Continued from EC 1.14.19.51-81
EC 1.14 Acting on paired donors with incorporation of molecular oxygen [continued]
EC 1.14.20 With 2-oxoglutarate as one donor, and the other dehydrogenated
EC 1.14.21 With NADH or NADPH as one donor, and the other dehydrogenated
Accepted name: deacetoxycephalosporin-C synthase
Reaction: penicillin N + 2-oxoglutarate + O2 = deacetoxycephalosporin C + succinate + CO2 + H2O
For diagram click here.
Other names: DAOCS; penicillin N expandase; DAOC synthase
Systematic name: penicillin-N,2-oxoglutarate:oxygen oxidoreductase (ring-expanding)
Comments: Forms part of the penicillin biosynthesis pathway (for pathway, click here).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 85746-10-7
References:
1. Cantwell, C., Beckmann, R., Whiteman, P., Queener, S.W. and Abraham, E.P. Isolation of deacetoxycephalosporin-c from fermentation broths of Penicillium chrysogenum transformants - construction of a new fungal biosynthetic-pathway. Proc. R. Soc. Lond. B Biol. Sci. 248 (1992) 283-289. [PMID: 1354366]
2. Lee, H.J., Lloyd, M.D., Harlos, K., Clifton, I.J., Baldwin, J.E. and Schofield, C.J. Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS). J. Mol. Biol. 308 (2001) 937-948. [PMID: 11352583]
3. Yeh, W.K., Ghag, S.K. and Queener, S.W. Enzymes for epimerization of isopenicillin N, ring expansion of penicillin N, and 3'-hydroxylation of deacetoxycephalosporin C. Function, evolution, refolding, and enzyme engineering. Ann. N.Y. Acad. Sci. 672 (1992) 396-408.
4. Valegård, K., van Scheltinga, A.C.T., Lloyd, M.D., Hara, T., Ramaswamy, S., Perrakis, A., Thompson, A., Lee, H.-J., Baldwin, J.E., Schofield, C.J., Hajdu, J. and Andersson, I. Structure of a cephalosporin synthase. Nature 394 (1998) 805-809. [PMID: 9723623]
5. Dotzlaf, J.E. and Yeh, W.K. Purification and properties of deacetoxycephalosporin C synthase from recombinant Escherichia coli and its comparison with the native enzyme purified from Streptomyces clavuligerus. J. Biol. Chem. 264 (1989) 10219-10227. [PMID: 2656705]
[EC 1.14.20.2 Transferred entry: 2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase. Now EC 1.14.11.59, 2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase (EC 1.14.20.2 created 2012, deleted 2018)]
Accepted name: (5R)-carbapenem-3-carboxylate synthase
Reaction: (3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2 = (5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
Glossary: (3S,5S)-carbapenam-3-carboxylate = (2S,5S)-7-oxo-1-azabicyclo[3.2.0]heptane-2-carboxylate
(5R)-carbapen-2-em-3-carboxylate = (5R)-7-oxo-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
Other name(s): carC (gene name)
Systematic name: (3S,5S)-carbapenam-3-carboxylate,2-oxoglutarate:oxygen oxidoreductase (dehydrating)
Comments: Requires Fe2+. The enzyme is involved in the biosynthesis of the carbapenem β-lactam antibiotic (5R)-carbapen-2-em-3-carboxylate in the bacterium Pectobacterium carotovorum. It catalyses a stereoinversion at C-5 and introduces a double bond between C-2 and C-3.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, PDB, CAS registry number:
References:
1. Clifton, I.J., Doan, L.X., Sleeman, M.C., Topf, M., Suzuki, H., Wilmouth, R.C. and Schofield, C.J. Crystal structure of carbapenem synthase (CarC). J. Biol. Chem. 278 (2003) 20843-20850. [PMID: 12611886]
2. Stapon, A., Li, R. and Townsend, C.A. Carbapenem biosynthesis: confirmation of stereochemical assignments and the role of CarC in the ring stereoinversion process from L-proline. J. Am. Chem. Soc. 125 (2003) 8486-8493. [PMID: 12848554]
3. Sleeman, M.C., Smith, P., Kellam, B., Chhabra, S.R., Bycroft, B.W. and Schofield, C.J. Biosynthesis of carbapenem antibiotics: new carbapenam substrates for carbapenem synthase (CarC). ChemBioChem. 5 (2004) 879-882. [PMID: 15174175]
Accepted name: anthocyanidin synthase
Reaction: a (2R,3S,4S)-leucoanthocyanidin + 2-oxoglutarate + O2 = an anthocyanidin + succinate + CO2 + 2 H2O (overall reaction)
(1a) a (2R,3S,4S)-leucoanthocyanidin + 2-oxoglutarate + O2 = a (4S)- 2,3-dehydroflavan-3,4-diol + succinate + CO2 + H2O
(1b) a (4S)- 2,3-dehydroflavan-3,4-diol = an anthocyanidin + H2O
For diagram of reaction click here.
Glossary: taxifolin = 3,4-dihydroquercitin
Other name(s): leucocyanidin oxygenase; leucocyanidin,2-oxoglutarate:oxygen oxidoreductase; ANS (gene name)
Systematic name: (2R,3S,4S)-leucoanthocyanidin,2-oxoglutarate:oxygen oxidoreductase
Comments: The enzyme requires iron(II) and ascorbate. It is involved in the pathway by which many flowering plants make anthocyanin flower pigments (glycosylated anthocyandins). The enzyme hydroxylates the C-3 carbon, followed by a trans diaxial elimination, forming a C-2,C-3 enol. The product loses a second water molecule to form anthocyanidins. When assayed in vitro, non-enzymic epimerization of the product can lead to formation of dihydroflavanols. Thus when the substrate is leucocyanidin, a mixture of (+)-taxifolin and (+)-epitaxifolin are formed. The enzyme can also oxidize the formed (+)-taxifolin to quercetin (cf. EC 1.14.20.6, flavonol synthase) [2,3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Saito, K., Kobayashi, M., Gong, Z., Tanaka, Y. and Yamazaki, M. Direct evidence for anthocyanidin synthase as a 2-oxoglutarate-dependent oxygenase: molecular cloning and functional expression of cDNA from a red forma of Perilla frutescens. Plant J. 17 (1999) 181-190. [PMID: 10074715]
2. Turnbull, J.J., Sobey, W.J., Aplin, R.T., Hassan, A., Firmin, J.L., Schofield, C.J. and Prescott, A.G. Are anthocyanidins the immediate products of anthocyanidin synthase? Chem. Commun. (2000) 2473-2474.
3. Wilmouth, R.C., Turnbull, J.J., Welford, R.W., Clifton, I.J., Prescott, A.G. and Schofield, C.J. Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana. Structure 10 (2002) 93-103. [PMID: 11796114]
4. Turnbull, J.J., Nagle, M.J., Seibel, J.F., Welford, R.W., Grant, G.H. and Schofield, C.J. The C-4 stereochemistry of leucocyanidin substrates for anthocyanidin synthase affects product selectivity. Bioorg. Med. Chem. Lett. 13 (2003) 3853-3857. [PMID: 14552794]
5. Wellmann, F., Griesser, M., Schwab, W., Martens, S., Eisenreich, W., Matern, U. and Lukacin, R. Anthocyanidin synthase from Gerbera hybrida catalyzes the conversion of (+)-catechin to cyanidin and a novel procyanidin. FEBS Lett. 580 (2006) 1642-1648. [PMID: 16494872]
Accepted name: flavone synthase I
Reaction: a flavanone + 2-oxoglutarate + O2 = a flavone + succinate + CO2 + H2O
For diagram of reaction click here or click here.
Other name(s): FNSI (gene name)
Systematic name: flavanone,2-oxoglutarate:oxygen oxidoreductase (dehydrating)
Comments: The enzyme, which has been found in rice and in members of the Apiaceae (a plant family), is a member of the 2-oxoglutarate-dependent dioxygenases, and requires ascorbate and Fe2+ for full activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Martens, S., Forkmann, G., Matern, U. and Lukačin, R. Cloning of parsley flavone synthase I. Phytochemistry 58 (2001) 43-46. [PMID: 11524111]
2. Lukačin, R., Matern, U., Junghanns, K.T., Heskamp, M.L., Britsch, L., Forkmann, G. and Martens, S. Purification and antigenicity of flavone synthase I from irradiated parsley cells. Arch. Biochem. Biophys. 393 (2001) 177-183. [PMID: 11516175]
3. Martens, S., Forkmann, G., Britsch, L., Wellmann, F., Matern, U. and Lukačin, R. Divergent evolution of flavonoid 2-oxoglutarate-dependent dioxygenases in parsley. FEBS Lett. 544 (2003) 93-98. [PMID: 12782296]
Accepted name: flavonol synthase
Reaction: a dihydroflavonol + 2-oxoglutarate + O2 = a flavonol + succinate + CO2 + H2O
For diagram of reaction click here or click here. or click here
Other name(s): FLS (gene name)
Systematic name: dihydroflavonol,2-oxoglutarate:oxygen oxidoreductase
Comments: In addition to the desaturation of (2R,3R)-dihydroflavonols to flavonols, the enzyme from Citrus unshiu (satsuma mandarin) also has a non-specific activity that trans-hydroxylates the flavanones (2S)-naringenin and the unnatural (2R)-naringenin at C-3 to kaempferol and (2R,3R)-dihydrokaempferol, respectively [2]. Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wellmann, F., Lukačin, R., Moriguchi, T., Britsch, L., Schiltz, E. and Matern, U. Functional expression and mutational analysis of flavonol synthase from Citrus unshiu. Eur. J. Biochem. 269 (2002) 4134-4142. [PMID: 12180990]
2. Lukačin, R., Wellmann, F., Britsch, L., Martens, S. and Matern, U. Flavonol synthase from Citrus unshiu is a bifunctional dioxygenase. Phytochemistry 62 (2003) 287-292. [PMID: 12620339]
3. Martens, S., Forkmann, G., Britsch, L., Wellmann, F., Matern, U. and Lukačin, R. Divergent evolution of flavonoid 2-oxoglutarate-dependent dioxygenases in parsley. FEBS Lett. 544 (2003) 93-98. [PMID: 12782296]
4. Turnbull, J.J., Nakajima, J., Welford, R.W., Yamazaki, M., Saito, K. and Schofield, C.J. Mechanistic studies on three 2-oxoglutarate-dependent oxygenases of flavonoid biosynthesis: anthocyanidin synthase, flavonol synthase, and flavanone 3β-hydroxylase. J. Biol. Chem. 279 (2004) 1206-1216. [PMID: 14570878]
Accepted name: 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)
Reaction: L-arginine + 2-oxoglutarate + O2 = succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O (overall reaction)
(1a) L-arginine + 2-oxoglutarate + O2 = 5-hydroxy-L-arginine + succinate + CO2
(1b) 5-hydroxy-L-arginine = guanidine + L-glutamate-5-semialdehyde
(1c) L-glutamate-5-semialdehyde = (S)-1-pyrroline-5-carboxylate + H2O (spontaneous)
Other name(s): ethene-forming enzyme; ethylene-forming enzyme; EFE
Systematic name: L-arginine,2-oxoglutarate:oxygen oxidoreductase (succinate-forming)
Comments: This is one of two simultaneous reactions catalysed by the enzyme, which is responsible for ethylene production in bacteria of the Pseudomonas syringae group. In the other reaction [EC 1.13.12.19, 2-oxoglutarate dioxygenase (ethene-forming)] the enzyme catalyses the dioxygenation of 2-oxoglutarate forming ethene and three molecules of carbon dioxide.The enzyme catalyses two cycles of the ethene-forming reaction for each cycle of the succinate-forming reaction, so that the stoichiometry of the products ethene and succinate is 2:1.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Nagahama, K., Ogawa, T., Fujii, T., Tazaki, M., Tanase, S., Morino, Y. and Fukuda, H. Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2. J. Gen. Microbiol. 137 (1991) 2281-2286. [PMID: 1770346]
2. Fukuda, H., Ogawa, T., Tazaki, M., Nagahama, K., Fujii, T., Tanase, S. and Morino, Y. Two reactions are simultaneously catalyzed by a single enzyme: the arginine-dependent simultaneous formation of two products, ethylene and succinate, from 2-oxoglutarate by an enzyme from Pseudomonas syringae. Biochem. Biophys. Res. Commun. 188 (1992) 483-489. [PMID: 1445291]
3. Fukuda, H., Ogawa, T., Ishihara, K., Fujii, T., Nagahama, K., Omata, T., Inoue, Y., Tanase, S. and Morino, Y. Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of Pseudomonas syringae pv. phaseolicola PK2. Biochem. Biophys. Res. Commun. 188 (1992) 826-832. [PMID: 1445325]
4. Martinez, S., Fellner, M., Herr, C.Q., Ritchie, A., Hu, J. and Hausinger, R.P. Structures and mechanisms of the non-heme Fe(II)- and 2-oxoglutarate-dependent ethylene-forming enzyme: substrate binding creates a twist. J. Am. Chem. Soc. 139 (2017) 11980-11988. [PMID: 28780854]
Accepted name: (–)-deoxypodophyllotoxin synthase
Reaction: (–)-yatein + 2-oxoglutarate + O2 = (–)-deoxypodophyllotoxin + succinate + CO2 + H2O
For diagram of reaction click here.
Glossary: (–)-yatein = (3R,4R)-4-(1,3-benzodioxol-5-ylmethyl)-3-(3,4,5-trimethoxybenzyl)dihydrofuran-2(3H)-one
(–)-deoxypodophyllotoxin = (5R,5aR,8aR)-5-(3,4,5-trimethoxyphenyl)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5a)-one
Other name(s): 2-ODD (gene name)
Systematic name: (–)-yatein,2-oxoglutarate:oxygen oxidoreductase (ring-forming)
Comments: The enzyme, characterized from the plant Sinopodophyllum hexandrum (mayapple), is involved in the biosynthetic pathway of podophyllotoxin, a non-alkaloid toxin lignan whose derivatives are important anticancer drugs. It catalyses the closure of the central six-membered ring in the aryltetralin scaffold.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, 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: L-tyrosine isonitrile desaturase
Reaction: (2S)-3-(4-hydroxyphenyl)-2-isocyanopropanoate + 2-oxoglutarate + O2 = (2E)-3-(4-hydroxyphenyl)-2-isocyanoprop-2-enoate + succinate + CO2 + H2O
Glossary: (2S)-3-(4-hydroxyphenyl)-2-isocyanopropanoic acid = L-tyrosine isonitrile
paerucumarin = 6,7-dihydroxy-3-isocyanochromen-2-one
Other name(s): pvcB (gene name)
Systematic name: (2S)-3-(4-hydroxyphenyl)-2-isocyanopropanoate,2-oxoglutarate:oxygen oxidoreductase
Comments: The enzyme is a member of the Fe2+, 2-oxoglutarate-dependent oxygenases and requires Fe2+. It has been characterized from bacteria that form the isonitrile-functionalized compound paerucumarin. cf. EC 1.14.20.10, L-tyrosine isonitrile desaturase/decarboxylase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Clarke-Pearson, M.F. and Brady, S.F. Paerucumarin, a new metabolite produced by the pvc gene cluster from Pseudomonas aeruginosa. J. Bacteriol. 190 (2008) 6927-6930. [PMID: 18689486]
2. Drake, E.J. and Gulick, A.M. Three-dimensional structures of Pseudomonas aeruginosa PvcA and PvcB, two proteins involved in the synthesis of 2-isocyano-6,7-dihydroxycoumarin. J. Mol. Biol. 384 (2008) 193-205. [PMID: 18824174]
3. Zhu, J., Lippa, G.M., Gulick, A.M. and Tipton, P.A. Examining reaction specificity in PvcB, a source of diversity in isonitrile-containing natural products. Biochemistry 54 (2015) 2659-2669. [PMID: 25866990]
Accepted name: L-tyrosine isonitrile desaturase/decarboxylase
Reaction: (2S)-3-(4-hydroxyphenyl)-2-isocyanopropanoate + 2-oxoglutarate + O2 = 4-[(E)-2-isocyanoethenyl]phenol + succinate + 2 CO2 + H2O
Glossary: (2S)-3-(4-hydroxyphenyl)-2-isocyanopropanoic acid = L-tyrosine isonitrile
rhabduscin = N-[(2S,3S,4R,5S,6R)-4,5-dihydroxy-6-{4-[(E)-2-isocyanoethenyl]phenoxy}-2-methyloxan-3-yl]acetamide
Other name(s): pvcB (gene name)
Systematic name: (2S)-3-(4-hydroxyphenyl)-2-isocyanopropanoate,2-oxoglutarate:oxygen oxidoreductase (decarboxylating)
Comments: The enzyme, characterized from the bacterium Xenorhabdus nematophila, is involved in rhabduscin biosynthesis. The enzyme is a member of the Fe2+, 2-oxoglutarate-dependent oxygenases. It is similar to EC 1.14.20.9, L-tyrosine isonitrile desaturase. However, the latter does not catalyse a decarboxylation of the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Crawford, J.M., Portmann, C., Zhang, X., Roeffaers, M.B. and Clardy, J. Small molecule perimeter defense in entomopathogenic bacteria. Proc. Natl Acad. Sci. USA 109 (2012) 10821-10826. [PMID: 22711807]
2. Zhu, J., Lippa, G.M., Gulick, A.M. and Tipton, P.A. Examining reaction specificity in PvcB, a source of diversity in isonitrile-containing natural products. Biochemistry 54 (2015) 2659-2669. [PMID: 25866990]
Accepted name: 3-[(Z)-2-isocyanoethenyl]-1H-indole synthase
Reaction: (2S)-3-(1H-indol-3-yl)-2-isocyanopropanoate + 2-oxoglutarate + O2 = 3-[(Z)-2-isocyanoethenyl]-1H-indole + succinate + 2 CO2 + H2O
Glossary: (2S)-3-(1H-indol-3-yl)-2-isocyanopropanoate = L-tryptophan isonitrile
Other name(s): ambI3 (gene name); famH3 (gene name); L-tryptophan isonitrile desaturase/decarboxylase (3-[(Z)-2-isocyanoethenyl]-1H-indole-forming)
Systematic name: (2S)-3-(1H-indol-3-yl)-2-isocyanopropanoate,2-oxoglutarate:oxygen oxidoreductase (decarboxylating, 3-[(Z)-2-isocyanoethenyl]-1H-indole-forming)
Comments: The enzyme, characterized from the cyanobacterium Fischerella ambigua UTEX 1903, participates in the biosynthesis of hapalindole-type alkaloids. The enzyme catalyses an Fe2+, 2-oxoglutarate-dependent monooxygenation at C-3, which is followed by decarboxylation and dehydration, resulting in the generation of a cis C-C double bond. cf. EC 1.14.20.12, 3-[(E)-2-isocyanoethenyl]-1H-indole synthase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hillwig, M.L., Zhu, Q. and Liu, X. Biosynthesis of ambiguine indole alkaloids in cyanobacterium Fischerella ambigua. ACS Chem. Biol. 9 (2014) 372-377. [PMID: 24180436]
2. Chang, W.C., Sanyal, D., Huang, J.L., Ittiamornkul, K., Zhu, Q. and Liu, X. In vitro stepwise reconstitution of amino acid derived vinyl isocyanide biosynthesis: detection of an elusive intermediate. Org. Lett. 19 (2017) 1208-1211. [PMID: 28212039]
Accepted name: 3-[(E)-2-isocyanoethenyl]-1H-indole synthase
Reaction: (2S)-3-(1H-indol-3-yl)-2-isocyanopropanoate + 2-oxoglutarate + O2 = 3-[(E)-2-isocyanoethenyl]-1H-indole + succinate + 2 CO2 + H2O
Glossary: (2S)-3-(1H-indol-3-yl)-2-isocyanopropanoate = L-tryptophan isonitrile
Other name(s): isnB (gene name); L-tryptophan isonitrile desaturase/decarboxylase (3-[(E)-2-isocyanoethenyl]-1H-indole-forming)
Systematic name: (2S)-3-(1H-indol-3-yl)-2-isocyanopropanoate,2-oxoglutarate:oxygen oxidoreductase (decarboxylating, 3-[(E)-2-isocyanoethenyl]-1H-indole-forming)
Comments: The enzyme has been characterized from an unidentified soil bacterium. It catalyses an Fe2+, 2-oxoglutarate-dependent monooxygenation at C-3, which is followed by decarboxylation and dehydration, resulting in the generation of a trans C-C double bond. cf. EC 1.14.20.11, 3-[(Z)-2-isocyanoethenyl]-1H-indole synthase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Brady, S.F. and Clardy, J. Cloning and heterologous expression of isocyanide biosynthetic genes from environmental DNA. Angew Chem Int Ed Engl 44 (2005) 7063-7065. [PMID: 16206308]
2. Chang, W.C., Sanyal, D., Huang, J.L., Ittiamornkul, K., Zhu, Q. and Liu, X. In vitro stepwise reconstitution of amino acid derived vinyl isocyanide biosynthesis: detection of an elusive intermediate. Org. Lett. 19 (2017) 1208-1211. [PMID: 28212039]
Accepted name: 6β-hydroxyhyoscyamine epoxidase
Reaction: (6S)-6β-hydroxyhyoscyamine + 2-oxoglutarate + O2 = scopolamine + succinate + CO2 + H2O
For diagram of reaction click here.
Glossary: scopolamine = hyoscine = (1R,2R,4S,5S,7s)-9-methyl-3-oxa-9-azatricyclo[3.3.1.02,4]nonan-7-yl (2S)-3-hydroxy-2-phenylpropanoate
Other name(s): hydroxyhyoscyamine dioxygenase; (6S)-6-hydroxyhyoscyamine,2-oxoglutarate oxidoreductase (epoxide-forming)
Systematic name: (6S)-6β-hydroxyhyoscyamine,2-oxoglutarate:oxygen oxidoreductase (epoxide-forming)
Comments: Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hashimoto, T., Kohno, J. and Yamada, Y. 6β-Hydroxyhyoscyamine epoxidase from cultured roots of Hyoscyamus niger. Phytochemistry 28 (1989) 1077-1082.
Accepted name: hapalindole-type alkaloid chlorinase
Reaction: (1) hapalindole U + 2-oxoglutarate + O2 + chloride = hapalindole G + succinate + CO2 + H2O
(2)12-epi-fischerindole U + 2-oxoglutarate + O2 + chloride = 12-epi-fischerindole G + succinate + CO2 + H2O
For diagram of reaction click here.
Glossary: 12-epi-fischerindole U = (6aS,9S,10R,10aS)-9-ethenyl-10-isocyano-6,6,9-trimethyl-5,6,6a,7,8,9,10,10a-octahydroindeno[2,1-b]indole
12-epi-fischerindole G = (6aR,8R,9S,10R,10aS)-8-chloro-9-ethenyl-10-isocyano-6,6,9-trimethyl-5,6,6a,7,8,9,10,10a-octahydroindeno[2,1-b]indole
Other name(s): ambO5 (gene name); welO5 (gene name)
Systematic name: 12-epi-fischerindole U,2-oxoglutarate:oxygen oxidoreductase (13-halogenating)
Comments: The enzyme, characterized from hapalindole-type alkaloids-producing cyanobacteria, is a specialized Fe(II)/2-oxoglutarate-dependent oxygenase that catalyses the chlorination of its substrates in a reaction that requires oxygen, chloride ions, ferrous iron and 2-oxoglutarate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hillwig, M.L. and Liu, X. A new family of iron-dependent halogenases acts on freestanding substrates. Nat. Chem. Biol. 10 (2014) 921-923. [PMID: 25218740]
2. Zhu, Q., Hillwig, M.L., Doi, Y. and Liu, X. Aliphatic halogenase enables late-stage C-H functionalization: selective synthesis of a brominated fischerindole alkaloid with enhanced antibacterial activity. Chembiochem 17 (2016) 466-470. [PMID: 26749394]
3. Hillwig, M.L., Zhu, Q., Ittiamornkul, K. and Liu, X. Discovery of a promiscuous non-heme iron halogenase in ambiguine alkaloid biogenesis: implication for an evolvable enzyme family for late-stage halogenation of aliphatic carbons in small molecules. Angew Chem Int Ed Engl 55 (2016) 5780-5784. [PMID: 27027281]
Accepted name: L-threonyl-[L-threonyl-carrier protein] 4-chlorinase
Reaction: an L-threonyl-[L-threonyl-carrier protein] + 2-oxoglutarate + O2 + Cl- = a 4-chloro-L-threonyl-[L-threonyl-carrier protein] + succinate + CO2 + H2O
Other name(s): syrB2 (gene name)
Systematic name: L-threonyl-[L-threonyl-carrier protein],2-oxoglutarate:oxygen oxidoreductase (4-halogenating)
Comments: The enzyme, characterized from the bacterium Pseudomonas syringae, participates in syringomycin E biosynthesis. The enzyme is a specialized Fe(II)/2-oxoglutarate-dependent oxygenase that catalyses the chlorination of its substrate in a reaction that requires oxygen, chloride ions, ferrous iron and 2-oxoglutarate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Vaillancourt, F.H., Yin, J. and Walsh, C.T. SyrB2 in syringomycin E biosynthesis is a nonheme FeII α-ketoglutarate- and O2-dependent halogenase. Proc. Natl Acad. Sci. USA 102 (2005) 10111-10116. [PMID: 16002467]
Accepted name: 4α,5β-5,20-epoxytax-11-ene-4,9-diol 9-dehydrogenase
Reaction: 4α,5β-5,20-epoxytax-11-ene-4,9-diol + 2-oxoglutarate + O2 = 4-hydroxy-4α,5β-5,20-epoxytax-11-en-9-one + succinate + CO2 + H2O
Other name(s): T9α oxidase
Systematic name: 4α,5β-5,20-epoxytax-11-ene-4,9-diol,2-oxoglutarate:oxygen 9-oxidoreductase
Comments: The enzyme is active in the biosynthetic pathway of paclitaxel (Taxol) in Taxus species (yew).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Zhang, Y., Wiese, L., Fang, H., Alseekh, S., Perez de Souza, L., Scossa, F., Molloy, J., Christmann, M. and Fernie, A.R. Synthetic biology identifies the minimal gene set required for paclitaxel biosynthesis in a plant chassis. Mol. Plant 16 (2023) 1951-1961. [PMID: 37897038]
[EC 1.14.21.2 Transferred entry: (S)-cheilanthifoline synthase. Now EC 1.14.19.65, (S)-cheilanthifoline synthase (EC 1.14.21.2 created 2002, modified 2016, deleted 2018)]
[EC 1.14.21.3 Transferred entry: berbamunine synthase. Now EC 1.14.19.66, berbamunine synthase (EC 1.14.21.3 created 2002, deleted 2018)]
[EC 1.14.21.4 Transferred entry: salutaridine synthase. Now EC 1.14.19.67, salutaridine synthase (EC 1.14.21.4 created 2002, deleted 2018)]
[EC 1.14.21.5 Transferred entry: (S)-canadine synthase. Now EC 1.14.19.68, (S)-canadine synthase (EC 1.14.21.5 created 2002, deleted 2018)]
[EC 1.14.21.6 Transferred entry: lathosterol oxidase. Now EC 1.14.19.20, Δ7-sterol 5(6)-desaturase (EC 1.14.21.6 created 1972 as EC 1.3.3.2, transferred 2005 to EC 1.14.21.6, deleted 2015)]
[EC 1.14.21.7 Transferred entry: biflaviolin synthase. Now EC 1.14.19.69, biflaviolin synthase (EC 1.14.21.7 created 2008, deleted 2018)]
[EC 1.14.21.8 Transferred entry: pseudobaptigenin synthase. Now EC 1.14.19.63, pseudobaptigenin synthase. (EC 1.14.21.8 created 2011, deleted 2018)]
[EC 1.14.21.9 Transferred entry: mycocyclosin synthase. Now EC 1.14.19.70, mycocyclosin synthase (EC 1.14.21.9 created 2013, deleted 2018)]
[EC 1.14.21.10 Transferred entry: fumitremorgin C synthase. Now EC 1.14.19.71, fumitremorgin C synthase (EC 1.14.21.10 created 2013, deleted 2018)]
[EC 1.14.21.11 Transferred entry: (ndash)-pluviatolide synthase. Now EC 1.14.19.72, (ndash)-pluviatolide synthase (EC 1.14.21.11 created 2016, deleted 2018)]
[EC 1.14.21.12 Transferred entry: (S)-nandinine synthase. Now EC 1.14.19.73, (S)-nandinine synthase (EC 1.14.21.12 created 2016, deleted 2018)]