The Enzyme Database

Your query returned 11 entries.    printer_iconPrintable version

Accepted name: progesterone monooxygenase
Reaction: progesterone + reduced acceptor + O2 = testosterone acetate + acceptor + H2O
Other name(s): progesterone hydroxylase
Systematic name: progesterone,hydrogen-donor:oxygen oxidoreductase (hydroxylating)
Comments: Has a wide specificity. A single enzyme from ascomycete the Neonectria radicicola (EC ketosteroid monooxygenase) catalyses both this reaction and that catalysed by EC androst-4-ene-3,17-dione monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-85-2
1.  Rahim, M.A. and Sih, C.J. Mechanisms of steroid oxidation by microorganisms. XI. Enzymatic cleavage of the pregnane side chain. J. Biol. Chem. 241 (1966) 3615–3623. [PMID: 5950688]
[EC created 1972, modified 1999]
Transferred entry: 5,6-dimethylbenzimidazole synthase. Now EC, 5,6-dimethylbenzimidazole synthase
[EC created 2010, deleted 2014]
Transferred entry: all-trans-8′-apo-β-carotenal 15,15′-oxygenase. Now EC, all-trans-8′-apo-β-carotenal 15,15′-oxygenase
[EC created 2010, deleted 2013]
Transferred entry: zeaxanthin 7,8-dioxygenase. Now EC, crocetin dialdehyde synthase
[EC created 2011, modified 2014, deleted 2017]
Transferred entry: β-amyrin 24-hydroxylase. Now EC, β-amyrin 24-hydroxylase
[EC created 2011, deleted 2018]
Accepted name: diapolycopene oxygenase
Reaction: 4,4′-diapolycopene + 4 reduced acceptor + 4 O2 = 4,4′-diapolycopenedial + 4 acceptor + 6 H2O
For diagram of C30 carotenoid biosynthesis, click here
Other name(s): crtP (ambiguous)
Systematic name: 4,4′-diapolycopene,AH2:oxygen oxidoreductase (4,4′-hydroxylating)
Comments: Little activity with neurosporene or lycopene. Involved in the biosynthesis of C30 carotenoids such as staphyloxanthin. The enzyme oxidizes each methyl group to the hydroxymethyl and then a dihydroxymethyl group, followed by the spontaneous loss of water to give an aldehyde group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Mijts, B.N., Lee, P.C. and Schmidt-Dannert, C. Identification of a carotenoid oxygenase synthesizing acyclic xanthophylls: combinatorial biosynthesis and directed evolution. Chem. Biol. 12 (2005) 453–460. [DOI] [PMID: 15850982]
2.  Tao, L., Schenzle, A., Odom, J.M. and Cheng, Q. Novel carotenoid oxidase involved in biosynthesis of 4,4′-diapolycopene dialdehyde. Appl. Environ. Microbiol. 71 (2005) 3294–3301. [DOI] [PMID: 15933032]
[EC created 2011]
Transferred entry: carotene ε-monooxygenase. Now EC, carotene ε-monooxygenase
[EC created 2011, deleted 2018]
Accepted name: pyrimidine oxygenase
Reaction: (1) uracil + FMNH2 + O2 = (Z)-3-ureidoacrylate peracid + FMN
(2) thymine + FMNH2 + O2 = (Z)-2-methylureidoacrylate peracid + FMN
Glossary: ureidoperacrylic acid = (Z)-3-ureidoacrylate peracid = (2Z)-3-(carbamoylamino)prop-2-eneperoxoic acid
(Z)-2-methylureidoperacrylic acid = (Z)-2-methylureidoacrylate peracid = (2Z)-3-(carbamoylamino)-2-methylprop-2-eneperoxoic acid
Other name(s): RutA
Systematic name: uracil,FMNH2:oxygen oxidoreductase (uracil hydroxylating, ring-opening)
Comments: In vitro the product (Z)-3-ureidoacrylate peracid is spontaneously reduced to ureidoacrylate [1,2]. Part of the Rut pyrimidine catabolic pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Mukherjee, T., Zhang, Y., Abdelwahed, S., Ealick, S.E. and Begley, T.P. Catalysis of a flavoenzyme-mediated amide hydrolysis. J. Am. Chem. Soc. 132 (2010) 5550–5551. [DOI] [PMID: 20369853]
2.  Kim, K.S., Pelton, J.G., Inwood, W.B., Andersen, U., Kustu, S. and Wemmer, D.E. The Rut pathway for pyrimidine degradation: novel chemistry and toxicity problems. J. Bacteriol. 192 (2010) 4089–4102. [DOI] [PMID: 20400551]
[EC created 2012]
Accepted name: (+)-larreatricin hydroxylase
Reaction: (+)-larreatricin + reduced acceptor + O2 = (+)-3′-hydroxylarreatricin + acceptor + H2O
Glossary: (+)-larreatricin = 4,4′-[(2R,3R,4S,5R)-3,4-dimethyltetrahydrofuran-2,5-diyl]bisphenol
Systematic name: (+)-larreatricin:oxygen 3′-hydroxylase
Comments: Isolated from the plant Larrea tridentata (creosote bush). The enzyme has a strong preference for the 3′ position of (+)-larreatricin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Cho, M.H., Moinuddin, S.G., Helms, G.L., Hishiyama, S., Eichinger, D., Davin, L.B. and Lewis, N.G. (+)-Larreatricin hydroxylase, an enantio-specific polyphenol oxidase from the creosote bush (Larrea tridentata). Proc. Natl. Acad. Sci. USA 100 (2003) 10641–10646. [DOI] [PMID: 12960376]
[EC created 2012]
Accepted name: heme oxygenase (staphylobilin-producing)
Reaction: (1) protoheme + 5 reduced acceptor + 4 O2 = β-staphylobilin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
(2) protoheme + 5 reduced acceptor + 4 O2 = δ-staphylobilin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
For diagram of staphylobilin biosynthesis, click here
Glossary: β-staphylobilin = 10-oxo-β-bilirubin = 3,7-bis(2-carboxyethyl)-2,8,13,18-tetramethyl-12,17-divinylbiladiene-ac-1,10,19(21H,24H)-trione
δ-staphylobilin = 10-oxo-δ-bilirubin = 3,7-bis(2-carboxyethyl)-2,8,12,17-tetramethyl-13,18-divinylbiladiene-ac-1,10,19(21H,24H)-trione
Other name(s): haem oxygenase (ambiguous); heme oxygenase (decyclizing) (ambiguous); heme oxidase (ambiguous); haem oxidase (ambiguous); heme oxygenase (ambiguous); isdG (gene name); isdI (gene name)
Systematic name: protoheme,hydrogen-donor:oxygen oxidoreductase (δ/β-methene-oxidizing, hydroxylating)
Comments: This enzyme, which is found in some pathogenic bacteria, is involved in an iron acquisition system that catabolizes the host’s hemoglobin. The two enzymes from the bacterium Staphylococcus aureus, encoded by the isdG and isdI genes, produce 67.5 % and 56.2 % δ-staphylobilin, respectively.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Reniere, M.L., Ukpabi, G.N., Harry, S.R., Stec, D.F., Krull, R., Wright, D.W., Bachmann, B.O., Murphy, M.E. and Skaar, E.P. The IsdG-family of haem oxygenases degrades haem to a novel chromophore. Mol. Microbiol. 75 (2010) 1529–1538. [DOI] [PMID: 20180905]
2.  Matsui, T., Nambu, S., Ono, Y., Goulding, C.W., Tsumoto, K. and Ikeda-Saito, M. Heme degradation by Staphylococcus aureus IsdG and IsdI liberates formaldehyde rather than carbon monoxide. Biochemistry 52 (2013) 3025–3027. [DOI] [PMID: 23600533]
3.  Streit, B.R., Kant, R., Tokmina-Lukaszewska, M., Celis, A.I., Machovina, M.M., Skaar, E.P., Bothner, B. and DuBois, J.L. Time-resolved studies of IsdG protein identify molecular signposts along the non-canonical heme oxygenase pathway. J. Biol. Chem. 291 (2016) 862–871. [DOI] [PMID: 26534961]
[EC created 2013]
Transferred entry: 2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase. Now EC, 2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase
[EC created 2014, deleted 2018]

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