with significant activity.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:
References:
1. Varbanova, M., Yamaguchi, S., Yang, Y., McKelvey, K., Hanada, A., Borochov, R., Yu, F., Jikumaru, Y., Ross, J., Cortes, D., Ma, C.J., Noel, J.P., Mander, L., Shulaev, V., Kamiya, Y., Rodermel, S., Weiss, D. and Pichersky, E. Methylation of gibberellins by Arabidopsis GAMT1 and GAMT2. Plant Cell 19 (2007) 32-45. [PMID: 17220201]
Accepted name: gibberellin A4 carboxyl methyltransferase
Reaction: S-adenosyl-L-methionine + gibberellin A4 = S-adenosyl-L-homocysteine + methyl gibberellin A4
Glossary: gibberellin A4 = (1S,2S,4aR,4bR,7R,9aR,10S,10aR)-2-hydroxy-1-methyl-8-methylidene-13-oxododecahydro-4a,1-(epoxymethano)-7,9a-methanobenzo[a]azulene-10-carboxylic acid
methyl gibberellin A4 = methyl (1S,2S,4aR,4bR,7R,9aR,10S,10aR)-2-hydroxy-1-methyl-8-methylene-13-oxododecahydro-4a,1-(epoxymethano)-7,9a-methanobenzo[a]azulene-10-carboxylate
Other name(s): GAMT2; gibberellin A4 O-methyltransferase
Systematic name: S-adenosyl-L-methionine:gibberellin A4 O-methyltransferase
Comments: The enzyme also methylates gibberellins A34 (80%), A9 (60%), and A3 (45%) with significant activity.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:
References:
1. Varbanova, M., Yamaguchi, S., Yang, Y., McKelvey, K., Hanada, A., Borochov, R., Yu, F., Jikumaru, Y., Ross, J., Cortes, D., Ma, C.J., Noel, J.P., Mander, L., Shulaev, V., Kamiya, Y., Rodermel, S., Weiss, D. and Pichersky, E. Methylation of gibberellins by Arabidopsis GAMT1 and GAMT2. Plant Cell 19 (2007) 32-45. [PMID: 17220201]
Accepted name: anthranilate O-methyltransferase
Reaction: S-adenosyl-L-methionine + anthranilate = S-adenosyl-L-homocysteine + O-methyl anthranilate
Other name(s): AAMT
Systematic name: S-adenosyl-L-methionine:anthranilate O-methyltransferase
Comments: In the plant maize (Zea mays), the isoforms AAMT1 and AAMT2 are specific for anthranilate while AAMT3 also has the activity of EC 2.1.1.273, benzoate methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:
References:
1. Köllner, T.G., Lenk, C., Zhao, N., Seidl-Adams, I., Gershenzon, J., Chen, F. and Degenhardt, J. Herbivore-induced SABATH methyltransferases of maize that methylate anthranilic acid using s-adenosyl-L-methionine. Plant Physiol. 153 (2010) 1795-1807. [PMID: 20519632]
Accepted name: indole-3-acetate O-methyltransferase
Reaction: S-adenosyl-L-methionine + (indol-3-yl)acetate = S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
Other name(s): IAA carboxylmethyltransferase; IAMT
Systematic name: S-adenosyl-L-methionine:(indol-3-yl)acetate O-methyltransferase
Comments: Binds Mg2+. The enzyme is found in plants and is important for regulation of the plant hormone (indol-3-yl)acetate. The product, methyl (indol-3-yl)acetate is inactive as hormone [2].
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, PDB, CAS registry number:
References:
1. Zubieta, C., Ross, J.R., Koscheski, P., Yang, Y., Pichersky, E. and Noel, J.P. Structural basis for substrate recognition in the salicylic acid carboxyl methyltransferase family. Plant Cell 15 (2003) 1704-1716. [PMID: 12897246]
2. Li, L., Hou, X., Tsuge, T., Ding, M., Aoyama, T., Oka, A., Gu, H., Zhao, Y. and Qu, L.J. The possible action mechanisms of indole-3-acetic acid methyl ester in Arabidopsis. Plant Cell Rep. 27 (2008) 575-584. [PMID: 17926040]
3. Zhao, N., Ferrer, J.L., Ross, J., Guan, J., Yang, Y., Pichersky, E., Noel, J.P. and Chen, F. Structural, biochemical, and phylogenetic analyses suggest that indole-3-acetic acid methyltransferase is an evolutionarily ancient member of the SABATH family. Plant Physiol. 146 (2008) 455-467. [PMID: 18162595]
Accepted name: trans-anol O-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + trans-anol = S-adenosyl-L-homocysteine + trans-anethole
(2) S-adenosyl-L-methionine + isoeugenol = S-adenosyl-L-homocysteine + isomethyleugenol
Glossary: trans-anol = 4-[(1E)-prop-1-en-1-yl]phenol
trans-anethole = 1-methoxy-4-[(1E)-prop-1-en-1-yl]benzene
Other name(s): AIMT1; S-adenosyl-L-methionine:t-anol/isoeugenol O-methyltransferase; t-anol O-methyltransferase
Systematic name: S-adenosyl-L-methionine:trans-anol O-methyltransferase
Comments: The enzyme from anise (Pimpinella anisum) is highly specific for substrates in which the double bond in the propenyl side chain is located between C7 and C8, and, in contrast to EC 2.1.1.146, (iso)eugenol O-methyltransferase, does not have activity with eugenol or chavicol.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:
References:
1. Koeduka, T., Baiga, T.J., Noel, J.P. and Pichersky, E. Biosynthesis of t-anethole in anise: characterization of t-anol/isoeugenol synthase and an O-methyltransferase specific for a C7-C8 propenyl side chain. Plant Physiol. 149 (2009) 384-394. [PMID: 18987218]
Accepted name: selenocysteine Se-methyltransferase
Reaction: S-methyl-L-methionine + L-selenocysteine = L-methionine + Se-methyl-L-selenocysteine
Other name(s): SMT
Systematic name: S-methyl-L-methionine:L-selenocysteine Se-methyltransferase
Comments: The enzyme uses S-adenosyl-L-methionine as methyl donor less actively than S-methyl-L-methionine. The enzyme from broccoli (Brassica oleracea var. italica) also has the activity of EC 2.1.1.10, homocysteine S-methyltransferase [4].
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:
References:
1. Neuhierl, B. and Bock, A. On the mechanism of selenium tolerance in selenium-accumulating plants. Purification and characterization of a specific selenocysteine methyltransferase from cultured cells of Astragalus bisculatus. Eur. J. Biochem. 239 (1996) 235-238. [PMID: 8706715]
2. Neuhierl, B., Thanbichler, M., Lottspeich, F. and Bock, A. A family of S-methylmethionine-dependent thiol/selenol methyltransferases. Role in selenium tolerance and evolutionary relation. J. Biol. Chem. 274 (1999) 5407-5414. [PMID: 10026151]
3. Lyi, S.M., Heller, L.I., Rutzke, M., Welch, R.M., Kochian, L.V. and Li, L. Molecular and biochemical characterization of the selenocysteine Se-methyltransferase gene and Se-methylselenocysteine synthesis in broccoli. Plant Physiol. 138 (2005) 409-420. [PMID: 15863700]
4. Lyi, S.M., Zhou, X., Kochian, L.V. and Li, L. Biochemical and molecular characterization of the homocysteine S-methyltransferase from broccoli (Brassica oleracea var. italica). Phytochemistry 68 (2007) 1112-1119. [PMID: 17391716]
Accepted name: phenylpyruvate C3-methyltransferase
Reaction: S-adenosyl-L-methionine + 3-phenylpyruvate = S-adenosyl-L-homocysteine + (3S)-2-oxo-3-phenylbutanoate
Glossary: 3-phenylpyruvate = 2-oxo-3-phenylpropanoate
(3S)-2-oxo-3-methyl-3-phenylpropanoate = (3S)-β-methyl-phenylpyruvate
Other name(s): phenylpyruvate Cβ-methyltransferase; phenylpyruvate methyltransferase; mppJ (gene name)
Systematic name: S-adenosyl-L-methionine:2-oxo-3-phenylpropanoate C3-methyltransferase
Comments: The enzyme from the bacterium Streptomyces hygroscopicus NRRL3085 is involved in synthesis of the nonproteinogenic amino acid (2S,3S)-β-methyl-phenylalanine, a building block of the antibiotic mannopeptimycin.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, PDB, CAS registry number:
References:
1. Huang, Y.T., Lyu, S.Y., Chuang, P.H., Hsu, N.S., Li, Y.S., Chan, H.C., Huang, C.J., Liu, Y.C., Wu, C.J., Yang, W.B. and Li, T.L. In vitro characterization of enzymes involved in the synthesis of nonproteinogenic residue (2S,3S)-β-methylphenylalanine in glycopeptide antibiotic mannopeptimycin. Chembiochem 10 (2009) 2480-2487. [PMID: 19731276]
Accepted name: tRNAPhe 7-[(3-amino-3-carboxypropyl)-4-demethylwyosine37-N4]-methyltransferase
Reaction: S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe = S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
For diagram of reaction click here.
Glossary: wyosine = 4,6-dimethyl-3-(β-D-ribofuranosyl)-3,4-dihydro-9H-imidazo[1,2-a]purin-9-one
wybutosine = yW = 7-{(3S)-4-methoxy-3-[(methoxycarbonyl)amino]-4-oxobutyl}-4,5-dimethyl-3-(β-D-ribofuranosyl)-3,4-dihydro-9H-imidazo[1,2-a]purin-9-one
Other name(s): TYW3 (gene name); tRNA-yW synthesizing enzyme-3
Systematic name: S-adenosyl-L-methionine:tRNAPhe 7-[(3S)-(3-amino-3-carboxypropyl)-4-demethylwyosine-N4]-methyltransferase
Comments: The enzyme is involved in the biosynthesis of hypermodified tricyclic bases found at position 37 of certain tRNAs. These modifications are important for translational reading-frame maintenance. The enzyme is found in all eukaryotes and in some archaea, but not in bacteria. The eukaryotic enzyme is involved in the biosynthesis of wybutosine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Noma, A., Kirino, Y., Ikeuchi, Y. and Suzuki, T. Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA. EMBO J. 25 (2006) 2142-2154. [PMID: 16642040]
Accepted name: emodin O-methyltransferase
Reaction: S-adenosyl-L-methionine + emodin = S-adenosyl-L-homocysteine + questin
Glossary: emodin = 1,3,8-trihydroxy-6-methyl-9,10-anthraquinone
questin = 1,6-dihydroxy-8-methoxy-3-methyl-9,10-anthraquinone
Other name(s): EOMT
Systematic name: S-adenosyl-L-methionine:emodin 8-O-methyltransferase
Comments: The enzyme is involved in biosynthesis of the seco-anthraquinone (+)-geodin.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:
References:
1. Chen, Z.G., Fujii, I., Ebizuka, Y. and Sankawa, U. Emodin O-methyltransferase from Aspergillus terreus. Arch. Microbiol. 158 (1992) 29-34. [PMID: 1444712]
Accepted name: 8-demethylnovobiocic acid C8-methyltransferase
Reaction: S-adenosyl-L-methionine + 8-demethylnovobiocic acid = S-adenosyl-L-homocysteine + novobiocic acid
For diagram of reaction click here.
Glossary: novobiocic acid = N-(2,7-dihydroxy-8-methyl-4-oxochromen-3-yl)-4-hydroxy-3-(3-methylbut-2-enyl) benzamide
Other name(s): NovO
Systematic name: S-adenosyl-L-methionine:8-demethylnovobiocic acid C8-methyltransferase
Comments: The enzyme is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, PDB, CAS registry number:
References:
1. Pacholec, M., Tao, J. and Walsh, C.T. CouO and NovO: C-methyltransferases for tailoring the aminocoumarin scaffold in coumermycin and novobiocin antibiotic biosynthesis. Biochemistry 44 (2005) 14969-14976. [PMID: 16274243]
Accepted name: demethyldecarbamoylnovobiocin O-methyltransferase
Reaction: S-adenosyl-L-methionine + demethyldecarbamoylnovobiocin = S-adenosyl-L-homocysteine + decarbamoylnovobiocin
For diagram of reaction click here.
Glossary: demethyldecarbamoylnovobiocin = N-{7-[(6-deoxy-5-methyl-β-D-gulopyranosyl)oxy]-4-hydroxy-8-methyl-2-oxo-2H-chromen-3-yl}-4-hydroxy-3-(3-methylbut-2-en-1-yl)benzamide
decarbamoylnovobiocin = N-{7-[(6-deoxy-5-methyl-4-O-methyl-β-D-gulopyranosyl)oxy]4-hydroxy-8-methyl-2-oxo-2H-chromen-3-yl}-4-hydroxy-3-(3-methyl-2-buten-1-yl)benzamide
Other name(s): NovP
Systematic name: S-adenosyl-L-methionine:demethyldecarbamoylnovobiocin 4''-O-methyltransferase
Comments: The enzyme is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, PDB, CAS registry number:
References:
1. Freel Meyers, C.L., Oberthur, M., Xu, H., Heide, L., Kahne, D. and Walsh, C.T. Characterization of NovP and NovN: completion of novobiocin biosynthesis by sequential tailoring of the noviosyl ring. Angew. Chem. Int. Ed. Engl. 43 (2004) 67-70. [PMID: 14694473]
2. Gomez Garcia, I., Stevenson, C.E., Uson, I., Freel Meyers, C.L., Walsh, C.T. and Lawson, D.M. The crystal structure of the novobiocin biosynthetic enzyme NovP: the first representative structure for the TylF O-methyltransferase superfamily. J. Mol. Biol. 395 (2010) 390-407. [PMID: 19857499]
Accepted name: 25S rRNA (adenine2142-N1)-methyltransferase
Reaction: S-adenosyl-L-methionine + adenine2142 in 25S rRNA = S-adenosyl-L-homocysteine + N1-methyladenine2142 in 25S rRNA
Other name(s): BMT2 (gene name); 25S rRNA m1A2142 methyltransferase
Systematic name: S-adenosyl-L-methionine:25S rRNA (adenine2142-N1)-methyltransferase
Comments: In the yeast Saccharomyces cerevisiae this methylation is important for resistance towards hydrogen peroxide and the antibiotic anisomycin.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:
References:
1. Sharma, S., Watzinger, P., Kotter, P. and Entian, K.D. Identification of a novel methyltransferase, Bmt2, responsible for the N-1-methyl-adenosine base modification of 25S rRNA in Saccharomyces cerevisiae. Nucleic Acids Res. 41 (2013) 5428-5443. [PMID: 23558746]
Accepted name: 25S rRNA (adenine645-N1)-methyltransferase
Reaction: S-adenosyl-L-methionine + adenine645 in 25S rRNA = S-adenosyl-L-homocysteine + N1-methyladenine645 in 25S rRNA
Other name(s): 25S rRNA m1A645 methyltransferase; Rrp8
Systematic name: S-adenosyl-L-methionine:25S rRNA (adenine645-N1)-methyltransferase
Comments: The enzyme is found in eukaryotes. The adenine position refers to tRNA the yeast Saccharomyces cerevisiae, in which the enzyme is important for ribosome biogenesis.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:
References:
1. Peifer, C., Sharma, S., Watzinger, P., Lamberth, S., Kotter, P. and Entian, K.D. Yeast Rrp8p, a novel methyltransferase responsible for m1A 645 base modification of 25S rRNA. Nucleic Acids Res. 41 (2013) 1151-1163. [PMID: 23180764]
Accepted name: aklanonic acid methyltransferase
Reaction: S-adenosyl-L-methionine + aklanonate = S-adenosyl-L-homocysteine + methyl aklanonate
For diagram of reaction click here.
Glossary: methyl aklanonate = methyl [1,4,5-trihydroxy-9,10-dioxo-3-(3-oxopentanoyl)-9,10-dihydroanthracen-2-yl]acetate
aklanonate = [4,5-dihydroxy-9,10-dioxo-3-(3-oxopentanoyl)-9,10-dihydroanthracen-2-yl]acetic acid
Other name(s): DauC; AAMT
Systematic name: S-adenosyl-L-methionine:aklanonate O-methyltransferase
Comments: The enzyme from the Gram-positive bacterium Streptomyces sp. C5 is involved in the biosynthesis of the anthracycline daunorubicin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Dickens, M.L., Ye, J. and Strohl, W.R. Analysis of clustered genes encoding both early and late steps in daunomycin biosynthesis by Streptomyces sp. strain C5. J. Bacteriol. 177 (1995) 536-543. [PMID: 7836284]
Accepted name: cobalt-precorrin-7 (C5)-methyltransferase
Reaction: S-adenosyl-L-methionine + cobalt-precorrin-7 = S-adenosyl-L-homocysteine + cobalt-precorrin-8
For diagram of reaction, click here
Other name(s): CbiE
Systematic name: S-adenosyl-L-methionine:precorrin-7 C5-methyltransferase
Comments: This enzyme catalyses the methylation at C-5 of cobalt-precorrin-7, a step in the anaerobic (early cobalt insertion) adenosylcobalamin biosynthesis pathway. The equivalent activity in the aerobic adenosylcobalamin biosynthesis pathway is catalysed by the bifunctional enzyme EC 2.1.1.132, precorrin-6B C5.15-methyltransferase (decarboxylating).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Santander, P.J., Kajiwara, Y., Williams, H.J. and Scott, A.I. Structural characterization of novel cobalt corrinoids synthesized by enzymes of the vitamin B12 anaerobic pathway. Bioorg. Med. Chem. 14 (2006) 724-731. [PMID: 16198574]
2. Moore, S.J., Lawrence, A.D., Biedendieck, R., Deery, E., Frank, S., Howard, M.J., Rigby, S.E. and Warren, M.J. Elucidation of the anaerobic pathway for the corrin component of cobalamin (vitamin B12). Proc. Natl. Acad. Sci. USA 110 (2013) 14906-14911. [PMID: 23922391]
Accepted name: tRNAPhe [7-(3-amino-3-carboxypropyl)wyosine37-O]-methyltransferase
Reaction: S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-carboxypropyl]wyosine37 in tRNAPhe = S-adenosyl-L-homocysteine + 7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37 in tRNAPhe
For diagram of reaction, click here
Glossary: wyosine = 4,6-dimethyl-3-(β-D-ribofuranosyl)-3,4-dihydro-9H-imidazo[1,2-a]purin-9-one
wybutosine = yW = 7-[(3S)-3-(methoxycarbonyl)-3-(methoxycarbonylamino)propyl]-4,5-dimethyl-3-(β-D-ribofuranosyl)-3,4-dihydro-9H-imidazo[1,2-a]purin-9-one
Other name(s): TYW4 (ambiguous); tRNA-yW synthesizing enzyme-4 (ambiguous)
Systematic name: S-adenosyl-L-methionine:tRNAPhe {7-[(3S)-3-amino-3-carboxypropyl]wyosine37-O}-methyltransferase
Comments: The enzyme is found only in eukaryotes, where it is involved in the biosynthesis of wybutosine, a hypermodified tricyclic base found at position 37 of certain tRNAs. The modification is important for translational reading-frame maintenance. In some species that produce hydroxywybutosine the enzyme uses 7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine37 in tRNAPhe as substrate. The enzyme also has the activity of EC 2.3.1.231, tRNAPhe 7-[(3S)-4-methoxy-(3-amino-3-carboxypropyl)wyosine37-O]-carbonyltransferase [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Noma, A., Kirino, Y., Ikeuchi, Y. and Suzuki, T. Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA. EMBO J. 25 (2006) 2142-2154. [PMID: 16642040]
2. Suzuki, Y., Noma, A., Suzuki, T., Ishitani, R. and Nureki, O. Structural basis of tRNA modification with CO2 fixation and methylation by wybutosine synthesizing enzyme TYW4. Nucleic Acids Res. 37 (2009) 2910-2925. [PMID: 19287006]
3. Kato, M., Araiso, Y., Noma, A., Nagao, A., Suzuki, T., Ishitani, R. and Nureki, O. Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification. Nucleic Acids Res. 39 (2011) 1576-1585. [PMID: 20972222]
Accepted name: (R,S)-reticuline 7-O-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + (S)-reticuline = S-adenosyl-L-homocysteine + (S)-laudanine
(2) S-adenosyl-L-methionine + (R)-reticuline = S-adenosyl-L-homocysteine + (R)-laudanine
For diagram of reaction, click here
Glossary: (S)-reticuline = (1S)-1-[(3-hydroxy-4-methoxyphenyl)methyl]-6-methoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-7-ol
(R)-reticuline = (1R)-1-[(3-hydroxy-4-methoxyphenyl)methyl]-6-methoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-7-ol
(S)-laudanine = 5-[((1S)-6,7-dimethoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-1-yl)methyl]-2-methoxyphenol
(R)-laudanine = 5-[((1R)-6,7-dimethoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-1-yl)methyl]-2-methoxyphenol
Systematic name: S-adenosyl-L-methionine:(R,S)-reticuline 7-O-methyltransferase
Comments: The enzyme from the plant Papaver somniferum (opium poppy) methylates (S)- and (R)-reticuline with equal efficiency and is involved in the biosynthesis of tetrahydrobenzylisoquinoline alkaloids.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Ounaroon, A., Decker, G., Schmidt, J., Lottspeich, F. and Kutchan, T.M. (R,S)-Reticuline 7-O-methyltransferase and (R,S)-norcoclaurine 6-O-methyltransferase of Papaver somniferum - cDNA cloning and characterization of methyl transfer enzymes of alkaloid biosynthesis in opium poppy. Plant J. 36 (2003) 808-819. [PMID: 14675446]
2. Weid, M., Ziegler, J. and Kutchan, T.M. The roles of latex and the vascular bundle in morphine biosynthesis in the opium poppy, Papaver somniferum. Proc. Natl. Acad. Sci. USA 101 (2004) 13957-13962. [PMID: 15353584]
Accepted name: carminomycin 4-O-methyltransferase
Reaction: S-adenosyl-L-methionine + carminomycin = S-adenosyl-L-homocysteine + daunorubicin
For diagram of reaction, click here
Glossary: daunorubicin = (+)-daunomycin = (8S,10S)-8-acetyl-10-[(2S,4S,5S,6S)-4-amino-5-hydroxy-6-methyloxan-2-yl]oxy-6,8,11-trihydroxy-1-methoxy-9,10-dihydro-7H-tetracene-5,12-dione
carminomycin = (1S,3S)-3-acetyl-3,5,10,12-tetrahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranoside = (1S,3S)-3-acetyl-3,5,10,12-tetrahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydronaphthacen-1-yl 3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranoside
carubicin = (1S,3S)-3-acetyl-3,5,12-trihydroxy-10-methoxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranoside
= (8S,10S)-8-acetyl-10-[(3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranosyl)oxy]-6,8,11-trihydroxy-1-methoxy-7,8,9,10-tetrahydronaphthacene-5,12-dione
Other name(s): DnrK; DauK
Systematic name: S-adenosyl-L-methionine:carminomycin 4-O-methyltransferase
Comments: The enzymes from the Gram-positive bacteria Streptomyces sp. C5 and Streptomyces peucetius are involved in the biosynthesis of the anthracycline daunorubicin. In vitro the enzyme from Streptomyces sp. C5 also catalyses the 4-O-methylation of 13-dihydrocarminomycin, rhodomycin D and 10-carboxy-13-deoxycarminomycin [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Connors, N.C. and Strohl, W.R. Partial purification and properties of carminomycin 4-O-methyltransferase from Streptomyces sp. strain C5. J. Gen. Microbiol. 139 Pt 6 (1993) 1353-1362. [PMID: 8360627]
2. Jansson, A., Koskiniemi, H., Mantsala, P., Niemi, J. and Schneider, G. Crystal structure of a ternary complex of DnrK, a methyltransferase in daunorubicin biosynthesis, with bound products. J. Biol. Chem. 279 (2004) 41149-41156. [PMID: 15273252]
3. Dickens, M.L., Priestley, N.D. and Strohl, W.R. In vivo and in vitro bioconversion of ε-rhodomycinone glycoside to doxorubicin: functions of DauP, DauK, and DoxA. J. Bacteriol. 179 (1997) 2641-2650. [PMID: 9098063]
Accepted name: 6-hydroxytryprostatin B O-methyltransferase
Reaction: S-adenosyl-L-methionine + 6-hydroxytryprostatin B = S-adenosyl-L-homocysteine + tryprostatin A
For diagram of reaction, click here
Glossary: 6-hydroxytryprostatin B = (3S,8aS)-3-{[6-hydroxy-2-(3-methylbut-2-en-1-yl)-1H-indol-3-yl]methyl}hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
tryprostatin A = (3S,8aS)-3-{[6-methoxy-2-(3-methylbut-2-en-1-yl)-1H-indol-3-yl]methyl}hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
Other name(s): ftmD (gene name)
Systematic name: S-adenosyl-L-methionine:6-hydroxytryprostatin B O-methyltransferase
Comments: Involved in the biosynthetic pathways of several indole alkaloids such as tryprostatins, fumitremorgins and verruculogen.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kato, N., Suzuki, H., Okumura, H., Takahashi, S. and Osada, H. A point mutation in ftmD blocks the fumitremorgin biosynthetic pathway in Aspergillus fumigatus strain Af293. Biosci. Biotechnol. Biochem. 77 (2013) 1061-1067. [PMID: 23649274]
Accepted name: 3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase
Reaction: S-adenosyl-L-methionine + 3-O-phospho-α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol = S-adenosyl-L-homocysteine + 3-O-methylphospho-α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WbdD; S-adenosyl-L-methionine:3-O-phospho-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→3)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-α-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase
Systematic name: S-adenosyl-L-methionine:3-O-phospho-α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase
Comments: The enzyme is involved in the biosynthesis of the polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotype O9a. O-Polysaccharide structures vary extensively because of differences in the number and type of sugars in the repeat unit. The dual kinase/methylase WbdD also catalyses the preceding phosphorylation of α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol (cf. EC 2.7.1.181, polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Clarke, B.R., Cuthbertson, L. and Whitfield, C. Nonreducing terminal modifications determine the chain length of polymannose O antigens of Escherichia coli and couple chain termination to polymer export via an ATP-binding cassette transporter. J. Biol. Chem. 279 (2004) 35709-35718. [PMID: 15184370]
2. Clarke, B.R., Greenfield, L.K., Bouwman, C. and Whitfield, C. Coordination of polymerization, chain termination, and export in assembly of the Escherichia coli lipopolysaccharide O9a antigen in an ATP-binding cassette transporter-dependent pathway. J. Biol. Chem. 284 (2009) 30662-30672. [PMID: 19734145]
3. Clarke, B.R., Richards, M.R., Greenfield, L.K., Hou, D., Lowary, T.L. and Whitfield, C. In vitro reconstruction of the chain termination reaction in biosynthesis of the Escherichia coli O9a O-polysaccharide: the chain-length regulator, WbdD, catalyzes the addition of methyl phosphate to the non-reducing terminus of the growing glycan. J. Biol. Chem. 286 (2011) 41391-41401. [PMID: 21990359]
4. Liston, S.D., Clarke, B.R., Greenfield, L.K., Richards, M.R., Lowary, T.L. and Whitfield, C. Domain interactions control complex formation and polymerase specificity in the biosynthesis of the Escherichia coli O9a antigen. J. Biol. Chem. 290 (2015) 1075-1085. [PMID: 25422321]
Accepted name: 2-methyl-6-phytyl-1,4-hydroquinone methyltransferase
Reaction: (1) S-adenosyl-L-methionine + 2-methyl-6-phytylbenzene-1,4-diol = S-adenosyl-L-homocysteine + 2,3-dimethyl-6-phytylbenzene-1,4-diol
(2) S-adenosyl-L-methionine + 2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol = S-adenosyl-L-homocysteine + plastoquinol
(3) S-adenosyl-L-methionine + 6-geranylgeranyl-2-methylbenzene-1,4-diol = S-adenosyl-L-homocysteine + 6-geranylgeranyl-2,3-dimethylbenzene-1,4-diol
For diagram of reaction click here or click here or click here.
Other name(s): VTE3 (gene name); 2-methyl-6-solanyl-1,4-hydroquinone methyltransferase; MPBQ/MSBQ methyltransferase; MPBQ/MSBQ MT
Systematic name: S-adenosyl-L-methionine:2-methyl-6-phytyl-1,4-benzoquinol C3-methyltransferase
Comments: Involved in the biosynthesis of plastoquinol, as well as vitamin E (tocopherols and tocotrienols).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Shintani, D.K., Cheng, Z. and DellaPenna, D. The role of 2-methyl-6-phytylbenzoquinone methyltransferase in determining tocopherol composition in Synechocystis sp. PCC6803. FEBS Lett 511 (2002) 1-5. [PMID: 11821038]
2. Cheng, Z., Sattler, S., Maeda, H., Sakuragi, Y., Bryant, D.A. and DellaPenna, D. Highly divergent methyltransferases catalyze a conserved reaction in tocopherol and plastoquinone synthesis in cyanobacteria and photosynthetic eukaryotes. Plant Cell 15 (2003) 2343-2356. [PMID: 14508009]
3. Van Eenennaam, A.L., Lincoln, K., Durrett, T.P., Valentin, H.E., Shewmaker, C.K., Thorne, G.M., Jiang, J., Baszis, S.R., Levering, C.K., Aasen, E.D., Hao, M., Stein, J.C., Norris, S.R. and Last, R.L. Engineering vitamin E content: from Arabidopsis mutant to soy oil. Plant Cell 15 (2003) 3007-3019. [PMID: 14630966]
Accepted name: methyltransferase cap2
Reaction: S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
Other name(s): CMTR2 (gene name); MTR2; cap2-MTase; mRNA (nucleoside-2'-O)-methyltransferase (ambiguous)
Systematic name: S-adenosyl-L-methionine:5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-ribonucleotide-[mRNA] 2'-O-methyltransferase
Comments: The enzyme, found in higher eukaryotes including insects and vertebrates, and their viruses, methylates the ribose of the ribonucleotide at the second transcribed position of mRNAs and snRNAs. This methylation event is known as cap2. The human enzyme can also methylate mRNA molecules where the upstream ribonucleotide is not methylated (see EC 2.1.1.57, methyltransferase cap1), but with lower efficiency [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Arhin, G.K., Ullu, E. and Tschudi, C. 2'-O-methylation of position 2 of the trypanosome spliced leader cap 4 is mediated by a 48 kDa protein related to vaccinia virus VP39. Mol. Biochem. Parasitol. 147 (2006) 137-139. [PMID: 16516986]
2. Werner, M., Purta, E., Kaminska, K.H., Cymerman, I.A., Campbell, D.A., Mittra, B., Zamudio, J.R., Sturm, N.R., Jaworski, J. and Bujnicki, J.M. 2'-O-ribose methylation of cap2 in human: function and evolution in a horizontally mobile family. Nucleic Acids Res. 39 (2011) 4756-4768. [PMID: 21310715]
Accepted name: peptide chain release factor N5-glutamine methyltransferase
Reaction: S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine = S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
Other name(s): N5-glutamine S-adenosyl-L-methionine dependent methyltransferase; N5-glutamine MTase; HemK; PrmC
Systematic name: S-adenosyl-L-methionine:[peptide chain release factor 1 or 2]-L-glutamine (N5-glutamine)-methyltransferase
Comments: Modifies the glutamine residue in the universally conserved glycylglycylglutamine (GGQ) motif of peptide chain release factor, resulting in almost complete loss of release activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Nakahigashi, K., Kubo, N., Narita, S., Shimaoka, T., Goto, S., Oshima, T., Mori, H., Maeda, M., Wada, C. and Inokuchi, H. HemK, a class of protein methyl transferase with similarity to DNA methyl transferases, methylates polypeptide chain release factors, and hemK knockout induces defects in translational termination. Proc. Natl. Acad. Sci. USA 99 (2002) 1473-1478. [PMID: 11805295]
2. Heurgue-Hamard, V., Champ, S., Engstrom, A., Ehrenberg, M. and Buckingham, R.H. The hemK gene in Escherichia coli encodes the N5-glutamine methyltransferase that modifies peptide release factors. EMBO J. 21 (2002) 769-778. [PMID: 11847124]
3. Schubert, H.L., Phillips, J.D. and Hill, C.P. Structures along the catalytic pathway of PrmC/HemK, an N5-glutamine AdoMet-dependent methyltransferase. Biochemistry 42 (2003) 5592-5599. [PMID: 12741815]
4. Yoon, H.J., Kang, K.Y., Ahn, H.J., Shim, S.M., Ha, J.Y., Lee, S.K., Mikami, B. and Suh, S.W. X-ray crystallographic studies of HemK from Thermotoga maritima, an N5-glutamine methyltransferase. Mol. Cells 16 (2003) 266-269. [PMID: 14651272]
5. Yang, Z., Shipman, L., Zhang, M., Anton, B.P., Roberts, R.J. and Cheng, X. Structural characterization and comparative phylogenetic analysis of Escherichia coli HemK, a protein (N5)-glutamine methyltransferase. J. Mol. Biol. 340 (2004) 695-706. [PMID: 15223314]
6. Pannekoek, Y., Heurgue-Hamard, V., Langerak, A.A., Speijer, D., Buckingham, R.H. and van der Ende, A. The N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase PrmC/HemK in Chlamydia trachomatis methylates class 1 release factors. J. Bacteriol. 187 (2005) 507-511. [PMID: 15629922]
Accepted name: ribosomal protein uL3 N5-glutamine methyltransferase
Reaction: S-adenosyl-L-methionine + [ribosomal protein uL3]-L-glutamine = S-adenosyl-L-homocysteine + [ribosomal protein uL3]-N5-methyl-L-glutamine
Other name(s): YfcB; PrmB
Systematic name: S-adenosyl-L-methionine:[ribosomal protein uL3]-L-glutamine (N5-glutamine)-methyltransferase
Comments: Modifies the glutamine residue in the glycylglycylglutamine (GGQ) motif of ribosomal protein uL3 (Gln150 in the protein from the bacterium Escherichia coli). The enzyme does not act on peptide chain release factor 1 or 2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Heurgue-Hamard, V., Champ, S., Engstrom, A., Ehrenberg, M. and Buckingham, R.H. The hemK gene in Escherichia coli encodes the N5-glutamine methyltransferase that modifies peptide release factors. EMBO J. 21 (2002) 769-778. [PMID: 11847124]
Accepted name: protein N-terminal monomethyltransferase
Reaction: S-adenosyl-L-methionine + N-terminal-(A,P,S)PK-[protein] = S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-(A,P,S)PK-[protein]
Other name(s): NRMT2 (gene name); METTL11B (gene name); N-terminal monomethylase
Systematic name: S-adenosyl-L-methionine:N-terminal-(A,P,S)PK-[protein] monomethyltransferase
Comments: This enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. In contrast to EC 2.1.1.244, protein N-terminal methyltransferase, the protein only adds one methyl group to the N-terminal.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Petkowski, J.J., Bonsignore, L.A., Tooley, J.G., Wilkey, D.W., Merchant, M.L., Macara, I.G. and Schaner Tooley, C.E. NRMT2 is an N-terminal monomethylase that primes for its homologue NRMT1. Biochem. J. 456 (2013) 453-462. [PMID: 24090352]
Accepted name: pavine N-methyltransferase
Reaction: S-adenosyl-L-methionine + (±)-pavine = S-adenosyl-L-homocysteine + N-methylpavine
Other name(s): PavNMT
Systematic name: S-adenosyl-L-methionine:(±)-pavine N-methyltransferase
Comments: The enzyme, isolated from the plant Thalictrum flavum, also methylates (R,S)-stylopine and (S)-scoulerine (11%) with lower activity (14% and 11%, respectively).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Jain, A., Ziegler, J., Liscombe, D.K., Facchini, P.J., Tucker, P.A. and Panjikar, S. Purification, crystallization and X-ray diffraction analysis of pavine N-methyltransferase from Thalictrum flavum. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 1066-1069. [PMID: 18997344]
2. Liscombe, D.K., Ziegler, J., Schmidt, J., Ammer, C. and Facchini, P.J. Targeted metabolite and transcript profiling for elucidating enzyme function: isolation of novel N-methyltransferases from three benzylisoquinoline alkaloid-producing species. Plant J. 60 (2009) 729-743. [PMID: 19624470]