The Enzyme Database

Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB)

Proposed Changes to the Enzyme List

The entries below are proposed additions and amendments to the Enzyme Nomenclature list. The entries below are proposed additions and amendments to the Enzyme Nomenclature list. They were prepared for the NC-IUBMB by Kristian Axelsen, Sinéad Boyce, Richard Cammack, Ron Caspi, Minoru Kanehisa, Andrew McDonald, Gerry Moss, Dietmar Schomburg, Ida Schomburg and Keith Tipton. Comments and suggestions on these draft entries should be sent to Dr Andrew McDonald (Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland). The date on which an enzyme will be made official is appended after the EC number. To prevent confusion please do not quote new EC numbers until they are incorporated into the main list.

An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.

Contents

EC 1.1.1.301 D-arabitol-phosphate dehydrogenase
EC 1.1.5.6 formate dehydrogenase-N
EC 1.1.5.7 cyclic alcohol dehydrogenase (quinone)
EC 1.1.99.33 formate dehydrogenase (acceptor)
EC 1.2.1.77 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+)
EC 1.4.3.23 7-chloro-L-tryptophan oxidase
EC 1.7.5.1 nitrate reductase (quinone)
EC 1.8.1.16 glutathione amide reductase
EC 1.11.1.17 glutathione amide-dependent peroxidase
EC 1.13.12.17 dichloroarcyriaflavin A synthase
EC 1.14.12.21 benzoyl-CoA 2,3-dioxygenase
EC 1.14.13.111 methanesulfonate monooxygenase
EC 1.14.13.112 3-epi-6-deoxocathasterone 23-monooxygenase
EC 1.14.14.6 transferred
EC 1.14.15.8 steroid 15β-monooxygenase
EC 1.14.99.39 ammonia monooxygenase
EC 2.1.1.164 demethylrebeccamycin-D-glucose O-methyltransferase
EC 2.1.1.165 methyl halide transferase
EC 2.3.1.189 mycothiol synthase
EC 2.4.1.250 D-inositol-3-phosphate glycosyltransferase
EC 2.4.2.42 UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase
EC 2.7.7.68 2-phospho-L-lactate guanylyltransferase
EC 2.7.8.28 2-phospho-L-lactate transferase
EC 3.1.3.80 2,3-bisphosphoglycerate 3-phosphatase
EC 3.5.1.102 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5′-monophosphate deformylase
EC 3.5.1.103 N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-α-D-glucopyranoside deacetylase
EC 4.1.2.44 benzoyl-CoA-dihydrodiol lyase
EC 4.3.1.26 chromopyrrolate synthase
EC 4.3.3.5 4′-demethylrebeccamycin synthase

EC 1.1.1.301 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: D-arabitol-phosphate dehydrogenase
Reaction: D-arabitol 1-phosphate + NAD+ = D-xylulose 5-phosphate + NADH + H+
Other name(s): APDH; D-arabitol 1-phosphate dehydrogenase; D-arabitol 5-phosphate dehydrogenase
Systematic name: D-arabitol-phosphate:NAD+ oxidoreductase
Comments: This enzyme participates in arabitol catabolism. The enzyme also converts D-arabitol 5-phosphate to D-ribulose 5-phosphate at a lower rate [1].
References:
1.  Povelainen, M., Eneyskaya, E.V., Kulminskaya, A.A., Ivanen, D.R., Kalkkinen, N., Neustroev, K.N. and Miasnikov, A.N. Biochemical and genetic characterization of a novel enzyme of pentitol metabolism: D-arabitol-phosphate dehydrogenase. Biochem. J. 371 (2003) 191–197. [PMID: 12467497]
[EC 1.1.1.301 created 2010]
 
 
EC 1.1.5.6 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: formate dehydrogenase-N
Reaction: formate + a quinone = CO2 + a quinol
Other name(s): Fdh-N; FdnGHI; nitrate-inducible formate dehydrogenase; formate dehydrogenase N; FDH-N; nitrate inducible Fdn; nitrate inducible formate dehydrogenase
Systematic name: formate:quinone oxidoreductase
Comments: The enzyme contains molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters and two heme b groups. Formate dehydrogenase-N oxidizes formate in the periplasm, transferring electrons via the menaquinone pool in the cytoplasmic membrane to a dissimilatory nitrate reductase (EC 1.7.5.1), which transfers electrons to nitrate in the cytoplasm. The system generates proton motive force under anaerobic conditions [3].
References:
1.  Enoch, H.G. and Lester, R.L. The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli. J. Biol. Chem. 250 (1975) 6693–6705. [PMID: 1099093]
2.  Jormakka, M., Tornroth, S., Byrne, B. and Iwata, S. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science 295 (2002) 1863–1868. [PMID: 11884747]
3.  Jormakka, M., Tornroth, S., Abramson, J., Byrne, B. and Iwata, S. Purification and crystallization of the respiratory complex formate dehydrogenase-N from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 58 (2002) 160–162. [PMID: 11752799]
[EC 1.1.5.6 created 2010]
 
 
EC 1.1.5.7 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: cyclic alcohol dehydrogenase (quinone)
Reaction: a cyclic alcohol + a quinone = a cyclic ketone + a quinol
Other name(s): cyclic alcohol dehydrogenase; MCAD
Systematic name: cyclic alcohol:quinone oxidoreductase
Comments: This enzyme oxidizes a wide variety of cyclic alcohols. Some minor enzyme activity is found with aliphatic secondary alcohols and sugar alcohols, but not primary alcohols. The enzyme is unable to catalyse the reverse reaction of cyclic ketones or aldehydes to cyclic alcohols. This enzyme differs from EC 1.1.5.5, alcohol dehydrogenase (quinone), which shows activity with ethanol [1].
References:
1.  Moonmangmee, D., Fujii, Y., Toyama, H., Theeragool, G., Lotong, N., Matsushita, K. and Adachi, O. Purification and characterization of membrane-bound quinoprotein cyclic alcohol dehydrogenase from Gluconobacter frateurii CHM 9. Biosci. Biotechnol. Biochem. 65 (2001) 2763–2772. [PMID: 11826975]
[EC 1.1.5.7 created 2010]
 
 
EC 1.1.99.33 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: formate dehydrogenase (acceptor)
Reaction: formate + acceptor = CO2 + reduced acceptor
Other name(s): FDHH; FDH-H; FDH-O; formate dehydrogenase H; formate dehydrogenase O
Systematic name: formate:acceptor oxidoreductase
Comments: Formate dehydrogenase H is a cytoplasmic enzyme that oxidizes formate without oxygen transfer, transferring electrons to a hydrogenase. The two enzymes form the formate-hydrogen lyase complex [1]. The enzyme contains an [4Fe-4S] cluster, a selenocysteine residue and a molybdopterin cofactor [1].
References:
1.  Axley, M.J., Grahame, D.A. and Stadtman, T.C. Escherichia coli formate-hydrogen lyase. Purification and properties of the selenium-dependent formate dehydrogenase component. J. Biol. Chem. 265 (1990) 18213–18218. [PMID: 2211698]
2.  Gladyshev, V.N., Boyington, J.C., Khangulov, S.V., Grahame, D.A., Stadtman, T.C. and Sun, P.D. Characterization of crystalline formate dehydrogenase H from Escherichia coli. Stabilization, EPR spectroscopy, and preliminary crystallographic analysis. J. Biol. Chem. 271 (1996) 8095–8100. [PMID: 8626495]
3.  Khangulov, S.V., Gladyshev, V.N., Dismukes, G.C. and Stadtman, T.C. Selenium-containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer. Biochemistry 37 (1998) 3518–3528. [PMID: 9521673]
[EC 1.1.99.33 created 2010]
 
 
EC 1.2.1.77 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+)
Reaction: 3,4-didehydroadipyl-CoA semialdehyde + NADP+ + H2O = 3,4-didehydroadipyl-CoA + NADPH + H+
Other name(s): BoxD; 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase
Systematic name: 3,4-didehydroadipyl-CoA semialdehyde:NADP+ oxidoreductase
Comments: This enzyme catalyses a step in the aerobic benzoyl-coenzyme A catabolic pathway in Azoarcus evansii and Burkholderia xenovorans.
References:
1.  Gescher, J., Ismail, W., Olgeschlager, E., Eisenreich, W., Worth, J. and Fuchs, G. Aerobic benzoyl-coenzyme A (CoA) catabolic pathway in Azoarcus evansii: conversion of ring cleavage product by 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase. J. Bacteriol. 188 (2006) 2919–2927. [PMID: 16585753]
2.  Bains, J. and Boulanger, M.J. Structural and biochemical characterization of a novel aldehyde dehydrogenase encoded by the benzoate oxidation pathway in Burkholderia xenovorans LB400. J. Mol. Biol. 379 (2008) 597–608. [PMID: 18462753]
[EC 1.2.1.77 created 2010]
 
 
EC 1.4.3.23 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: 7-chloro-L-tryptophan oxidase
Reaction: 7-chloro-L-tryptophan + O2 = 2-imino-3-(7-chloroindol-3-yl)propanoate + H2O2
For diagram of rebeccamycin biosynthesis, click here
Other name(s): RebO
Systematic name: 7-chloro-L-tryptophan:oxygen oxidoreductase
Comments: Contains a noncovalently bound FAD [1,2]. This enzyme catalyses a step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the Actinobacterium Lechevalieria aerocolonigenes. During catalysis, the bound FAD is reoxidized at the expense of molecular oxygen, producing one molecule of hydrogen peroxide. The enzyme shows significant preference for 7-chloro-L-tryptophan over L-tryptophan [1].
References:
1.  Nishizawa, T., Aldrich, C.C. and Sherman, D.H. Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243. J. Bacteriol. 187 (2005) 2084–2092. [PMID: 15743957]
2.  Howard-Jones, A.R. and Walsh, C.T. Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD. Biochemistry 44 (2005) 15652–15663. [PMID: 16313168]
[EC 1.4.3.23 created 2010]
 
 
EC 1.7.5.1 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: nitrate reductase (quinone)
Reaction: nitrate + a quinol = nitrite + a quinone + H2O
Other name(s): nitrate reductase A; nitrate reductase Z; NarGHI; quinol/nitrate oxidoreductase; quinol-nitrate oxidoreductase; quinol:nitrate oxidoreductase; NarA; NarZ; NarGHI; dissimilatory nitrate reductase
Systematic name: nitrite:quinone oxidoreductase
Comments: A membrane-bound enzyme which supports anaerobic respiration on nitrate under anaerobic conditions and in the presence of nitrate. Contains the bicyclic form of the molybdo-bis(molybdopterin guanine dinucleotide) cofactor, iron-sulfur clusters and heme b. Escherichia coli expresses two forms NarA and NarZ, both being comprised of three subunits.
References:
1.  Enoch, H.G. and Lester, R.L. The role of a novel cytochrome b-containing nitrate reductase and quinone in the in vitro reconstruction of formate-nitrate reductase activity of E. coli. Biochem. Biophys. Res. Commun. 61 (1974) 1234–1241. [PMID: 4616697]
2.  Bertero, M.G., Rothery, R.A., Palak, M., Hou, C., Lim, D., Blasco, F., Weiner, J.H. and Strynadka, N.C. Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nat. Struct. Biol. 10 (2003) 681–687. [PMID: 12910261]
3.  Lanciano, P., Magalon, A., Bertrand, P., Guigliarelli, B. and Grimaldi, S. High-stability semiquinone intermediate in nitrate reductase A (NarGHI) from Escherichia coli is located in a quinol oxidation site close to heme bD. Biochemistry 46 (2007) 5323–5329. [PMID: 17439244]
4.  Bertero, M.G., Rothery, R.A., Boroumand, N., Palak, M., Blasco, F., Ginet, N., Weiner, J.H. and Strynadka, N.C. Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A. J. Biol. Chem. 280 (2005) 14836–14843. [PMID: 15615728]
5.  Bonnefoy, V. and Demoss, J.A. Nitrate reductases in Escherichia coli. Antonie Van Leeuwenhoek 66 (1994) 47–56. [PMID: 7747940]
6.  Guigliarelli, B., Asso, M., More, C., Augier, V., Blasco, F., Pommier, J., Giordano, G. and Bertrand, P. EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism. Eur. J. Biochem. 207 (1992) 61–68. [PMID: 1321049]
[EC 1.7.5.1 created 2010]
 
 
EC 1.8.1.16 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: glutathione amide reductase
Reaction: 2 glutathione amide + NAD+ = glutathione amide disulfide + NADH + H+
Other name(s): GAR
Systematic name: glutathione amide:NAD+ oxidoreductase
Comments: A dimeric flavoprotein (FAD). The enzyme restores glutathione amide disulfide, which is produced during the reduction of peroxide by EC 1.11.1.17 (glutathione amide-dependent peroxidase), back to glutathione amide (it catalyses the reaction in the opposite direction to that shown). The enzyme belongs to the family of flavoprotein disulfide oxidoreductases, but unlike other members of the family, which are specific for NADPH, it prefers NADH [1].
References:
1.  Vergauwen, B., Pauwels, F., Jacquemotte, F., Meyer, T.E., Cusanovich, M.A., Bartsch, R.G. and Van Beeumen, J.J. Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling. J. Biol. Chem. 276 (2001) 20890–20897. [PMID: 11399772]
2.  Vergauwen, B., Van Petegem, F., Remaut, H., Pauwels, F. and Van Beeumen, J.J. Crystallization and preliminary X-ray crystallographic analysis of glutathione amide reductase from Chromatium gracile. Acta Crystallogr. D Biol. Crystallogr. 58 (2002) 339–340. [PMID: 11807270]
[EC 1.8.1.16 created 2010]
 
 
EC 1.11.1.17 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: glutathione amide-dependent peroxidase
Reaction: 2 glutathione amide + H2O2 = glutathione amide disulfide + 2 H2O
Systematic name: glutathione amide:hydrogen-peroxide oxidoreductase
Comments: This enzyme, which has been characterized from the proteobacterium Marichromatium gracile, is a chimeric protein, containing a peroxiredoxin-like N-terminus and a glutaredoxin-like C terminus. The enzyme has peroxidase activity towards hydrogen peroxide and several small alkyl hydroperoxides, and is thought to represent an early adaptation for fighting oxidative stress [1]. The glutathione amide disulfide produced by this enzyme can be restored to glutathione amide by EC 1.8.1.16 (glutathione amide reductase).
References:
1.  Vergauwen, B., Pauwels, F., Jacquemotte, F., Meyer, T.E., Cusanovich, M.A., Bartsch, R.G. and Van Beeumen, J.J. Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling. J. Biol. Chem. 276 (2001) 20890–20897. [PMID: 11399772]
[EC 1.11.1.17 created 2010]
 
 
EC 1.13.12.17 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: dichloroarcyriaflavin A synthase
Reaction: dichlorochromopyrrolate + 3 O2 + 3 NADH + 3 H+ = dichloroarcyriaflavin A + 2 CO2 + 4 H2O + 3 NAD+
For diagram of rebeccamycin biosynthesis, click here
Glossary: dichloro-arcyriaflavin A = rebeccamycin aglycone
Comments: The conversion of dichlorochromopyrrolate to dichloroarcyriaflavin A is a complex process that involves two enzyme components. RebP is an NAD-dependent cytochrome P450 oxygenase that performs an aryl-aryl bond formation yielding the six-ring indolocarbazole scaffold [1]. Along with RebC, a flavin-dependent hydroxylase, it also catalyses the oxidative decarboxylation of both carboxyl groups. The presence of RebC ensures that the only product is the rebeccamycin aglycone dichloroarcyriaflavin A [2]. The enzymes are similar, but not identical, to StaP and StaC, which are involved in the synthesis of staurosporine [3].
References:
1.  Makino, M., Sugimoto, H., Shiro, Y., Asamizu, S., Onaka, H. and Nagano, S. Crystal structures and catalytic mechanism of cytochrome P450 StaP that produces the indolocarbazole skeleton. Proc. Natl. Acad. Sci. USA 104:1159 (2007). [PMID: 17606921]
2.  Howard-Jones, A.R. and Walsh, C.T. Staurosporine and rebeccamycin aglycones are assembled by the oxidative action of StaP, StaC, and RebC on chromopyrrolic acid. J. Am. Chem. Soc. 128:1228 (2006). [PMID: 16967980]
3.  Sanchez, C., Zhu, L., Brana, A.F., Salas, A.P., Rohr, J., Mendez, C. and Salas, J.A. Combinatorial biosynthesis of antitumor indolocarbazole compounds. Proc. Natl. Acad. Sci. USA 102:461 (2005). [PMID: 15625109]
[EC 1.13.12.17 created 2010]
 
 
EC 1.14.12.21 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: benzoyl-CoA 2,3-dioxygenase
Reaction: benzoyl-CoA + NADPH + H+ + O2 = 2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+
Other name(s): benzoyl-CoA dioxygenase/reductase; BoxBA; BoxA/BoxB system
Systematic name: benzoyl-CoA,NADPH:oxygen oxidoreductase (2,3-hydroxylating)
Comments: The enzyme is involved in aerobic benzoate metabolism in Azoarcus evansii. BoxB functions as the oxygenase part of benzoyl-CoA oxygenase in conjunction with BoxA, the reductase component, which upon binding of benzoyl-CoA, transfers two electrons to the ring in the course of dioxygenation. BoxA is a homodimeric 46 kDa iron-sulphur-flavoprotein (FAD), BoxB is a monomeric iron-protein [1].
References:
1.  Zaar, A., Gescher, J., Eisenreich, W., Bacher, A. and Fuchs, G. New enzymes involved in aerobic benzoate metabolism in Azoarcus evansii. Mol. Microbiol. 54 (2004) 223–238. [PMID: 15458418]
2.  Gescher, J., Zaar, A., Mohamed, M., Schagger, H. and Fuchs, G. Genes coding for a new pathway of aerobic benzoate metabolism in Azoarcus evansii. J. Bacteriol. 184 (2002) 6301–6315. [PMID: 12399500]
3.  Mohamed, M.E., Zaar, A., Ebenau-Jehle, C. and Fuchs, G. Reinvestigation of a new type of aerobic benzoate metabolism in the proteobacterium Azoarcus evansii. J. Bacteriol. 183 (2001) 1899–1908. [PMID: 11222587]
[EC 1.14.12.21 created 2010]
 
 
EC 1.14.13.111 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: methanesulfonate monooxygenase
Reaction: methanesulfonate + NADH + H+ + O2 = formaldehyde + NAD+ + sulfite + H2O
Glossary: methanesulfonate = CH3-SO3-
formaldehyde = H-CHO
Other name(s): mesylate monooxygenase; mesylate,reduced-FMN:oxygen oxidoreductase; MsmABC; methanesulfonic acid monooxygenase; MSA monooxygenase; MSAMO
Systematic name: methanesulfonate,FMNH2:oxygen oxidoreductase
Comments: A flavoprotein. Methanesulfonate is the simplest of the sulfonates and is a substrate for the growth of certain methylotrophic microorganisms. Compared with EC 1.14.14.5, alkanesulfonate monooxygenase, this enzyme has a restricted substrate range that includes only the short-chain aliphatic sulfonates (methanesulfonate to butanesulfonate) and excludes all larger molecules, such as arylsulfonates [1]. The enzyme from the bacterium Methylosulfonomonas methylovora is a multicomponent system comprising a hydroxylase, a reductase (MsmD; EC 1.5.1.29, FMN reductase) and a ferredoxin (MsmC). The hydroxylase has both large (MsmA) and small (MsmB) subunits, with each large subunit containing a Rieske-type [2Fe-2S] centre.
References:
1.  de Marco, P., Moradas-Ferreira, P., Higgins, T.P., McDonald, I., Kenna, E.M. and Murrell, J.C. Molecular analysis of a novel methanesulfonic acid monooxygenase from the methylotroph Methylosulfonomonas methylovora. J. Bacteriol. 181 (1999) 2244–2251. [PMID: 10094704]
2.  Higgins, T.P., Davey, M., Trickett, J., Kelly, D.P. and Murrell, J.C. Metabolism of methanesulfonic acid involves a multicomponent monooxygenase enzyme. Microbiology 142 (1996) 251–260. [PMID: 8932698]
[EC 1.14.13.111 created 2009 as EC 1.14.14.6, transferred 2010 to EC 1.14.13.111]
 
 
EC 1.14.13.112 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: 3-epi-6-deoxocathasterone 23-monooxygenase
Reaction: (1) 3-epi-6-deoxocathasterone + NADPH + H+ + O2 = 6-deoxotyphasterol + NADP+ + H2O
(2) (22S,24R)-22-hydroxy-5α-ergostan-3-one + NADPH + H+ + O2 = 3-dehydro-6-deoxoteasterone + NADP+ + H2O
Other name(s): cytochrome P450 90C1; CYP90D1; CYP90C1
Systematic name: 3-epi-6-deoxocathasterone,NADPH:oxygen oxidoreductase (C-23-hydroxylating)
Comments: This enzyme is involved in brassinosteroid biosynthesis. C-23 hydroxylation shortcuts bypass campestanol, 6-deoxocathasterone, and 6-deoxoteasterone and lead directly from (22S,24R)-22-hydroxy-5α-ergostan-3-one and 3-epi-6-deoxocathasterone to 3-dehydro-6-deoxoteasterone and 6-deoxotyphasterol [1].
References:
1.  Ohnishi, T., Szatmari, A.M., Watanabe, B., Fujita, S., Bancos, S., Koncz, C., Lafos, M., Shibata, K., Yokota, T., Sakata, K., Szekeres, M. and Mizutani, M. C-23 hydroxylation by Arabidopsis CYP90C1 and CYP90D1 reveals a novel shortcut in brassinosteroid biosynthesis. Plant Cell 18 (2006) 3275–3288. [PMID: 17138693]
[EC 1.14.13.112 created 2010]
 
 
EC 1.14.14.6 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Transferred entry: methanesulfonate monooxygenase. Now EC 1.14.13.111, methanesulfonate monooxygenase. Formerly thought to involve FMNH2 but now shown to use NADH.
[EC 1.14.14.6 created 2009, transferred 2010 to EC 1.14.13.111]
 
 
EC 1.14.15.8 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: steroid 15β-monooxygenase
Reaction: progesterone + reduced ferredoxin + O2 = 15β-hydroxyprogesterone + oxidized ferredoxin + H2O
Other name(s): cytochrome P-450meg; cytochrome P450meg; steroid 15β-hydroxylase; CYP106A2; BmCYP106A2
Systematic name: progesterone,reduced-ferredoxin:oxygen oxidoreductase (15β-hydroxylating)
Comments: The enzyme from Bacillus megaterium hydroxylates a variety of 3-oxo-Δ4-steroids in position 15β. Ring A-reduced, aromatic, and 3β-hydroxy-Δ4-steroids do not serve as substrates [2].
References:
1.  Berg, A., Ingelman-Sundberg, M. and Gustafsson, J.A. Purification and characterization of cytochrome P-450meg. J. Biol. Chem. 254 (1979) 5264–5271. [PMID: 109432]
2.  Berg, A., Gustafsson, J.A. and Ingelman-Sundberg, M. Characterization of a cytochrome P-450-dependent steroid hydroxylase system present in Bacillus megaterium. J. Biol. Chem. 251 (1976) 2831–2838. [PMID: 177422]
3.  Lisurek, M., Kang, M.J., Hartmann, R.W. and Bernhardt, R. Identification of monohydroxy progesterones produced by CYP106A2 using comparative HPLC and electrospray ionisation collision-induced dissociation mass spectrometry. Biochem. Biophys. Res. Commun. 319 (2004) 677–682. [PMID: 15178459]
4.  Goni, G., Zollner, A., Lisurek, M., Velazquez-Campoy, A., Pinto, S., Gomez-Moreno, C., Hannemann, F., Bernhardt, R. and Medina, M. Cyanobacterial electron carrier proteins as electron donors to CYP106A2 from Bacillus megaterium ATCC 13368. Biochim. Biophys. Acta 1794 (2009) 1635–1642. [PMID: 19635596]
5.  Lisurek, M., Simgen, B., Antes, I. and Bernhardt, R. Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation. Chembiochem 9 (2008) 1439–1449. [PMID: 18481342]
[EC 1.14.15.8 created 2010]
 
 
EC 1.14.99.39 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: ammonia monooxygenase
Reaction: ammonia + AH2 + O2 = NH2OH + A + H2O
Other name(s): AMO
Comments: Contains copper and possibly nonheme iron. The donor is membrane-bound. Electrons are derived indirectly from ubiquinol.
References:
1.  Hyman, M.R., Page, C.L. and Arp, D.J. Oxidation of methyl fluoride and dimethyl ether by ammonia monooxygenase in Nitrosomonas europaea. Appl. Environ. Microbiol. 60 (1994) 3033–3035. [PMID: 8085841]
2.  Bergmann, D.J. and Hooper, A.B. Sequence of the gene, amoB, for the 43-kDa polypeptide of ammonia monoxygenase of Nitrosomonas europaea. Biochem. Biophys. Res. Commun. 204 (1994) 759–762. [PMID: 7980540]
3.  Holmes, A.J., Costello, A., Lidstrom, M.E. and Murrell, J.C. Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related. FEMS Microbiol. Lett. 132 (1995) 203–208. [PMID: 7590173]
4.  Zahn, J.A., Arciero, D.M., Hooper, A.B. and DiSpirito, A.A. Evidence for an iron center in the ammonia monooxygenase from Nitrosomonas europaea. FEBS Lett. 397 (1996) 35–38. [PMID: 8941709]
5.  Moir, J.W., Crossman, L.C., Spiro, S. and Richardson, D.J. The purification of ammonia monooxygenase from Paracoccus denitrificans. FEBS Lett. 387 (1996) 71–74. [PMID: 8654570]
6.  Whittaker, M., Bergmann, D., Arciero, D. and Hooper, A.B. Electron transfer during the oxidation of ammonia by the chemolithotrophic bacterium Nitrosomonas europaea. Biochim. Biophys. Acta 1459 (2000) 346–355. [PMID: 11004450]
7.  Arp, D.J., Sayavedra-Soto, L.A. and Hommes, N.G. Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea. Arch. Microbiol. 178 (2002) 250–255. [PMID: 12209257]
8.  Gilch, S., Meyer, O. and Schmidt, I. A soluble form of ammonia monooxygenase in Nitrosomonas europaea. Biol. Chem. 390 (2009) 863–873. [PMID: 19453274]
9.  Rasche, M.E., Hicks, R.E., Hyman, M.R. and Arp, D.J. Oxidation of monohalogenated ethanes and n-chlorinated alkanes by whole cells of Nitrosomonas europaea. J. Bacteriol. 172 (1990) 5368–5373. [PMID: 2394686]
[EC 1.14.99.39 created 2010]
 
 
EC 2.1.1.164 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: demethylrebeccamycin-D-glucose O-methyltransferase
Reaction: 4′-demethylrebeccamycin + S-adenosyl-L-methionine = rebeccamycin + S-adenosyl-L-homocysteine
For diagram of rebeccamycin biosynthesis, click here
Other name(s): RebM
Systematic name: S-adenosyl-L-methionine:demethylrebeccamycin-D-glucose O-methyltransferase
Comments: Catalyses the last step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the Actinobacterium Lechevalieria aerocolonigenes. The enzyme is able to use a wide variety substrates, tolerating variation on the imide heterocycle, deoxygenation of the sugar moiety, and even indolocarbazole glycoside anomers [1]. The enzyme is a member of the general acid/base-dependent O-methyltransferase family [2].
References:
1.  Zhang, C., Albermann, C., Fu, X., Peters, N.R., Chisholm, J.D., Zhang, G., Gilbert, E.J., Wang, P.G., Van Vranken, D.L. and Thorson, J.S. RebG- and RebM-catalyzed indolocarbazole diversification. Chembiochem 7 (2006) 795–804. [PMID: 16575939]
2.  Singh, S., McCoy, J.G., Zhang, C., Bingman, C.A., Phillips, G.N., Jr. and Thorson, J.S. Structure and mechanism of the rebeccamycin sugar 4′-O-methyltransferase RebM. J. Biol. Chem. 283 (2008) 22628–22636. [PMID: 18502766]
[EC 2.1.1.164 created 2010]
 
 
EC 2.1.1.165 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: methyl halide transferase
Reaction: S-adenosyl-L-methionine + iodide = S-adenosyl-L-homocysteine + methyl iodide
Other name(s): MCT; methyl chloride transferase; S-adenosyl-L-methionine:halide/bisulfide methyltransferase; AtHOL1; AtHOL2; AtHOL3; HARMLESS TO OZONE LAYER protein; HMT; S-adenosyl-L-methionine: halide ion methyltransferase; SAM:halide ion methyltransferase
Systematic name: S-adenosylmethionine:iodide methyltransferase
Comments: This enzyme contributes to the methyl halide emissions from Arabidopsis [6].
References:
1.  Ni, X. and Hager, L.P. Expression of Batis maritima methyl chloride transferase in Escherichia coli. Proc. Natl. Acad. Sci. USA 96 (1999) 3611–3615. [PMID: 10097085]
2.  Saxena, D., Aouad, S., Attieh, J. and Saini, H.S. Biochemical characterization of chloromethane emission from the wood-rotting fungus Phellinus pomaceus. Appl. Environ. Microbiol. 64 (1998) 2831–2835. [PMID: 9687437]
3.  Attieh, J.M., Hanson, A.D. and Saini, H.S. Purification and characterization of a novel methyltransferase responsible for biosynthesis of halomethanes and methanethiol in Brassica oleracea. J. Biol. Chem. 270 (1995) 9250–9257. [PMID: 7721844]
4.  Itoh, N., Toda, H., Matsuda, M., Negishi, T., Taniguchi, T. and Ohsawa, N. Involvement of S-adenosylmethionine-dependent halide/thiol methyltransferase (HTMT) in methyl halide emissions from agricultural plants: isolation and characterization of an HTMT-coding gene from Raphanus sativus (daikon radish). BMC Plant Biol. 9 (2009) 116. [PMID: 19723322]
5.  Ohsawa, N., Tsujita, M., Morikawa, S. and Itoh, N. Purification and characterization of a monohalomethane-producing enzyme S-adenosyl-L-methionine: halide ion methyltransferase from a marine microalga, Pavlova pinguis. Biosci. Biotechnol. Biochem. 65 (2001) 2397–2404. [PMID: 11791711]
6.  Nagatoshi, Y.and Nakamura, T. Characterization of three halide methyltransferases in Arabidopsis thaliana. Plant Biotechnol 24 (2007) 503–506.
[EC 2.1.1.165 created 2010]
 
 
EC 2.3.1.189 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: mycothiol synthase
Reaction: desacetylmycothiol + acetyl-CoA = mycothiol + coenzyme-A
For diagram of mycothiol biosynthesis, click here
Glossary: desacetylmycothiol = 1-O-[2-(L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol
mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol
Other name(s): MshD
Systematic name: acetyl-CoA:desacetylmycothiol O-acetyltransferase
Comments: This enzyme catalyses the last step in the biosynthesis of mycothiol, the major thiol in most actinomycetes, including Mycobacterium [1]. The enzyme is a member of a large family of GCN5-related N-acetyltransferases (GNATs) [2]. The enzyme has been purified from Mycobacterium tuberculosis H37Rv. Acetyl-CoA is the preferred CoA thioester but propionyl-CoA is also a substrate [3].
References:
1.  Spies, H.S. and Steenkamp, D.J. Thiols of intracellular pathogens. Identification of ovothiol A in Leishmania donovani and structural analysis of a novel thiol from Mycobacterium bovis. Eur. J. Biochem. 224 (1994) 203–213. [PMID: 8076641]
2.  Koledin, T., Newton, G.L. and Fahey, R.C. Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes. Arch. Microbiol. 178 (2002) 331–337. [PMID: 12375100]
3.  Vetting, M.W., Roderick, S.L., Yu, M. and Blanchard, J.S. Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases. Protein Sci. 12 (2003) 1954–1959. [PMID: 12930994]
[EC 2.3.1.189 created 2010]
 
 
EC 2.4.1.250 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: D-inositol-3-phosphate glycosyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + 1D-myo-inositol 3-phosphate = 1-O-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol 3-phosphate + UDP
For diagram of mycothiol biosynthesis, click here
Other name(s): mycothiol glycosyltransferases; MshA
Systematic name: UDP-N-acetyl-D-glucosamine:1D-myo-inositol 3-phosphate α-D-glycosyltransferase
Comments: The enzyme, which belongs to the GT-B fold superfamily, catalyses the first dedicated reaction in the biosynthesis of mycothiol [1]. The substrate was initially believed to be inositol, but eventually shown to be D-myo-inositol 3-phosphate [2]. A substantial conformational change occurs upon UDP binding, which generates the binding site for D-myo-inositol 3-phosphate [3]
References:
1.  Newton, G.L., Koledin, T., Gorovitz, B., Rawat, M., Fahey, R.C. and Av-Gay, Y. The glycosyltransferase gene encoding the enzyme catalyzing the first step of mycothiol biosynthesis (mshA). J. Bacteriol. 185 (2003) 3476–3479. [PMID: 12754249]
2.  Newton, G.L., Ta, P., Bzymek, K.P. and Fahey, R.C. Biochemistry of the initial steps of mycothiol biosynthesis. J. Biol. Chem. 281 (2006) 33910–33920. [PMID: 16940050]
3.  Vetting, M.W., Frantom, P.A. and Blanchard, J.S. Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: substrate-assisted catalysis. J. Biol. Chem. 283 (2008) 15834–15844. [PMID: 18390549]
[EC 2.4.1.250 created 2010]
 
 
EC 2.4.2.42 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase
Reaction: UDP-D-xylose + Glcβ-Ser53-EGF-like domain of bovine factor IX(45-87) = UDP + Xylα(1-3)Glcβ-Ser53-EGF-like domain of bovine factor IX(45-87)
Other name(s): β-glucoside α-1,3-xylosyltransferase
Systematic name: UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase
Comments: The enzyme is involved in the biosynthesis of the Xylα(1-3)Xylα(1-3)Glcβ-1-O-Ser on epidermal growth factor-like domains [1].
References:
1.  Ishimizu, T., Sano, K., Uchida, T., Teshima, H., Omichi, K., Hojo, H., Nakahara, Y. and Hase, S. Purification and substrate specificity of UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xyl α1-3Xyl α1-3Glc β1-O-Ser on epidermal growth factor-like domains. J. Biochem. 141 (2007) 593–600. [PMID: 17317689]
2.  Omichi, K., Aoki, K., Minamida, S. and Hase, S. Presence of UDP-D-xylose: β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xyl α 1-3Glc β-Ser structure of glycoproteins in the human hepatoma cell line HepG2. Eur. J. Biochem. 245 (1997) 143–146. [PMID: 9128735]
[EC 2.4.2.42 created 2010]
 
 
EC 2.7.7.68 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: 2-phospho-L-lactate guanylyltransferase
Reaction: (2S)-2-phospholactate + GTP = (2S)-lactyl-2-diphospho-5′-guanosine + diphosphate
Glossary: (2S)-2-phospholactate = (2S)-2-(phosphonooxy)propanoate
Other name(s): CofC; MJ0887
Systematic name: GTP:2-phospho-L-lactate guanylyltransferase
Comments: This enzyme is involved in the biosynthesis of coenzyme F420, a redox-active cofactor found in all methanogenic archaea, as well as some eubacteria.
References:
1.  Grochowski, L.L., Xu, H. and White, R.H. Identification and characterization of the 2-phospho-L-lactate guanylyltransferase involved in coenzyme F420 biosynthesis. Biochemistry 47 (2008) 3033–3037. [PMID: 18260642]
[EC 2.7.7.68 created 2010]
 
 
EC 2.7.8.28 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: 2-phospho-L-lactate transferase
Reaction: (2S)-lactyl-2-diphospho-5′-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = guanosine 5′-phosphate + coenzyme F420-0
Other name(s): LPPG:Fo 2-phospho-L-lactate transferase; LPPG:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase; MJ1256, lactyl-2-diphospho-(5′)guanosine:Fo 2-phospho-L-lactate transferase; CofD
Systematic name: (2S)-lactyl-2-diphospho-5′-guanosine:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase
Comments: This enzyme is involved in the biosynthesis of coenzyme F420, a redox-active cofactor found in all methanogenic archaea, as well as some eubacteria.
References:
1.  Graupner, M., Xu, H. and White, R.H. Characterization of the 2-phospho-L-lactate transferase enzyme involved in coenzyme F420 biosynthesis in Methanococcus jannaschii. Biochemistry 41 (2002) 3754–3761. [PMID: 11888293]
2.  Forouhar, F., Abashidze, M., Xu, H., Grochowski, L.L., Seetharaman, J., Hussain, M., Kuzin, A., Chen, Y., Zhou, W., Xiao, R., Acton, T.B., Montelione, G.T., Galinier, A., White, R.H. and Tong, L. Molecular insights into the biosynthesis of the F420 coenzyme. J. Biol. Chem. 283 (2008) 11832–11840. [PMID: 18252724]
[EC 2.7.8.28 created 2010]
 
 
EC 3.1.3.80 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: 2,3-bisphosphoglycerate 3-phosphatase
Reaction: 2,3-bisphospho-D-glycerate + H2O = 2-phospho-D-glycerate + phosphate
Other name(s): MIPP1; 2,3-BPG 3-phosphatase
Systematic name: 2,3-bisphospho-D-glycerate 3-phosphohydrolase
Comments: This reaction is a shortcut in the Rapoport-Luebering shunt. It bypasses the reactions of EC 3.1.3.13/EC 5.4.2.1 (bisphosphoglycerate phosphatase/phosphoglycerate mutase) and directly forms 2-phospho-D-glycerate by removing the 3-phospho-group of 2,3-diphospho-D-glycerate [1]. The MIPP1 protein also catalyses the reaction of EC 3.1.3.62 (multiple inositol-polyphosphate phosphatase).
References:
1.  Cho, J., King, J.S., Qian, X., Harwood, A.J. and Shears, S.B. Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt. Proc. Natl. Acad. Sci. USA 105 (2008) 5998–6003. [PMID: 18413611]
[EC 3.1.3.80 created 2010]
 
 
EC 3.5.1.102 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5′-monophosphate deformylase
Reaction: 2-amino-5-formylamino-6-(D-ribosylamino)pyrimidin-4(3H)-one 5′-phosphate + H2O = 2,5-diamino-6-(D-ribosylamino)pyrimidin-4(3H)-one 5′-phosphate + formate
Other name(s): ArfB
Systematic name: 2-amino-5-formylamino-6-(D-ribosylamino)pyrimidin-4(3H)-one 5′-phosphate amidohydrolase
Comments: The enzyme catalyses the second step in archaeal riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin biosynthesis. The first step is catalysed by EC 3.5.4.29 (GTP cyclohydrolase IIa). The bacterial enzyme, EC 3.5.4.25 (GTP cyclohydrolase II) catalyses both reactions.
References:
1.  Grochowski, L.L., Xu, H. and White, R.H. An iron(II) dependent formamide hydrolase catalyzes the second step in the archaeal biosynthetic pathway to riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin. Biochemistry 48 (2009) 4181–4188. [PMID: 19309161]
[EC 3.5.1.102 created 2010]
 
 
EC 3.5.1.103 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-α-D-glucopyranoside deacetylase
Reaction: 1-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol + H2O = 1-(2-amino-2-deoxy-α-D-glucopyranoside)-1D-myo-inositol + acetate
For diagram of mycothiol biosynthesis, click here
Other name(s): MshB
Systematic name: 1-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol acetylhydrolase
Comments: This enzyme is considered the key enzyme and rate limiting step in the mycothiol biosynthesis pathway [1]. In addition to acetylase activity, the enzyme possesses weak mycothiol conjugate amidase activity, and shares sequence similarity with mycothiol S-conjugate amidase [2]. The enzyme requires a divalent transition metal ion for activity, believed to be Zn2+ [3].
References:
1.  Rawat, M., Kovacevic, S., Billman-Jacobe, H. and Av-Gay, Y. Inactivation of mshB, a key gene in the mycothiol biosynthesis pathway in Mycobacterium smegmatis. Microbiology 149 (2003) 1341–1349. [PMID: 12724395]
2.  Newton, G.L., Av-Gay, Y. and Fahey, R.C. N-Acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis. J. Bacteriol. 182 (2000) 6958–6963. [PMID: 11092856]
3.  Maynes, J.T., Garen, C., Cherney, M.M., Newton, G., Arad, D., Av-Gay, Y., Fahey, R.C. and James, M.N. The crystal structure of 1-D-myo-inosityl 2-acetamido-2-deoxy-α-D-glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold. J. Biol. Chem. 278 (2003) 47166–47170. [PMID: 12958317]
[EC 3.5.1.103 created 2010]
 
 
EC 4.1.2.44 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: benzoyl-CoA-dihydrodiol lyase
Reaction: 2,3-dihydro-2,3-dihydroxybenzoyl-CoA + H2O = 3,4-didehydroadipyl-CoA semialdehyde + formate
Other name(s): 2,3-dihydro-2,3-dihydroxybenzoyl-CoA lyase/hydrolase (deformylating); BoxC; dihydrodiol transforming enzyme; benzoyl-CoA oxidation component C
Systematic name: 2,3-dihydro-2,3-dihydroxybenzoyl-CoA 3,4-didehydroadipyl-CoA semialdehyde-lyase (formate-forming)
Comments: The enzyme is involved in the aerobic benzoyl-CoA catabolic pathway in Azoarcus evansii. In a previous step benzoyl-CoA is oxidized to 2,3-dihydro-2,3-dihydroxybenzoyl-CoA (benzoyl-CoA dihydrodiol) by EC 1.14.12.21 (benzoyl-CoA 2,3-dioxygenase) in the presence of molecular oxygen [1].
References:
1.  Gescher, J., Eisenreich, W., Worth, J., Bacher, A. and Fuchs, G. Aerobic benzoyl-CoA catabolic pathway in Azoarcus evansii: studies on the non-oxygenolytic ring cleavage enzyme. Mol. Microbiol. 56 (2005) 1586–1600. [PMID: 15916608]
[EC 4.1.2.44 created 2010]
 
 
EC 4.3.1.26 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: chromopyrrolate synthase
Reaction: 2 2-imino-3-(7-chloroindol-3-yl)propanoate = dichlorochromopyrrolate + ammonium
For diagram of rebeccamycin biosynthesis, click here
Other name(s): RebD; chromopyrrolic acid synthase
Comments: This enzyme catalyses a step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the Actinobacterium Lechevalieria aerocolonigenes. The enzyme is a dimeric heme-protein oxidase that catalyses the oxidative dimerization of two L-tryptophan-derived molecules to form dichlorochromopyrrolic acid, the precursor for the fused six-ring indolocarbazole scaffold of rebeccamycin [1]. Contains one molecule of heme b per monomer, as well as non-heme iron that is not part of an iron-sulfur center [2]. The enzyme also possesses catalase activity.
References:
1.  Nishizawa, T., Gruschow, S., Jayamaha, D.H., Nishizawa-Harada, C. and Sherman, D.H. Enzymatic assembly of the bis-indole core of rebeccamycin. J. Am. Chem. Soc. 128 (2006) 724–725. [PMID: 16417354]
2.  Howard-Jones, A.R. and Walsh, C.T. Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD. Biochemistry 44 (2005) 15652–15663. [PMID: 16313168]
[EC 4.3.1.26 created 2010]
 
 
EC 4.3.3.5 – public review until 01 April 2010 [Last modified: 2010-03-04 13:05:59]
Accepted name: 4′-demethylrebeccamycin synthase
Reaction: 4′-O-demethylrebeccamycin + H2O = dichloro-arcyriaflavin A + β-D-glucose
For diagram of rebeccamycin biosynthesis, click here
Glossary: dichloro-arcyriaflavin A = rebeccamycin aglycone
Other name(s): arcyriaflavin A N-glycosyltransferase; RebG
Systematic name: 4′-demethylrebeccamycin D-glucose-lyase
Comments: This enzyme catalyses a step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the Actinobacterium Lechevalieria aerocolonigenes. The enzyme is a glycosylase, and acts in the reverse direction to that shown. It has a wide substrate range, and was shown to glycosylate several substrates, including the staurosporine aglycone, EJG-III-108A, J-104303, 6-N-methyl-arcyriaflavin C and indolo-[2,3-a]-carbazole [1,2].
References:
1.  Ohuchi, T., Ikeda-Araki, A., Watanabe-Sakamoto, A., Kojiri, K., Nagashima, M., Okanishi, M. and Suda, H. Cloning and expression of a gene encoding N-glycosyltransferase (ngt) from Saccharothrix aerocolonigenes ATCC39243. J. Antibiot. (Tokyo) 53 (2000) 393–403. [PMID: 10866221]
2.  Zhang, C., Albermann, C., Fu, X., Peters, N.R., Chisholm, J.D., Zhang, G., Gilbert, E.J., Wang, P.G., Van Vranken, D.L. and Thorson, J.S. RebG- and RebM-catalyzed indolocarbazole diversification. Chembiochem 7 (2006) 795–804. [PMID: 16575939]
[EC 4.3.3.5 created 2010]
 
 


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