Continued from EC 1.14.14 to EC 1.14.19
Accepted name: prostaglandin-endoperoxide synthase
Reaction: arachidonate + AH2 + 2 O2 = prostaglandin H2 + A + 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, PDB, CAS registry number: 39391-18-9
References:
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. [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]
Accepted name: kynurenine 7,8-hydroxylase
Reaction: kynurenate + AH2 + O2 = 7,8-dihydro-7,8-dihydroxykynurenate + A
Other name(s): kynurenic acid hydroxylase; kynurenic hydroxylase; kynurenate 7,8-hydroxylase
Systematic name: kynurenate,hydrogen-donor:oxygen oxidoreductase (hydroxylating)
Comments: Formerly EC 1.14.1.4.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9029-63-4
References:
1. Taniuchi, H. and Hayaishi, O. Studies on the metabolism of kynurenic acid. III. Enzymatic formation of 7,8-dihydroxykynurenic acid. J. Biol. Chem. 238 (1963) 283-293.
Accepted name: heme oxygenase
Reaction: heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
For diagram, click here
Other name(s): ORP33 proteins; haem oxygenase; heme oxygenase (decyclizing); heme oxidase; haem oxidase
Systematic name: heme,hydrogen-donor:oxygen oxidoreductase (α-methene-oxidizing, hydroxylating)
Comments: Requires NAD(P)H and EC 1.6.2.4, NADPH—hemoprotein reductase. The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules [4]. The third oxygen molecule provides the oxygen atom that converts the α-carbon to CO. The central iron is kept in the reduced state by NAD(P)H.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9059-22-7
References:
1. Maines, M.D., Ibrahim, N.G. and Kappas, K. Solubilization and partial purification of heme oxygenase from rat liver. J. Biol. Chem. 252 (1977) 5900-5903. [PMID: 18477]
2. Sunderman, F.W., Jr., Downs, J.R., Reid, M.C. and Bibeau, L.M. Gas-chromatographic assay for heme oxygenase activity. Clin. Chem. 28 (1982) 2026-2032. [PMID: 6897023]
3. Yoshida, T., Takahashi, S. and Kikuchi, J. Partial purification and reconstitution of the heme oxygenase system from pig spleen microsomes. J. Biochem. (Tokyo) 75 (1974) 1187-1191. [PMID: 4370250]
4. Noguchi, M., Yoshida, T. and Kikuchi, G. Specific requirement of NADPH-cytochrome c reductase for the microsomal heme oxygenase reaction yielding biliverdin IX α. FEBS Lett. 98 (1979) 281-284. [PMID: 105935]
5. Lad, L., Schuller, D.J., Shimizu, H., Friedman, J., Li, H., Ortiz de Montellano, P.R. and Poulos, T.L. Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1. J. Biol. Chem. 278 (2003) 7834-7843. [PMID: 12500973]
Accepted name: progesterone monooxygenase
Reaction: progesterone + AH2 + O2 = testosterone acetate + A + 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 1.14.13.54 ketosteroid monooxygenase) catalyses both this reaction and that catalysed by EC 1.14.99.12 androst-4-ene-3,17-dione monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37256-85-2
References:
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.
[EC 1.14.99.5 Transferred entry: now EC 1.14.19.1, stearoyl-CoA 9-desaturase (EC 1.14.99.5 created 1972, modified 1986, modified 2000, deleted 2000)]
[EC 1.14.99.6 Transferred entry: now EC 1.14.19.2, acyl-[acyl-carrier-protein] desaturase (EC 1.14.99.6 created 1972, modified 2000, deleted 2000)]
[EC 1.14.99.7 Transferred entry: squalene monooxygenase. Transferred to EC 1.14.13.132, squalene monooxygenase. (EC 1.14.99.7 created 1961 as EC 1.99.1.13, transferred 1965 to EC 1.14.1.3, part transferred 1972 to EC 1.14.99.7 rest to EC 5.4.99.7, deleted 2011)]
[EC 1.14.99.8 Deleted entry: arene monooxygenase (epoxidizing). Now included with EC 1.14.14.1 unspecific monooxygenase (EC 1.14.99.8 created 1972, deleted 1984)]
Accepted name: steroid 17α-monooxygenase
Reaction: a steroid + AH2 + O2 = a 17α-hydroxysteroid + A + H2O
Other name(s): steroid 17α-hydroxylase; cytochrome P-45017α; cytochrome P-450 (P-45017α,lyase); 17α-hydroxylase-C17,20 lyase
Systematic name: steroid,hydrogen-donor:oxygen oxidoreductase (17α-hydroxylating)
Comments: Requires NAD(P)H and P-450. Formerly EC 1.14.1.7 and EC 1.99.1.9.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9029-67-8
References:
1. Lynn, W.S. and Brown, R.H. The conversion of progesterone to androgens by testes. J. Biol. Chem. 232 (1958) 1015-1030.
2. Yoshida, K.-I., Oshima, H. and Troen, P. Studies of the human testis. XIII. Properties of nicotinamide adenine dinucleotide (reduced form)-linked 17α-hydroxylation. J. Clin. Endocrinol. Metab. 50 (1980) 895-899. [PMID: 6966286]
Accepted name: steroid 21-monooxygenase
Reaction: a steroid + AH2 + O2 = a 21-hydroxysteroid + A + H2O
Other name(s): steroid 21-hydroxylase; 21-hydroxylase
Systematic name: steroid,hydrogen-donor:oxygen oxidoreductase (21-hydroxylating)
Comments: An enzyme system involving a heme-thiolate protein (P-450) and flavoprotein. Formerly EC 1.14.1.8 and EC 1.99.1.11.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9029-68-9
References:
1. Hayano, M. and Dorfman, R.I. The action of adrenal homogenates on progesterone, 17-hydroxyprogesterone and 21-desoxycortisone. Arch. Biochem. Biophys. 36 (1952) 237-239.
2. Plager, J.E. and Samuels, L.T. Synthesis of C14-17-hydroxy-11-desoxycorticosterone and 17-hydroxycorticosterone by fractionated extracts of adrenal homogenates. Arch. Biochem. Biophys. 42 (1953) 477-478.
3. Ryan, K.J. and Engel, L.L. Hydroxylation of steroids at carbon 21. J. Biol. Chem. 225 (1957) 103-114.
Accepted name: estradiol 6β-monooxygenase
Reaction: estradiol-17β + AH2 + O2 = 6β-hydroxyestradiol-17β + A + H2O
Other name(s): estradiol 6β-hydroxylase
Systematic name: estradiol-17β,hydrogen-donor:oxygen oxidoreductase (6β-hydroxylating)
Comments: Formerly EC 1.14.1.10 and EC 1.99.1.8.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9029-70-3
References:
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.
Accepted name: androst-4-ene-3,17-dione monooxygenase
Reaction: androstenedione + AH2 + O2 = testololactone + A + H2O
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 1.14.13.54 ketosteroid monooxygenase) catalyses both this reaction and that catalysed by EC 1.4.99.4 aralkylamine dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37256-74-9
References:
1. Prairie, R.L. and Talalay, P. Enzymatic formation of testololactone. Biochemistry 2 (1963) 203-208.
[EC 1.14.99.13 Transferred entry: now EC 1.14.13.23 3-hydroxybenzoate 4-monooxygenase (EC 1.14.99.13 created 1972, deleted 1984)]
Accepted name: progesterone 11α-monooxygenase
Reaction: progesterone + AH2 + O2 = 11α-hydroxyprogesterone + A + H2O
Other name(s): progesterone 11α-hydroxylase
Systematic name: progesterone,hydrogen-donor:oxygen oxidoreductase (11α-hydroxylating)
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37256-77-2
References:
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. [PMID: 5417182]
Accepted name: 4-methoxybenzoate monooxygenase (O-demethylating)
Reaction: 4-methoxybenzoate + AH2 + O2 = 4-hydroxybenzoate + formaldehyde + A + 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, UM-BBD, CAS registry number: 37256-78-3
References:
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. [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. [PMID: 6273164]
[EC 1.14.99.16 Deleted entry: methylsterol monooxygenase, transferred to EC 1.14.13.72 (EC 1.14.99.16 created 1972, deleted 2002)]
[EC 1.14.99.17 Transferred entry: now EC 1.14.16.5 glyceryl-ether monooxygenase (EC 1.14.99.17 created 1972, deleted 1976)]
[EC 1.14.99.18 Deleted entry: CMP-N-acetylneuraminate monooxygenase. (EC 1.14.99.18 created 1976, modified 1999, deleted 2003)]
Accepted name: plasmanylethanolamine desaturase
Reaction: O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine + AH2 + O2 = O-1-alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine + A + 2 H2O
Other name(s): alkylacylglycerophosphoethanolamine desaturase; alkylacylglycero-phosphorylethanolamine dehydrogenase; dehydrogenase, alkyl-acylglycerophosphorylethanolamine; 1-O-alkyl-2-acyl-sn-glycero-3-phosphorylethanolamine desaturase; 1-O-alkyl 2-acyl-sn-glycero-3-phosphorylethanolamine desaturase
Systematic name: O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine,hydrogen-donor:oxygen oxidoreductase
Comments: Requires NADPH or NADH. May involve cytochrome b5. Requires Mg2+ and ATP.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 39391-13-4
References:
1. Paltauf, F. and Holasek, A. Enzymatic synthesis of plasmalogens. Characterization of the 1-O-alkyl-2-acyl-sn-glycero-3-phosphorylethanolamine desaturase from mucosa of hamster small intestine. J. Biol. Chem. 248 (1973) 1609-1615. [PMID: 4144394]
2. Wykle, R.L., Blank, M.L., Malone, B. and Snyder, F. Evidence for a mixed function oxidase in the biosynthesis of ethanolamine plasmalogens from 1-alkyl-2-acyl-sn-glycero-3-phosphorylethanolamine. J. Biol. Chem. 247 (1972) 5442-5447. [PMID: 4403444]
Accepted name: phylloquinone monooxygenase (2,3-epoxidizing)
Reaction: phylloquinone + AH2 + O2 = 2,3-epoxyphylloquinone + A + 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, CAS registry number: 54596-37-1
References:
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]
Accepted name: Latia-luciferin monooxygenase (demethylating)
Reaction: Latia luciferin + AH2 + 2 O2 = oxidized Latia luciferin + CO2 + formate + A + H2O + hν
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, CAS registry number: 62213-54-1
References:
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. [PMID: 4506078]
Accepted name: ecdysone 20-monooxygenase
Reaction: ecdysone + AH2 + O2 = 20-hydroxyecdysone + A + 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, CAS registry number: 55071-97-1
References:
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]
Accepted name: 3-hydroxybenzoate 2-monooxygenase
Reaction: 3-hydroxybenzoate + AH2 + O2 = 2,3-dihydroxybenzoate + A + 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, CAS registry number: 73507-96-7
References:
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]
Accepted name: steroid 9α-monooxygenase
Reaction: pregna-4,9(11)-diene-3,20-dione + AH2 + O2 = 9,11α-epoxypregn-4-ene-3,20-dione + A + 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, CAS registry number: 82869-33-8
References:
1. Strijewski, A. The steroid-9α-hydroxylation system from Nocardia species. Eur. J. Biochem. 128 (1982) 125-135. [PMID: 7173200]
[EC 1.14.99.25 Transferred entry: now EC 1.14.19.3, linoleoyl-CoA desaturase (EC 1.14.99.25 created 1986, deleted 2000)]
Accepted name: 2-hydroxypyridine 5-monooxygenase
Reaction: 2-hydroxypyridine + AH2 + O2 = 2,5-dihydroxypyridine + A + 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, CAS registry number: 96779-45-2
References:
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.
Accepted name: juglone 3-monooxygenase
Reaction: 5-hydroxy-1,4-naphthoquinone + AH2 + O2 = 3,5-dihydroxy-1,4-naphthoquinone + A + H2O
Other name(s): juglone hydroxylase; naphthoquinone hydroxylase; naphthoquinone-hydroxylase
Systematic name: 5-hydroxy-1,4-naphthoquinone,hydrogen-donor:oxygen oxidoreductase (3-hydroxylating)
Comments: Also acts on 1,4-naphthoquinone, naphthazarin and 2-chloro-1,4-naphthoquinone, but not on other related compounds.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 98865-54-4
References:
1. Rettenmaier, H. and Lingens, F. Purification and some properties of two isofunctional juglone hydroxylases from Pseudomonas putida J1. Biol. Chem. Hoppe-Seyler 366 (1985) 637-646. [PMID: 4041238]
Accepted name: linalool 8-monooxygenase
Reaction: 3,7-dimethylocta-1,6-dien-3-ol + AH2 + O2 = (E)-3,7-dimethylocta-1,6-dien-3,8-diol + A + H2O
Systematic name: 3,7-dimethylocta-1,6-dien-3-ol,hydrogen-donor:oxygen oxidoreductase (8-hydroxylating)
Comments: A heme-thiolate protein (P-450).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 95329-13-8
References:
1. Bhattacharyya, P.K., Samanta, T.B., Ullah, A.H.J. and Gunsalus, I.C. Chemical probes into the active centre of a heme thiolate monoxygenase. Proc. Indian Acad. Sci., Chem. Sci. 93 (1984) 1289-1304.
Accepted name: deoxyhypusine monooxygenase
Reaction: protein N6-(4-aminobutyl)-L-lysine + AH2 + O2 = protein N6-[(R)-4-amino-2-hydroxybutyl]-L-lysine + A + H2O
For diagram click here.
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, CAS registry number: 101920-83-6
References:
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 1.14.99.30 Transferred entry: carotene 7,8-desaturase. Now EC 1.3.5.6, 9,9'-dicis-ζ-carotene desaturase. (EC 1.14.99.30 created 1999, deleted 2011)]
Accepted name: myristoyl-CoA 11-(E) desaturase
Reaction: myristoyl-CoA + NAD(P)H + H+ + O2 = (E)-11-tetradecenoyl-CoA + NAD(P)+ + 2 H2O
Other name(s): n-tetradecanoyl-CoA,NADPH:O2 oxidoreductase [11-(E) desaturating]
Systematic name: n-tetradecanoyl-CoA,NAD(P)H:O2 oxidoreductase [11-(E) desaturating]
Comments: Involved in sex pheromone synthesis in the moth Spodoptera littoralis. (E)-11-Tetradecenoyl-CoA is formed by stereospecific removal of the pro-R H at C-11 and the pro-S H at C-12. EC 1.14.99.32, myristoyl-CoA 11-(Z) desaturase, forms the Z isomer by stereospecific cleavage of pro-R H at C-11 and C-12.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 199543-17-4
References:
1. Navaro, I., Font, I., Fabrias, G. and Camps, F. Stereospecificity of the (E)- and (Z)-11 myristoyl desaturases in the biosynthesis of Spodoptera littoralis sex pheromone. J. Am. Chem. Soc. 119 (1997) 11335-11336.
Accepted name: myristoyl-CoA 11-(Z) desaturase
Reaction: myristoyl-CoA + NAD(P)H + H+ + O2 = (Z)-11-tetradecenoyl-CoA + NAD(P)+ + 2 H2O
Other name(s): n-tetradecanoyl-CoA,NADPH:O2 oxidoreductase [11-(Z) desaturating]
Systematic name: n-tetradecanoyl-CoA,NAD(P)H:O2 oxidoreductase [11-(Z) desaturating]
Comments: Involved in sex pheromone synthesis in the moth Spodoptera littoralis. (Z)-11-Tetradecenoyl-CoA is formed by stereospecific removal of H from the pro-R positions at C-11 and C-12. EC 1.14.99.31, myristoyl-CoA 11-(E) desaturase, forms the (E)-isomer by removing the pro-R H group at C-11 and the pro-S H group at C-12.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 199543-16-3
References:
1. Navaro, I., Font, I., Fabrias, G. and Camps, F. Stereospecificity of the (E)- and (Z)-11 myristoyl desaturases in the biosynthesis of Spodoptera littoralis sex pheromone. J. Am. Chem. Soc. 119 (1997) 11335-11336.
Accepted name: δ12-fatty acid dehydrogenase
Reaction: linoleate + AH2 + O2 = crepenynate + A + 2 H2O
Glossary entries:
crepenynate: (9Z)-octadec-9-en-12-ynoate
linoleate: (9Z,12Z)-octadeca-9,12-dienoate
Other name(s): crepenynate synthase; linoleate δ12-fatty acid acetylenase (desaturase)
Systematic name: linoleate, hydrogen-donor:oxygen oxidoreductase (δ12-unsaturating)
Comments: Contains non-heme iron.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 197025-40-4
References:
1. Banas, A., Bafor, M., Wiberg, E., Lenman, M., Staahl, U. and Stymne, S. Biosynthesis of an acetylenic fatty acid in microsomal preparations from developing seeds Crepis alpina. Physiol. Biochem. Mol. Biol. Plant Lipids [Proc. Int. Symp. Plant Lipids] 12th (1997) 57-59.
2. Lee, M., Lenman, M., Banas, A., Bafor, M., Singh, S., Schweizer, M., Nilsson, R., Liljenberg, C., Dahlqvist, A., Gummeson, P.O., Sjodahl, S., Green, A. and Stymne, S. Identification of non-heme di-iron proteins that catalyze triple bond and epoxy group formation. Science 280 (1998) 915-918. [PMID: 9572738]
Accepted name: monoprenyl isoflavone epoxidase
Reaction: 7-O-methylluteone + NADPH + H+ + O2 = dihydrofurano derivatives + NADP+ + H2O
Glossary entries:
luteone: 3-(2,4-dihydroxyphenyl)-5,7-dihydroxy-6-(3-methyl-2-butenyl)-4H-1-benzopyran-4-one
naringenin: (S)-2,3-dihydo-5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-1-benzopyran-4-one
Other name(s): monoprenyl isoflavone monooxygenase; 7-O-methylluteone:O2 oxidoreductase
Systematic name: 7-O-methylluteone,NADPH:O2 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 nonenzymically 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, CAS registry number: 198496-86-5
References:
1. Tanaka, M. and Tahara, S. FAD-dependent epoxidase as a key enzyme in fungal metabolism of prenylated flavonoids. Phytochemistry 46 (1997) 433-439.
Accepted name: thiophene-2-carbonyl-CoA monooxygenase
Reaction: thiophene-2-carbonyl-CoA + AH2 + O2 = 5-hydroxythiophene-2-carbonyl-CoA + A + 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, UM-BBD, CAS registry number: 208540-44-7
References:
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]
Accepted name: β-carotene 15,15'-monooxygenase
Reaction: β-carotene + O2 = 2 retinal
For diagram of reaction click here and mechanism click here.
Other name(s): β-carotene 15,15'-dioxygenase, carotene dioxygenase; carotene 15,15'-dioxygenase
Systematic name: β-carotene:oxygen 15,15'-oxidoreductase (bond-cleaving)
Comments: Requires bile salts and Fe(II). The reaction proceeds in three stages, epoxidation of the 15,15'-double bond, hydration of the double bond leading to ring opening, and oxidative cleavage of the diol formed [cf. EC 1.14.15.6, cholesterol monooxygenase (side-chain-cleaving)]. Thus only one atom of the dioxygen is incorporated into retinal. Formerly EC 1.13.11.21 as it was considered to be a dioxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37256-60-3
References:
1. Leuenberger, M.G., Engeloch-Jarret, C. and Woggon, W.D. The reaction mechanism of the enzyme-catalysed central cleavage of β-carotene to retinal. Angew. Chem. Int. Ed. 40 (2001) 2614-2616. [PMID: 11458349]
2. Goodman, D.S., Huang, H.S., Kanai, M. and Shiratori, T. The enzymatic conversion of all-trans β-carotene into retinal. J. Biol. Chem. 242 (1967) 3543-3554.
3. Goodman, D.S., Huang, H.S. and Shiratori, T. Mechanism of the biosynthesis of vitamin A from β-carotene. J. Biol. Chem. 241 (1966) 1929-1932. [PMID: 5946623]
Accepted name: taxadiene 5α-hydroxylase
Reaction: taxa-4,11-diene + AH2 + O2 = taxa-4(20),11-dien-5α-ol + A + H2O
For diagram click here.
Systematic name: taxa-4,11-diene,hydrogen-donor:oxygen oxidoreductase (5α-hydroxylating)
Comments: Requires P-450. The reaction includes rearrangement of the 4(5)-double bond to a 4(20)-double bond, possibly through allylic oxidation.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9035-51-2
References:
1. Hefner, J., Rubenstein, S.M., Ketchum, R.E., Gibson, D.M., Williams, R.M. and Croteau, R. Cytochrome P450-catalyzed hydroxylation of taxa-4(5),11(12)-diene to taxa-4(20),11(12)-dien-5alpha-ol: the first oxygenation step in taxol biosynthesis. Chem. Biol. 3 (1996) 479-489. [PMID: 8807878]
Accepted name: cholesterol 25-hydroxylase
Reaction: cholesterol + AH2 + O2 = 25-hydroxycholesterol + A + H2O
For diagram click here.
Glossary: cholesterol = cholest-5-en-3β-ol
Other name(s): cholesterol 25-monooxygenase
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).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 60202-07-5
References:
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. [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. [PMID: 12543708]
Accepted name: ammonia monooxygenase
Reaction: ammonia + AH2 + O2 = NH2OH + A + H2O
Other name(s): AMO
Systematic name: ammonia,hydrogen-donor:oxygen oxidoreductase (hydroxylating)
Comments: Contains copper and possibly nonheme iron. The donor is membrane-bound. Electrons are derived indirectly from ubiquinol.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
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]
Accepted name: 5,6-dimethylbenzimidazole synthase
Reaction: FMNH2 + NADH + H+ + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
For diagram of reaction, click here
Other name(s): BluB
Systematic name: FMNH2 oxidoreductase (5,6-dimethylbenzimidazole forming)
Comments: The C-2 of 5,6-dimethylbenzimidazole is derived from C-1' of the ribityl group of FMNH2 and 2-H from the ribityl 1'-pro-S hydrogen. The other product may be barbiturate. For a possible mechanism click here. The stoichiometery of the reaction is not known.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Gray, M.J. and Escalante-Semerena, J.C. Single-enzyme conversion of FMNH2 to 5,6-dimethylbenzimidazole, the lower ligand of B12. Proc. Natl. Acad. Sci. USA 104 (2007) 2921-2926. [PMID: 17301238]
2. Ealick, S.E. and Begley, T.P. Biochemistry: molecular cannibalism. Nature 446:387 (2007). [PMID: 17377573]
3. Taga, M.E., Larsen, N.A., Howard-Jones, A.R., Walsh, C.T. and Walker, G.C. BluB cannibalizes flavin to form the lower ligand of vitamin B12. Nature 446:449 (2007). [PMID: 17377583]
Accepted name: all-trans-8'-apo-β-carotenal 15,15'-oxygenase
Reaction: all-trans-8'-apo-β-carotenal + O2 = all-trans-retinal + (2E,4E,6E)-2,6-dimethylocta-2,4,6-trienedial
Other name(s): Diox1; ACO; 8'-apo-β-carotenal 15,15'-oxygenase
Systematic name: all-trans-8'-apo-β-carotenal:oxygen 15,15'-oxidoreductase (bond-cleaving)
Comments: Contains an Fe2+-4His arrangement. The enzyme is involved in retinal biosynthesis in bacteria [2].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Ruch, S., Beyer, P., Ernst, H. and Al-Babili, S. Retinal biosynthesis in Eubacteria: in vitro characterization of a novel carotenoid oxygenase from Synechocystis sp. PCC 6803. Mol. Microbiol. 55 (2005) 1015-1024. [PMID: 15686550]
2. Kloer, D.P., Ruch, S., Al-Babili, S., Beyer, P. and Schulz, G.E. The structure of a retinal-forming carotenoid oxygenase. Science 308 (2005) 267-269. [PMID: 15821095]
Accepted name: zeaxanthin 7,8-dioxygenase
Reaction: zeaxanthin + 2 O2 = crocetin dialdehyde + 2 (3S)-3-hydroxycyclocitral
For diagram of reaction click here.
Other name(s): zeaxanthin 7,8(7',8')-cleavage dioxygenase; CsZCD
Systematic name: zeaxanthin:oxygen oxidoreductase (7,8-cleaving)
Comments: Presumably the enzyme acts twice on zeaxanthin cleaving 3-hydroxycyclocitral off each 3-hydroxy end group.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Bouvier, F., Suire, C., Mutterer, J. and Camara, B. Oxidative remodeling of chromoplast carotenoids: identification of the carotenoid dioxygenase CsCCD and CsZCD genes involved in Crocus secondary metabolite biogenesis. Plant Cell 15 (2003) 47-62. [PMID: 12509521]
Accepted name: β-amyrin 24-hydroxylase
Reaction: (1) β-amyrin + AH2 + O2 = 24-hydroxy-β-amyrin + A + H2O
(2) sophoradiol + AH2 + O2 = 24-hydroxysophoradiol + A + H2O
For diagram of reaction click here.
Glossary: 24-hydroxy-β-amyrin = olean-12-ene-3β,24-diol
24-hydroxysophoradiol = soyasapogenol B
Other name(s): sophoradiol 24-hydroxylase; CYP93E1
Systematic name: β-amyrin,AH2:oxygen oxidoreductase (24-hydroxylating)
Comments: A heme-thiolate protein (P-450).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Shibuya, M., Hoshino, M., Katsube, Y., Hayashi, H., Kushiro, T. and Ebizuka, Y. Identification of β-amyrin and sophoradiol 24-hydroxylase by expressed sequence tag mining and functional expression assay. FEBS J. 273 (2006) 948-959. [PMID: 16478469]
Accepted name: diapolycopene oxygenase
Reaction: 4,4'-diapolycopene + 4 AH2 + 4 O2 = 4,4'-diapolycopenedial + 4 A + 6 H2O
For diagram of reaction 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, CAS registry number:
References:
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. [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. [PMID: 15933032]
Accepted name: carotene ε-monooxygenase
Reaction: α-carotene + O2 + AH2 = α-cryptoxanthin + A + H2O
For diagram of reaction click here.
Other name(s): CYP97C1; LUT1
Systematic name: α-carotene:oxygen oxidoreductase (3-hydroxylating)
Comments: A heme-thiolate protein (P450). Also acts on zeinoxanthin to give lutein.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Pogson, B., McDonald, K.A., Truong, M., Britton, G. and DellaPenna, D. Arabidopsis carotenoid mutants demonstrate that lutein is not essential for photosynthesis in higher plants. Plant Cell 8 (1996) 1627-1639. [PMID: 8837513]
2. Tian, L., Musetti, V., Kim, J., Magallanes-Lundback, M. and DellaPenna, D. The Arabidopsis LUT1 locus encodes a member of the cytochrome P450 family that is required for carotenoid ε-ring hydroxylation activity. Proc. Natl. Acad. Sci. USA 101 (2004) 402-407. [PMID: 14709673]