The Enzyme Database

Displaying entries 1-50 of 69.

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Accepted name: prostaglandin-endoperoxide synthase
Reaction: arachidonate + reduced acceptor + 2 O2 = prostaglandin H2 + acceptor + H2O
Other name(s): prostaglandin synthase; prostaglandin G/H synthase; (PG)H synthase; PG synthetase; prostaglandin synthetase; fatty acid cyclooxygenase; prostaglandin endoperoxide synthetase
Systematic name: (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate,hydrogen-donor:oxygen oxidoreductase
Comments: This enzyme acts both as a dioxygenase and as a peroxidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39391-18-9
1.  DeWitt, D.L. and Smith, W.L. Primary structure of prostaglandin G/H synthase from sheep vesicular gland determined from the complementary DNA sequence. Proc. Natl. Acad. Sci. USA 85 (1988) 1412–1416. [DOI] [PMID: 3125548]
2.  Ohki, S., Ogino, N., Yamamoto, S. and Hayaishi, O. Prostaglandin hydroperoxidase, an integral part of prostaglandin endoperoxide synthetase from bovine vesicular gland microsomes. J. Biol. Chem. 254 (1979) 829–836. [PMID: 104998]
[EC created 1972, modified 1990]
Accepted name: kynurenine 7,8-hydroxylase
Reaction: kynurenate + reduced acceptor + O2 = 7,8-dihydro-7,8-dihydroxykynurenate + acceptor
Other name(s): kynurenic acid hydroxylase; kynurenic hydroxylase; kynurenate 7,8-hydroxylase
Systematic name: kynurenate,hydrogen-donor:oxygen oxidoreductase (hydroxylating)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9029-63-4
1.  Taniuchi, H. and Hayaishi, O. Studies on the metabolism of kynurenic acid. III. Enzymatic formation of 7,8-dihydroxykynurenic acid from kynurenic acid. J. Biol. Chem. 238 (1963) 283–293. [PMID: 13984873]
[EC created 1965 as EC, transferred 1972 to EC]
Transferred entry: heme oxygenase (biliverdin-producing). Now EC, heme oxygenase (biliverdin-producing)
[EC created 1972, modified 2006, deleted 2015]
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: stearoyl-CoA desaturase. Now EC, stearoyl-CoA 9-desaturase
[EC created 1972, modified 1986, modified 2000, deleted 2000]
Transferred entry: acyl-[acyl-carrier-protein] desaturase. Now EC, acyl-[acyl-carrier-protein] desaturase
[EC created 1972, modified 2000, deleted 2000]
Transferred entry: squalene monooxygenase. Transferred to EC, squalene monooxygenase.
[EC created 1961 as EC, transferred 1965 to EC, part transferred 1972 to EC rest to EC, deleted 2011]
Deleted entry:  arene monooxygenase (epoxidizing). Now included with EC unspecific monooxygenase
[EC created 1972, deleted 1984]
Transferred entry: steroid 17α-monooxygenase, now classified as EC, steroid 17α-monooxygenase
[EC created 1961 as EC, transferred 1965 to EC, transferred 1972 to EC, modified 2013, deleted 2015]
Transferred entry: steroid 21-monooxygenase. Now EC, steroid 21-monooxygenase
[EC created 1961 as EC, transferred 1965 to EC, transferred 1972 to EC, modified 2013, deleted 2015]
Accepted name: estradiol 6β-monooxygenase
Reaction: estradiol-17β + reduced acceptor + O2 = 6β-hydroxyestradiol-17β + acceptor + H2O
Other name(s): estradiol 6β-hydroxylase
Systematic name: estradiol-17β,hydrogen-donor:oxygen oxidoreductase (6β-hydroxylating)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9029-70-3
1.  Haines, W.J. The biosynthesis of adrenal cortex hormones. Recent Progr. Hormone Res. 7 (1952) 255–305.
2.  Mueller, G.C. and Rumney, G. Formation of 6β-hydroxy and 6-keto derivatives of estradiol-16-C14 by mouse liver microsomes. J. Am. Chem. Soc. 79 (1957) 1004–1005.
[EC created 1965 as EC, transferred 1972 to EC]
Accepted name: androst-4-ene-3,17-dione monooxygenase
Reaction: androstenedione + reduced acceptor + O2 = testololactone + acceptor + H2O
Glossary: androstenedione = androst-4-ene-3,17-dione
testololactone = 3-oxo-13,17-secoandrost-4-eno-17,13-lactone
Other name(s): androstene-3,17-dione hydroxylase; androst-4-ene-3,17-dione 17-oxidoreductase; androst-4-ene-3,17-dione hydroxylase; androstenedione monooxygenase; 4-androstene-3,17-dione monooxygenase
Systematic name: androst-4-ene-3,17-dione-hydrogen-donor:oxygen oxidoreductase (13-hydroxylating, lactonizing)
Comments: Has a wide specificity. A single enzyme from the ascomycete Neonectria radicicola (EC, ketosteroid monooxygenase) catalyses both this reaction and that catalysed by EC, progesterone monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-74-9
1.  Prairie, R.L. and Talalay, P. Enzymatic formation of testololactone. Biochemistry 2 (1963) 203–208. [PMID: 13985909]
[EC created 1972, modified 1999]
Transferred entry: 3-hydroxybenzoate 4-monooxygenase. Now EC, 3-hydroxybenzoate 4-monooxygenase
[EC created 1972, deleted 1984]
Accepted name: progesterone 11α-monooxygenase
Reaction: progesterone + reduced acceptor + O2 = 11α-hydroxyprogesterone + acceptor + H2O
Other name(s): progesterone 11α-hydroxylase
Systematic name: progesterone,hydrogen-donor:oxygen oxidoreductase (11α-hydroxylating)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-77-2
1.  Shibahara, M., Moody, J.A. and Smith, L.L. Microbial hydroxylations. V. 11α-Hydroxylation of progesterone by cell-free preparations of Aspergillus ochraceus. Biochim. Biophys. Acta 202 (1970) 172–179. [DOI] [PMID: 5417182]
[EC created 1972]
Accepted name: 4-methoxybenzoate monooxygenase (O-demethylating)
Reaction: 4-methoxybenzoate + reduced acceptor + O2 = 4-hydroxybenzoate + formaldehyde + acceptor + H2O
Other name(s): 4-methoxybenzoate 4-monooxygenase (O-demethylating); 4-methoxybenzoate O-demethylase; p-anisic O-demethylase; piperonylate-4-O-demethylase
Systematic name: 4-methoxybenzoate,hydrogen-donor:oxygen oxidoreductase (O-demethylating)
Comments: The bacterial enzyme consists of a ferredoxin-type protein and an iron-sulfur flavoprotein (FMN). Also acts on 4-ethoxybenzoate, N-methyl-4-aminobenzoate and toluate. The fungal enzyme acts best on veratrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 37256-78-3
1.  Bernhardt, F.-H., Nastainczyk, W. and Seydewitz, V. Kinetic studies on a 4-methoxybenzoate O-demethylase from Pseudomonas putida. Eur. J. Biochem. 72 (1977) 107–115. [DOI] [PMID: 188654]
2.  Paszcynski, A. and Trojanowski, J. An affinity-column procedure for the purification of veratrate O-demethylase from fungi. Microbios 18 (1977) 111–121. [PMID: 25369]
3.  Twilfer, H., Bernhardt, F.-H. and Gersonde, K. An electron-spin-resonance study on the redox-active centers of the 4-methoxybenzoate monooxygenase from Pseudomonas putida. Eur. J. Biochem. 119 (1981) 595–602. [DOI] [PMID: 6273164]
[EC created 1972]
Transferred entry: methylsterol monooxygenase. Now EC, methylsterol monooxygenase
[EC created 1972, deleted 2002]
Transferred entry: glyceryl-ether monooxygenase. Now EC, glyceryl-ether monooxygenase
[EC created 1972, deleted 1976]
Deleted entry:  CMP-N-acetylneuraminate monooxygenase
[EC created 1976, modified 1999, deleted 2003]
Transferred entry: plasmanylethanolamine desaturase. Now classified as EC, plasmanylethanolamine desaturase
[EC created 1976, deleted 2020]
Accepted name: phylloquinone monooxygenase (2,3-epoxidizing)
Reaction: phylloquinone + reduced acceptor + O2 = 2,3-epoxyphylloquinone + acceptor + H2O
Other name(s): phylloquinone epoxidase; vitamin K 2,3-epoxidase; vitamin K epoxidase; vitamin K1 epoxidase
Systematic name: phylloquinone,hydrogen-donor:oxygen oxidoreductase (2,3-epoxidizing)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 54596-37-1
1.  Willingham, A.K. and Matschiner, J.T. Changes in phylloquinone epoxidase activity related to prothrombin synthesis and microsomal clotting activity in the rat. Biochem. J. 140 (1974) 435–441. [PMID: 4155625]
[EC created 1976]
Accepted name: Latia-luciferin monooxygenase (demethylating)
Reaction: Latia luciferin + reduced acceptor + 2 O2 = oxidized Latia luciferin + CO2 + formate + acceptor + H2O +
Glossary: Latia-luciferin = (E)-2-methyl-4-(2,6,6-trimethylcyclohex-1-en-1-yl)but-1-en-1-yl formate
Other name(s): luciferase (Latia luciferin); Latia luciferin monooxygenase (demethylating)
Systematic name: Latia-luciferin,hydrogen-donor:oxygen oxidoreductase (demethylating)
Comments: A flavoprotein. Latia is a bioluminescent mollusc. The reaction possibly involves two enzymes, an oxygenase followed by a monooxygenase for the actual light-emitting step.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-54-1
1.  Shimomura, O. and Johnson, F.H. The structure of Latia luciferin. Biochemistry 7 (1968) 1734–1738. [PMID: 5650377]
2.  Shimomura, O., Johnson, F.H. and Kohama, Y. Reactions involved in bioluminescence systems of limpet (Latia neritoides) and luminous bacteria. Proc. Natl. Acad. Sci. USA 69 (1972) 2086–2089. [DOI] [PMID: 4506078]
[EC created 1976, modified 1982]
Accepted name: ecdysone 20-monooxygenase
Reaction: ecdysone + reduced acceptor + O2 = 20-hydroxyecdysone + acceptor + H2O
Other name(s): α-ecdysone C-20 hydroxylase; ecdysone 20-hydroxylase
Systematic name: Ecdysone,hydrogen-donor:oxygen oxidoreductase (20-hydroxylating)
Comments: An enzyme from insect fat body or malpighian tubules involving a heme-thiolate protein (P-450). NADPH can act as ultimate hydrogen donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 55071-97-1
1.  Johnson, P. and Rees, H.H. The mechanism of C-20 hydroxylation of α-ecdysone in the desert locust, Schistocerca gregaria. Biochem. J. 168 (1977) 513–520. [PMID: 606249]
2.  Nigg, H.N., Svoboda, J.A., Thompson, M.J., Dutky, S.R., Kaplanis, J.N. and Robbins, W.E. Ecdysome 20-hydroxylase from the midgut of the tobacco hornworm (Manduca sexta L.). Experientia 32 (1976) 438–439. [PMID: 5286]
3.  Smith, S.L., Bollenbacher, W.E., Cooper, D.Y., Schleyer, H., Wielgus, J.J. and Gilbert, L.I. Ecdysone 20-monooxygenase: characterization of an insect cytochrome p-450 dependent steroid hydroxylase. Mol. Cell. Endocrinol. 15 (1979) 111–133. [PMID: 488526]
[EC created 1978]
Accepted name: 3-hydroxybenzoate 2-monooxygenase
Reaction: 3-hydroxybenzoate + reduced acceptor + O2 = 2,3-dihydroxybenzoate + acceptor + H2O
Other name(s): 3-hydroxybenzoate 2-hydroxylase; 3-HBA-2-hydroxylase
Systematic name: 3-hydroxybenzoate,hydrogen-donor:oxygen oxidoreductase (2-hydroxylating)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 73507-96-7
1.  Daumy, G.O. and McColl, A.S. Induction of 3-hydroxybenzoate 2-hydroxylase in a Pseudomonas testosteroni mutant. J. Bacteriol. 149 (1982) 384–385. [PMID: 7054148]
[EC created 1984]
Accepted name: steroid 9α-monooxygenase
Reaction: pregna-4,9(11)-diene-3,20-dione + reduced acceptor + O2 = 9,11α-epoxypregn-4-ene-3,20-dione + acceptor + H2O
Other name(s): steroid 9α-hydroxylase
Systematic name: steroid,hydrogen-donor:oxygen oxidoreductase (9-epoxidizing)
Comments: An enzyme system involving a flavoprotein (FMN) and two iron-sulfur proteins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 82869-33-8
1.  Strijewski, A. The steroid-9α-hydroxylation system from Nocardia species. Eur. J. Biochem. 128 (1982) 125–135. [DOI] [PMID: 7173200]
[EC created 1986]
Transferred entry: linoleoyl-CoA desaturase. Now EC, linoleoyl-CoA desaturase
[EC created 1986, deleted 2000]
Accepted name: 2-hydroxypyridine 5-monooxygenase
Reaction: 2-hydroxypyridine + reduced acceptor + O2 = 2,5-dihydroxypyridine + acceptor + H2O
Other name(s): 2-hydroxypyridine oxygenase
Systematic name: 2-hydroxypyridine,hydrogen-donor:oxygen oxidoreductase (5-hydroxylating)
Comments: Also oxidizes 2,5-dihydroxypyridine, but does not act on 3-hydroxypyridine, 4-hydroxypyridine or 2,6-dihydroxypyridine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 96779-45-2
1.  Sharma, M.L., Kaul, S.M. and Shukla, O.P. Metabolism of 2-hydroxypyridine by Bacillus brevis (INA). Biol. Membr. 9 (1984) 43–52.
[EC created 1989]
Transferred entry: juglone 3-monooxygenase, now classified as EC, juglone 3-monooxygenase
[EC created 1989, deleted 2016]
Transferred entry: linalool 8-monooxygenase. Now EC, linalool 8-monooxygenase
[EC created 1989, deleted 2012]
Accepted name: deoxyhypusine monooxygenase
Reaction: [eIF5A]-deoxyhypusine + reduced acceptor + O2 = [eIF5A]-hypusine + acceptor + H2O
For diagram of reaction, click here
Glossary: deoxyhypusine = N6-(4-aminobutyl)-L-lysine
hypusine = N6-[(R)-4-amino-2-hydroxybutyl]-L-lysine
Other name(s): deoxyhypusine hydroxylase; deoxyhypusine dioxygenase
Systematic name: deoxyhypusine,hydrogen-donor:oxygen oxidoreductase (2-hydroxylating)
Comments: The enzyme catalyses the final step in the formation of the amino acid hypusine in the eukaryotic initiation factor 5A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 101920-83-6
1.  Abbruzzese, A., Park, M.H. and Folk, J.E. Deoxyhypusine hydroxylase from rat testis. Partial purification and characterization. J. Biol. Chem. 261 (1986) 3085–3089. [PMID: 3949761]
[EC created 1989]
Transferred entry: carotene 7,8-desaturase. Now EC, 9,9′-dicis-ζ-carotene desaturase.
[EC created 1999, deleted 2011]
Transferred entry: myristoyl-CoA 11-(E) desaturase. Now classified as EC, myristoyl-CoA 11-(E) desaturase
[EC created 2000, deleted 2015]
Transferred entry: myristoyl-CoA 11-(Z) desaturase. Now classified as EC, acyl-CoA 11-(Z)-desaturase.
[EC created 2000, deleted 2015]
Transferred entry: Δ12-fatty acid dehydrogenase. Now EC, acyl-lipid Δ12-acetylenase
[EC created 2000, deleted 2015]
Accepted name: monoprenyl isoflavone epoxidase
Reaction: 7-O-methylluteone + NADPH + H+ + O2 = dihydrofurano derivatives + NADP+ + H2O
Glossary: luteone = 3-(2,4-dihydroxyphenyl)-5,7-dihydroxy-6-(3-methyl-2-butenyl)-4H-1-benzopyran-4-one
naringenin = 4′,5,7-trihydroxyflavan-4-one
Other name(s): monoprenyl isoflavone monooxygenase; 7-O-methylluteone:O2 oxidoreductase; 7-O-methylluteone,NADPH:O2 oxidoreductase
Systematic name: 7-O-methylluteone,NADPH:oxygen oxidoreductase
Comments: A flavoprotein (FAD) with high specificity for monoprenyl isoflavone. The product of the prenyl epoxidation reaction contains an oxygen atom derived from O2, but not from H2O. It is slowly and non-enzymically converted into the corresponding dihydrofurano derivative. The enzyme in the fungus Botrytis cinerea is induced by the substrate analogue, 6-prenylnaringenin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 198496-86-5
1.  Tanaka, M. and Tahara, S. FAD-dependent epoxidase as a key enzyme in fungal metabolism of prenylated flavonoids. Phytochemistry 46 (1997) 433–439.
[EC created 2000]
Accepted name: thiophene-2-carbonyl-CoA monooxygenase
Reaction: thiophene-2-carbonyl-CoA + reduced acceptor + O2 = 5-hydroxythiophene-2-carbonyl-CoA + acceptor + H2O
Other name(s): thiophene-2-carboxyl-CoA dehydrogenase; thiophene-2-carboxyl-CoA hydroxylase; thiophene-2-carboxyl-CoA monooxygenase
Systematic name: thiophene-2-carbonyl-CoA, hydrogen-donor:oxygen oxidoreductase
Comments: A molybdenum enzyme. Highly specific for thiophene-2-carbonyl-CoA. Tetrazolium salts can act as electron acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 208540-44-7
1.  Bambauer, A., Rainey, F.A., Stackebrandt, E. and Winter, J. Characterization of Aquamicrobium defluvii gen. nov. sp. nov., a thiophene-2-carboxylate-metabolizing bacterium from activated sludge. Arch. Microbiol. 169 (1998) 293–302. [PMID: 9531630]
[EC created 2000]
Transferred entry: β-carotene 15,15-monooxygenase. Now classified as EC, β-carotene 15,15′-dioxygenase.
[EC created 1972 as EC, transferred 2001 to EC, deleted 2015]
Transferred entry: taxadiene 5α-hydroxylase. Now, taxadiene 5α-hydroxylase
[EC created 2002, deleted 2020]
Accepted name: cholesterol 25-monooxygenase
Reaction: cholesterol + reduced acceptor + O2 = 25-hydroxycholesterol + acceptor + H2O
For diagram of cholic acid biosynthesis (sidechain), click here
Glossary: cholesterol = cholest-5-en-3β-ol
Other name(s): cholesterol 25-hydroxylase (ambiguous)
Systematic name: cholesterol,hydrogen-donor:oxygen oxidoreductase (25-hydroxylating)
Comments: Unlike most other sterol hydroxylases, this enzyme is not a cytochrome P-450. Instead, it uses diiron cofactors to catalyse the hydroxylation of hydrophobic substrates [1]. The diiron cofactor can be either Fe-O-Fe or Fe-OH-Fe and is bound to the enzyme through interactions with clustered histidine or glutamate residues [4,5]. In cell cultures, this enzyme down-regulates cholesterol synthesis and the processing of sterol regulatory element binding proteins (SREBPs). cf. EC, cholesterol C-25 hydroxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 60202-07-5
1.  Lund, E.G., Kerr, T.A., Sakai, J., Li, W.P. and Russell, D.W. cDNA cloning of mouse and human cholesterol 25-hydroxylases, polytopic membrane proteins that synthesize a potent oxysterol regulator of lipid metabolism. J. Biol. Chem. 273 (1998) 34316–34327. [DOI] [PMID: 9852097]
2.  Chen, J.J., Lukyanenko, Y. and Hutson, J.C. 25-Hydroxycholesterol is produced by testicular macrophages during the early postnatal period and influences differentiation of Leydig cells in vitro. Biol. Reprod. 66 (2002) 1336–1341. [PMID: 11967195]
3.  Lukyanenko, Y., Chen, J.J. and Hutson, J.C. Testosterone regulates 25-hydroxycholesterol production in testicular macrophages. Biol. Reprod. 67 (2002) 1435–1438. [PMID: 12390873]
4.  Fox, B.G., Shanklin, J., Ai, J., Loehr, T.M. and Sanders-Loehr, J. Resonance Raman evidence for an Fe-O-Fe center in stearoyl-ACP desaturase. Primary sequence identity with other diiron-oxo proteins. Biochemistry 33 (1994) 12776–12786. [PMID: 7947683]
5.  Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137–174. [DOI] [PMID: 12543708]
[EC created 2005, modified 2020]
Accepted name: ammonia monooxygenase
Reaction: NH3 + a reduced acceptor + O2 = NH2OH + an acceptor + H2O
Other name(s): AMO
Systematic name: ammonia,donor:oxygen oxidoreductase (hydroxylamine-producing)
Comments: The enzyme catalyses the first reaction in the pathway of ammonia oxidation to nitrite. It contains copper [1], iron [5] and possibly zinc [9]. The enzyme requires two electrons, which are derived indirectly from the quinone pool via a membrane-bound donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD
1.  Ensign, S.A., Hyman, M.R. and Arp, D.J. In vitro activation of ammonia monooxygenase from Nitrosomonas europaea by copper. J. Bacteriol. 175 (1993) 1971–1980. [DOI] [PMID: 8458839]
2.  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]
3.  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. [DOI] [PMID: 7980540]
4.  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. [DOI] [PMID: 7590173]
5.  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. [DOI] [PMID: 8941709]
6.  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. [DOI] [PMID: 8654570]
7.  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. [DOI] [PMID: 11004450]
8.  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. [DOI] [PMID: 12209257]
9.  Gilch, S., Meyer, O. and Schmidt, I. A soluble form of ammonia monooxygenase in Nitrosomonas europaea. Biol. Chem. 390 (2009) 863–873. [DOI] [PMID: 19453274]
[EC created 2010]
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 + NADH = (Z)-3-ureidoacrylate + H2O + FMN + NAD+ + H+ (overall reaction)
(1a) FMNH2 + O2 = FMN-N5-peroxide
(1b) uracil + FMN-N5-peroxide = (Z)-3-ureidoacrylate + FMN-N5-oxide
(1c) FMN-N5-oxide + NADH = FMN + H2O + NAD+ + H+ (spontaneous)
(2) thymine + FMNH2 + O2 + NADH = (Z)-2-methylureidoacrylate + H2O + FMN + NAD+ + H+ (overall reaction)
(2a) FMNH2 + O2 = FMN-N5-peroxide
(2b) thymine + FMN-N5-peroxide = (Z)-2-methylureidoacrylate + FMN-N5-oxide
(2c) FMN-N5-oxide + NADH = FMN + H2O + NAD+ + H+ (spontaneous)
Glossary: (Z)-3-ureidoacrylate = (2Z)-3-(carbamoylamino)prop-2-enoate
(Z)-2-methylureidoacrylate = (2Z)-3-(carbamoylamino)-2-methylprop-2-enoate
Other name(s): rutA (gene name)
Systematic name: uracil,FMNH2:oxygen oxidoreductase (uracil hydroxylating, ring-opening)
Comments: The enzyme participates in the Rut pyrimidine catabolic pathway. The flavin-N5-oxide that is formed by the enzyme reacts spontaneously with NADH to give oxidized flavin, releasing a water molecule.
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]
3.  Adak, S. and Begley, T.P. RutA-catalyzed oxidative cleavage of the uracil amide involves formation of a flavin-N5-oxide. Biochemistry 56 (2017) 3708–3709. [PMID: 28661684]
4.  Adak, S. and Begley, T.P. Flavin-N5-oxide: A new, catalytic motif in flavoenzymology. Arch. Biochem. Biophys. 632 (2017) 4–10. [PMID: 28784589]
5.  Matthews, A., Saleem-Batcha, R., Sanders, J.N., Stull, F., Houk, K.N. and Teufel, R. Aminoperoxide adducts expand the catalytic repertoire of flavin monooxygenases. Nat. Chem. Biol. 16 (2020) 556–563. [DOI] [PMID: 32066967]
[EC created 2012, modified 2019]
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]
Accepted name: γ-glutamyl hercynylcysteine S-oxide synthase
Reaction: hercynine + γ-L-glutamyl-L-cysteine + O2 = γ-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
For diagram of ergothioneine and ovothiol biosynthesis, click here
Glossary: hercynine = Nα,Nα,Nα-trimethyl-L-histidine
Other name(s): EgtB
Systematic name: hercynine,γ-L-glutamyl-L-cysteine:oxygen oxidoreductase [γ-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide-forming]
Comments: Requires Fe2+ for activity. The enzyme, found in bacteria, is specific for both hercynine and γ-L-glutamyl-L-cysteine. It is part of the biosynthesis pathway of ergothioneine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Seebeck, F.P. In vitro reconstitution of mycobacterial ergothioneine biosynthesis. J. Am. Chem. Soc. 132 (2010) 6632–6633. [DOI] [PMID: 20420449]
2.  Pluskal, T., Ueno, M. and Yanagida, M. Genetic and metabolomic dissection of the ergothioneine and selenoneine biosynthetic pathway in the fission yeast, S. pombe, and construction of an overproduction system. PLoS One 9:e97774 (2014). [DOI] [PMID: 24828577]
[EC created 2015]

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