Enzyme Nomenclature

Continued from EC 1.14.14 to EC 1.14.19

EC 1.14.99

EC 1.14.99 Miscellaneous

Contents

EC 1.14.99.1 prostaglandin-endoperoxide synthase
EC 1.14.99.2 kynurenine 7,8-hydroxylase
EC 1.14.99.3 transferred now EC 1.14.14.18
EC 1.14.99.4 progesterone monooxygenase
EC 1.14.99.5 now EC 1.14.19.1
EC 1.14.99.6 now EC 1.14.19.2
EC 1.14.99.7 now EC 1.14.13.132
EC 1.14.99.8 deleted, included in EC 1.14.14.1
EC 1.14.99.9 transferred now EC 1.14.14.19
EC 1.14.99.10 transferred now EC 1.14.14.16
EC 1.14.99.11 estradiol 6β-monooxygenase
EC 1.14.99.12 4-androstene-3,17-dione monooxygenase
EC 1.14.99.13 now EC 1.14.13.23
EC 1.14.99.14 progesterone 11α-monooxygenase
EC 1.14.99.15 4-methoxybenzoate monooxygenase (O-demethylating)
EC 1.14.99.16 now EC 1.14.13.72
EC 1.14.99.17 now EC 1.14.16.5
EC 1.14.99.18 deleted
EC 1.14.99.19 plasmanylethanolamine desaturase
EC 1.14.99.20 phylloquinone monooxygenase (2,3-epoxidizing)
EC 1.14.99.21 Latia-luciferin monooxygenase (demethylating)
EC 1.14.99.22 ecdysone 20-monooxygenase
EC 1.14.99.23 3-hydroxybenzoate 2-monooxygenase
EC 1.14.99.24 steroid 9α-monooxygenase
EC 1.14.99.25 deleted, now EC 1.14.19.3
EC 1.14.99.26 2-hydroxypyridine 5-monooxygenase
EC 1.14.99.27 now EC 1.17.3.4
EC 1.14.99.28 transferred now EC 1.14.13.151
EC 1.14.99.29 deoxyhypusine monooxygenase
EC 1.14.99.30 transferred to EC 1.3.5.6
EC 1.14.99.31 transferred now EC 1.14.19.24
EC 1.14.99.32 transferred now EC 1.14.19.5
EC 1.14.99.33 transferred now EC 1.14.19.39
EC 1.14.99.34 monoprenyl isoflavone epoxidase
EC 1.14.99.35 thiophene-2-carbonyl-CoA monooxygenase
EC 1.14.99.36 transferred now EC 1.13.11.63
EC 1.14.99.37 taxadiene 5α-hydroxylase
EC 1.14.99.38 cholesterol 25-hydroxylase
EC 1.14.99.39 ammonia monooxygenase
EC 1.14.99.40 transferred now EC 1.13.11.79
EC 1.14.99.41 transferred now EC 1.13.11.75
EC 1.14.99.42 zeaxanthin 7,8-dioxygenase
EC 1.14.99.43 β-amyrin 24-hydroxylase
EC 1.14.99.44 diapolycopene oxygenase
EC 1.14.99.45 carotene ε-monooxygenase
EC 1.14.99.46 pyrimidine oxygenase
EC 1.14.99.47 (+)-larreatricin hydroxylase
EC 1.14.99.48 heme oxygenase (staphylobilin-producing)
EC 1.14.99.49 2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase
EC 1.14.99.50 γ-glutamyl hercynylcysteine S-oxide synthase
EC 1.14.99.51 hercynylcysteine S-oxide synthase
EC 1.14.99.52 L-cysteinyl-L-histidinylsulfoxide synthase
EC 1.14.99.53 lytic chitin monoxygenase
EC 1.14.99.54 lytic cellulose monooxygenase (C1-hydroxylating)
EC 1.14.99.55 lytic starch monooxygenase
EC 1.14.99.56 lytic cellulose monooxygenase (C4-dehydrogenating)
EC 1.14.99.57 heme oxygenase (mycobilin-producing)

EC 1.14.99.1

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

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]

[EC 1.14.99.1 created 1972, modified 1990]

EC 1.14.99.2

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)

Comments: Formerly EC 1.14.1.4.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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.

[EC 1.14.99.2 created 1965 as EC 1.14.1.4, transferred 1972 to EC 1.14.99.2]

[EC 1.14.99.3 Transferred entry: heme oxygenase (biliverdin-producing). Now EC 1.14.14.18, heme oxygenase (biliverdin-producing) (EC 1.14.99.3 created 1972, modified 2006, deleted 2015)]

EC 1.14.99.4

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 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, Metacyc, 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 1.14.99.4 created 1972, modified 1999]

[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 1.14.99.7 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]

[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)]

[EC 1.14.99.9 Transferred entry: steroid 17α-monooxygenase. Now EC 1.14.14.19, steroid 17α-monooxygenase (EC 1.14.99.9 created 1961 as EC 1.99.1.9, transferred 1965 to EC 1.14.1.7, transferred 1972 to EC 1.14.99.9, modified 2013, deleted 2015)]

[EC 1.14.99.10 Transferred entry: steroid 21-monooxygenase. Now EC 1.14.14.16, steroid 21-monooxygenase (EC 1.14.99.10 created 1961 as EC 1.99.1.11, transferred 1965 to EC 1.14.1.8, transferred 1972 to EC 1.14.99.10, modified 2013, deleted 2015)]

EC 1.14.99.11

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

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.

[EC 1.14.99.11 created 1965 as EC 1.14.1.10, transferred 1972 to EC 1.14.99.11]

EC 1.14.99.12

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 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, Metacyc, CAS registry number: 37256-74-9

References:

1. Prairie, R.L. and Talalay, P. Enzymatic formation of testololactone. Biochemistry 2 (1963) 203-208.

[EC 1.14.99.12 created 1972, modified 1999]

[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)]

EC 1.14.99.14

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

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]

[EC 1.14.99.14 created 1972]

EC 1.14.99.15

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

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 1.14.99.15 created 1972]

[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)]

EC 1.14.99.19

Accepted name: plasmanylethanolamine desaturase

Reaction: O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine + reduced acceptor + O2 = O-1-alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine + acceptor + 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, Metacyc, 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]

[EC 1.14.99.19 created 1976]

EC 1.14.99.20

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

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]

[EC 1.14.99.20 created 1976]

EC 1.14.99.21

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

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]

[EC 1.14.99.21 created 1976, modified 1982]

EC 1.14.99.22

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

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]

[EC 1.14.99.22 created 1978]

EC 1.14.99.23

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

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]

[EC 1.14.99.23 created 1984]

EC 1.14.99.24

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

References:

1. Strijewski, A. The steroid-9α-hydroxylation system from Nocardia species. Eur. J. Biochem. 128 (1982) 125-135. [PMID: 7173200]

[EC 1.14.99.24 created 1986]

[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)]

EC 1.14.99.26

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

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.

[EC 1.14.99.26 created 1989]

[EC 1.14.99.27 Transferred entry: juglone 3-monooxygenase, now classified as EC 1.17.3.4, juglone 3-monooxygenase (EC 1.14.99.27 created 1989, deleted 2016)]

[EC 1.14.99.28 Transferred entry: linalool 8-monooxygenase. Now EC 1.14.13.151, linalool 8-monooxygenase (EC 1.14.99.28 created 1989, deleted 2012)]

EC 1.14.99.29

Accepted name: deoxyhypusine monooxygenase

Reaction: [eIF5A]-deoxyhypusine + reduced acceptor + O2 = [eIF5A]-hypusine + acceptor + H2O

For diagram 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

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 1.14.99.29 created 1989]

[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)]

[EC 1.14.99.31 Transferred entry: myristoyl-CoA 11-(E) desaturase. Now classified as EC 1.14.19.24, myristoyl-CoA 11-(E) desaturase (EC 1.14.99.31 created 2000, deleted 2015)]

[EC 1.14.99.32 Transferred entry: myristoyl-CoA 11-(Z) desaturase. Now classified as EC 1.14.19.5, acyl-CoA 11-(Z)-desaturase. (EC 1.14.99.32 created 2000, deleted 2015)]

[EC 1.14.99.33 Transferred entry: Δ12-fatty acid dehydrogenase. Now EC 1.14.19.39, acyl-lipid Δ12-acetylenase (EC 1.14.99.33 created 2000, deleted 2015)]

EC 1.14.99.34

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: (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; 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 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, Metacyc, 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.

[EC 1.14.99.34 created 2000]

EC 1.14.99.35

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

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]

[EC 1.14.99.35 created 2000]

[EC 1.14.99.36 Transferred entry: β-carotene 15,15-monooxygenase. Now classified as EC 1.13.11.63, β-carotene 15,15-dioxygenase. (EC 1.14.99.36 created 1972 as EC 1.13.11.21, transferred 2001 to EC 1.14.99.36, deleted 2015)]

EC 1.14.99.37

Accepted name: taxadiene 5α-hydroxylase

Reaction: taxa-4,11-diene + reduced acceptor + O2 = taxa-4(20),11-dien-5α-ol + acceptor + 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, Metacyc, 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]

[EC 1.14.99.37 created 2002]

EC 1.14.99.38

Accepted name: cholesterol 25-hydroxylase

Reaction: cholesterol + reduced acceptor + O2 = 25-hydroxycholesterol + acceptor + 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, Metacyc, 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]

[EC 1.14.99.38 created 2005]

EC 1.14.99.39

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: Contains copper and possibly nonheme iron. The donor is membrane-bound. Electrons are derived indirectly from ubiquinol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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]

[EC 1.14.99.39 created 2010]

[EC 1.14.99.40 Transferred entry: 5,6-dimethylbenzimidazole synthase. Now EC 1.13.11.79, 5,6-dimethylbenzimidazole synthase (EC 1.14.99.40 created 2010, deleted 2014)]

[EC 1.14.99.41 Transferred entry: all-trans-8'-apo-β-carotenal 15,15'-oxygenase. Now EC 1.13.11.75, all-trans-8'-apo-β-carotenal 15,15'-oxygenase (EC 1.14.99.41 created 2010, deleted 2013)]

EC 1.14.99.42

Accepted name: zeaxanthin 7,8-dioxygenase

Reaction: zeaxanthin + 2 O2 = crocetin dialdehyde + 2 (3S)-3-hydroxycyclocitral (overall reaction)
(1a) zeaxanthin + O2 = β-citraurin + (3S)-3-hydroxycyclocitral
(1b) β-citraurin + O2 = crocetin dialdehyde + (3S)-3-hydroxycyclocitral

For diagram of reaction click here.

Glossary: β-citraurin = 3-hydroxy-β-apo-8'-carotenal

Other name(s): zeaxanthin 7,8(7',8')-cleavage dioxygenase; CsZCD (incorrect); CCD2 (gene name)

Systematic name: zeaxanthin:oxygen oxidoreductase (7,8-cleaving)

Comments: The enzyme, characterized from the plant Crocus sativus, acts twice on zeaxanthin, cleaving 3-hydroxycyclocitral off each 3-hydroxy end group. It is part of the zeaxanthin degradation pathway in that organism, leading to the different compounds that impart the color, flavor and aroma of the saffron spice.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Frusciante, S., Diretto, G., Bruno, M., Ferrante, P., Pietrella, M., Prado-Cabrero, A., Rubio-Moraga, A., Beyer, P., Gomez-Gomez, L., Al-Babili, S. and Giuliano, G. Novel carotenoid cleavage dioxygenase catalyzes the first dedicated step in saffron crocin biosynthesis. Proc. Natl. Acad. Sci. USA 111 (2014) 12246-12251. [PMID: 25097262]

[EC 1.14.99.42 created 2011, modified 2014]

EC 1.14.99.43

Accepted name: β-amyrin 24-hydroxylase

Reaction: (1) β-amyrin + reduced acceptor + O2 = 24-hydroxy-β-amyrin + acceptor + H2O
(2) sophoradiol + reduced acceptor + O2 = 24-hydroxysophoradiol + acceptor + 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, Metacyc, 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]

[EC 1.14.99.43 created 2011]

EC 1.14.99.44

Accepted name: diapolycopene oxygenase

Reaction: 4,4'-diapolycopene + 4 reduced acceptor + 4 O2 = 4,4'-diapolycopenedial + 4 acceptor + 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, Metacyc, 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]

[EC 1.14.99.44 created 2011]

EC 1.14.99.45

Accepted name: carotene ε-monooxygenase

Reaction: α-carotene + reduced acceptor + O2 = α-cryptoxanthin + acceptor + 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, Metacyc, 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]

[EC 1.14.99.45 created 2011]

EC 1.14.99.46

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, CAS registry number:

References:

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. [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. [PMID: 20400551]

[EC 1.14.99.46 created 2012]

EC 1.14.99.47

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, CAS registry number:

References:

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. [PMID: 12960376]

[EC 1.14.99.47 created 2012]

EC 1.14.99.48

Accepted name: heme oxygenase (staphylobilin-producing)

Reaction: (1) protoheme + 5 reduced acceptor + 4 O2 = 5-oxo-δ-bilirubin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
(2) protoheme + 5 reduced acceptor + 4 O2 = 15-oxo-β-bilirubin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O

For diagram of reaction click here.

Glossary: staphylobilins = 5-oxo-δ-bilirubin and 15-oxo-β-bilirubin

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 % 5-oxo-δ-bilirubin, respectively.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

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. [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. [PMID: 23600533]

[EC 1.14.99.48 created 2013, modified 2017]

EC 1.14.99.49

Accepted name: 2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase

Reaction: 2-hydroxy-5-methyl-1-naphthoate + reduced acceptor + O2 = 2,7-dihydroxy-5-methyl-1-naphthoate + oxidized acceptor + H2O

For diagram of reaction click here.

Other name(s): NcsB3

Systematic name: 2-hydroxy-5-methyl-1-naphthoate,hydrogen-donor:oxygen oxidoreductase (7-hydroxylating)

Comments: A heme-thiolate protein (P-450) enzyme involved in the synthesis of neocarzinostatin in the bacterium Streptomyces carzinostaticus.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Hang, V.T.T., Oh, T.J., Yamaguchi, T. and Sohng, J.K. In vivo characterization of NcsB3 to establish the complete biosynthesis of the naphthoic acid moiety of the neocarzinostatin chromophore. FEMS Microbiol. Lett. 311 (2010) 119-125. [PMID: 20735485]

[EC 1.14.99.49 created 2014]

EC 1.14.99.50

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 reaction 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, CAS registry number:

References:

1. Seebeck, F.P. In vitro reconstitution of Mycobacterial ergothioneine biosynthesis. J. Am. Chem. Soc. 132 (2010) 6632-6633. [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 (2014) e97774. [PMID: 24828577]

[EC 1.14.99.50 created 2015]

EC 1.14.99.51

Accepted name: hercynylcysteine S-oxide synthase

Reaction: hercynine + L-cysteine + O2 = S-(hercyn-2-yl)-L-cysteine S-oxide + H2O

For diagram of reaction click here.

Glossary: hercynine = Nα,Nα,Nα-trimethyl-L-histidine

Other name(s): Egt1; Egt-1

Systematic name: hercynine,L-cysteine:oxygen [S-(hercyn-2-yl)-L-cysteine S-oxide-forming]

Comments: Requires Fe2+ for activity. The enzyme, found in fungal species, is part of a fusion protein that also has the the activity of EC 2.1.1.44, L-histidine Nα-methyltransferase. It is part of the biosynthesis pathway of ergothioneine. The enzyme can also use L-selenocysteine to produce hercynylselenocysteine, which can be converted to selenoneine.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. 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 (2014) e97774. [PMID: 24828577]

[EC 1.14.99.51 created 2015]

EC 1.14.99.52

Accepted name: L-cysteinyl-L-histidinylsulfoxide synthase

Reaction: L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O

For diagram of reaction click here.

Glossary: S-(L-histidin-5-yl)-L-cysteine S-oxide = 5-{[(2R)-2-amino-2-carboxyethyl]sulfinyl}-L-histidine

Other name(s): OvoA

Systematic name: L-histidine,L-cysteine:oxygen [S-(L-histidin-5-yl)-L-cysteine S-oxide-forming]

Comments: Requires Fe2+ for activity. The enzyme participates in ovothiol biosynthesis. It also has some activity as EC 1.13.11.20, cysteine dioxygenase, and can perform the reaction of EC 1.14.99.50, γ-glutamyl hercynylcysteine sulfoxide synthase, albeit with low activity [4].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Braunshausen, A. and Seebeck, F.P. Identification and characterization of the first ovothiol biosynthetic enzyme. J. Am. Chem. Soc. 133 (2011) 1757-1759. [PMID: 21247153]

2. Song, H., Leninger, M., Lee, N. and Liu, P. Regioselectivity of the oxidative C-S bond formation in ergothioneine and ovothiol biosyntheses. Org. Lett. 15 (2013) 4854-4857. [PMID: 24016264]

3. Mashabela, G.T. and Seebeck, F.P. Substrate specificity of an oxygen dependent sulfoxide synthase in ovothiol biosynthesis. Chem. Commun. (Camb.) 49 (2013) 7714-7716. [PMID: 23877651]

4. Song, H., Her, A.S., Raso, F., Zhen, Z., Huo, Y. and Liu, P. Cysteine oxidation reactions catalyzed by a mononuclear non-heme iron enzyme (OvoA) in ovothiol biosynthesis. Org. Lett. 16 (2014) 2122-2125. [PMID: 24684381]

[EC 1.14.99.52 created 2015]

EC 1.14.99.53

Accepted name: lytic chitin monoxygenase

Reaction: [(1→4)-N-acetyl-β-D-glucosaminyl]n+m + reduced acceptor + O2 = [(1→4)-N-acetyl-β-D-glucosaminyl]m-1-(1→4)-N-acetyl-2-deoxy-2-amino-D-glucono-1,5-lactone + [(1→4)-N-acetyl-β-D-glucosaminyl]n + acceptor + H2O

Other name(s): LPMO (ambiguous); CBP21; chitin oxidohydrolase

Systematic name: chitin, hydrogen-donor:oxygen oxidoreductase (N-acetyl-β-D-glucosaminyl C1-hydroxylating/C4-dehdrogenating)

Comments: The enzyme cleaves chitin in an oxidative manner, releasing fragments of chitin with an N-acetylamino-D-glucono-1,5-lactone at the reducing end. The initially formed lactone at the reducing end of the shortened chitin chain quickly hydrolyses spontaneously to the aldonic acid. In vitro ascorbate can serve as reducing agent. The enzyme contains copper at the active site.

References:

1. Vaaje-Kolstad, G., Westereng, B., Horn, S.J., Liu, Z., Zhai, H., Sorlie, M. and Eijsink, V.G. An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. Science 330 (2010) 219-222. [PMID: 20929773]

2. Vaaje-Kolstad, G., Bohle, L.A., Gaseidnes, S., Dalhus, B., Bjoras, M., Mathiesen, G. and Eijsink, V.G. Characterization of the chitinolytic machinery of Enterococcus faecalis V583 and high-resolution structure of its oxidative CBM33 enzyme. J. Mol. Biol. 416 (2012) 239-254. [PMID: 22210154]

3. Gudmundsson, M., Kim, S., Wu, M., Ishida, T., Momeni, M.H., Vaaje-Kolstad, G., Lundberg, D., Royant, A., Stahlberg, J., Eijsink, V.G., Beckham, G.T. and Sandgren, M. Structural and electronic snapshots during the transition from a Cu(II) to Cu(I) metal center of a lytic polysaccharide monooxygenase by X-ray photoreduction. J. Biol. Chem. 289 (2014) 18782-18792. [PMID: 24828494]

4. Zhang, H., Zhao, Y., Cao, H., Mou, G. and Yin, H. Expression and characterization of a lytic polysaccharide monooxygenase from Bacillus thuringiensis. Int. J. Biol. Macromol. 79 (2015) 72-75. [PMID: 25936286]

[EC 1.14.99.53 created 2017]

EC 1.14.99.54

Accepted name: lytic cellulose monooxygenase (C1-hydroxylating)

Reaction: [(1→4)-β-D-glucosyl]n+m + reduced acceptor + O2 = [(1→4)-β-D-glucosyl]m-1-(1→4)-D-glucono-1,5-lactone + [(1→4)-β-D-glucosyl]n + acceptor + H2O

Other name(s): lytic polysaccharide monooxygenase (ambiguous); LPMO (ambiguous); LPMO9A

Systematic name: cellulose, hydrogen-donor:oxygen oxidoreductase (D-glucosyl C1-hydroxylating)

Comments: This copper-containing enzyme, found in fungi and bacteria, cleaves cellulose in an oxidative manner. The cellulose fragments that are formed contain a D-glucono-1,5-lactone residue at the reducing end, which hydrolyses quickly and spontaneously to the aldonic acid. The electrons are provided in vivo by the cytochrome b domain of EC 1.1.99.18, cellobiose dehydrogenase (acceptor) [1]. Ascorbate can serve as the electron donor in vitro.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Phillips, C.M., Beeson, W.T., Cate, J.H. and Marletta, M.A. Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa. ACS Chem. Biol. 6 (2011) 1399-1406. [PMID: 22004347]

2. Beeson, W.T., Phillips, C.M., Cate, J.H. and Marletta, M.A. Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases. J. Am. Chem. Soc. 134 (2012) 890-892. [PMID: 22188218]

3. Li, X., Beeson, W.T., 4th, Phillips, C.M., Marletta, M.A. and Cate, J.H. Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases. Structure 20 (2012) 1051-1061. [PMID: 22578542]

4. Bey, M., Zhou, S., Poidevin, L., Henrissat, B., Coutinho, P.M., Berrin, J.G. and Sigoillot, J.C. Cello-oligosaccharide oxidation reveals differences between two lytic polysaccharide monooxygenases (family GH61) from Podospora anserina. Appl. Environ. Microbiol. 79 (2013) 488-496. [PMID: 23124232]

5. Frommhagen, M., Sforza, S., Westphal, A.H., Visser, J., Hinz, S.W., Koetsier, M.J., van Berkel, W.J., Gruppen, H. and Kabel, M.A. Discovery of the combined oxidative cleavage of plant xylan and cellulose by a new fungal polysaccharide monooxygenase. Biotechnol. Biofuels 8 (2015) 101. [PMID: 26185526]

6. Patel, I., Kracher, D., Ma, S., Garajova, S., Haon, M., Faulds, C.B., Berrin, J.G., Ludwig, R. and Record, E. Salt-responsive lytic polysaccharide monooxygenases from the mangrove fungus Pestalotiopsis sp. NCi6. Biotechnol Biofuels 9 (2016) 108. [PMID: 27213015]

7. Courtade, G., Wimmer, R., Rohr, A.K., Preims, M., Felice, A.K., Dimarogona, M., Vaaje-Kolstad, G., Sorlie, M., Sandgren, M., Ludwig, R., Eijsink, V.G. and Aachmann, F.L. Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase. Proc. Natl. Acad. Sci. USA 113 (2016) 5922-5927. [PMID: 27152023]

[EC 1.14.99.54 created 2017]

EC 1.14.99.55

Accepted name: lytic starch monooxygenase

Reaction: starch + reduced acceptor + O2 = D-glucono-1,5-lactone-terminated malto-oligosaccharides + short-chain malto-oligosaccharides + acceptor + H2O

Other name(s): LPMO (ambiguous)

Systematic name: starch, hydrogen-donor:oxygen oxidoreductase (D-glucosyl C1-hydroxylating)

Comments: The enzyme cleaves starch in an oxidative manner. It releases fragments of starch with a D-glucono-1,5-lactone at the reducing end. The initially formed α-D-glucono-1,5-lactone at the reducing end of the shortend amylose chain quickly hydrolyses spontaneously to the aldonic acid. In vitro ascorbate has been found to be able to serve as reducing agent. The enzyme contains copper at the active site.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Vu, V.V., Beeson, W.T., Span, E.A., Farquhar, E.R. and Marletta, M.A. A family of starch-active polysaccharide monooxygenases. Proc. Natl. Acad. Sci. USA 111 (2014) 13822-13827. [PMID: 25201969]

2. Gudmundsson, M., Kim, S., Wu, M., Ishida, T., Momeni, M.H., Vaaje-Kolstad, G., Lundberg, D., Royant, A., Stahlberg, J., Eijsink, V.G., Beckham, G.T. and Sandgren, M. Structural and electronic snapshots during the transition from a Cu(II) to Cu(I) metal center of a lytic polysaccharide monooxygenase by X-ray photoreduction. J. Biol. Chem. 289 (2014) 18782-18792. [PMID: 24828494]

3. Lo Leggio, L., Simmons, T.J., Poulsen, J.C., Frandsen, K.E., Hemsworth, G.R., Stringer, M.A., von Freiesleben, P., Tovborg, M., Johansen, K.S., De Maria, L., Harris, P.V., Soong, C.L., Dupree, P., Tryfona, T., Lenfant, N., Henrissat, B., Davies, G.J. and Walton, P.H. Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase. Nat. Commun. 6 (2015) 5961. [PMID: 25608804]

[EC 1.14.99.55 created 2017]

EC 1.14.99.56

Accepted name: lytic cellulose monooxygenase (C4-dehydrogenating)

Reaction: [(1→4)-β-D-glucosyl]n+m + reduced acceptor + O2 = 4-dehydro-β-D-glucosyl-[(1→4)-β-D-glucosyl]n-1 + [(1→4)-β-D-glucosyl]m + acceptor + H2O

Systematic name: cellulose, hydrogen-donor:oxygen oxidoreductase (D-glucosyl 4-dehydrogenating)

Comments: This copper-containing enzyme, found in fungi and bacteria, cleaves cellulose in an oxidative manner. The cellulose fragments that are formed contain a 4-dehydro-D-glucose residue at the non-reducing end. Some enzymes also oxidize cellulose at the C-1 position of the reducing end forming a D-glucono-1,5-lactone residue [cf. EC 1.14.99.54, lytic cellulose monooxygenase (C1-hydroxylating)].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Beeson, W.T., Phillips, C.M., Cate, J.H. and Marletta, M.A. Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases. J. Am. Chem. Soc. 134 (2012) 890-892. [PMID: 22188218]

2. Li, X., Beeson, W.T., 4th, Phillips, C.M., Marletta, M.A. and Cate, J.H. Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases. Structure 20 (2012) 1051-1061. [PMID: 22578542]

3. Forsberg, Z., Mackenzie, A.K., Sorlie, M., Rohr, A.K., Helland, R., Arvai, A.S., Vaaje-Kolstad, G. and Eijsink, V.G. Structural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenases. Proc. Natl. Acad. Sci. USA 111 (2014) 8446-8451. [PMID: 24912171]

4. Borisova, A.S., Isaksen, T., Dimarogona, M., Kognole, A.A., Mathiesen, G., Varnai, A., Rohr, A.K., Payne, C.M., Sorlie, M., Sandgren, M. and Eijsink, V.G. Structural and functional characterization of a lytic polysaccharide monooxygenase with broad substrate specificity. J. Biol. Chem. 290 (2015) 22955-22969. [PMID: 26178376]

5. Patel, I., Kracher, D., Ma, S., Garajova, S., Haon, M., Faulds, C.B., Berrin, J.G., Ludwig, R. and Record, E. Salt-responsive lytic polysaccharide monooxygenases from the mangrove fungus Pestalotiopsis sp. NCi6. Biotechnol Biofuels 9 (2016) 108. [PMID: 27213015]

[EC 1.14.99.56 created 2017]

EC 1.14.99.57

Accepted name: heme oxygenase (mycobilin-producing)

Reaction: (1) protoheme + 3 reduced acceptor + 3 O2 = mycobilin a + Fe2+ + 3 acceptor + 3 H2O
(2) protoheme + 3 reduced acceptor + 3 O2 = mycobilin b + Fe2+ + 3 acceptor + 3 H2O

For diagram of reaction click here.

Glossary: mycobilin a = 8,12-bis(2-carboxyethyl)-19-formyl-3,7,13,18-tetramethyl-3,17-divinylbiladiene-ab-1,15(21H)-dione
mycobilin b = 8,12-bis(2-carboxyethyl)-19-formyl-2,7,13,17-tetramethyl-3,18-divinylbiladiene-ab-1,15(21H)-dione

Other name(s): mhuD (gene name)

Systematic name: protoheme,donor:oxygen oxidoreductase (mycobilin-producing)

Comments: The enzyme, characterized from the bacterium Mycobacterium tuberculosis, is involved in heme degradation and iron utilization. The enzyme binds two stacked protoheme molecules per monomer. Unlike the canonical heme oxygenases, the enzyme does not release carbon monoxide or formaldehyde. Instead, it forms unique products, named mycobilins, that retain the α-meso-carbon at the ring cleavage site as an aldehyde group. EC 1.6.2.4, NADPH-hemoprotein reductase, can act as electron donor in vitro.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Chim, N., Iniguez, A., Nguyen, T.Q. and Goulding, C.W. Unusual diheme conformation of the heme-degrading protein from Mycobacterium tuberculosis. J. Mol. Biol. 395 (2010) 595-608. [PMID: 19917297]

2. Nambu, S., Matsui, T., Goulding, C.W., Takahashi, S. and Ikeda-Saito, M. A new way to degrade heme: the Mycobacterium tuberculosis enzyme MhuD catalyzes heme degradation without generating CO. J. Biol. Chem. 288 (2013) 10101-10109. [PMID: 23420845]

3. Graves, A.B., Morse, R.P., Chao, A., Iniguez, A., Goulding, C.W. and Liptak, M.D. Crystallographic and spectroscopic insights into heme degradation by Mycobacterium tuberculosis MhuD. Inorg. Chem. 53 (2014) 5931-5940. [PMID: 24901029]

[EC 1.14.99.57 created 2017]


Continued with EC 1.15 to EC 1.97
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