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Your query returned 11 entries. 
Printable version
| EC | 1.14.15.3 | ||||||||
| Accepted name: | alkane 1-monooxygenase | ||||||||
| Reaction: | octane + 2 reduced rubredoxin + O2 + 2 H+ = 1-octanol + 2 oxidized rubredoxin + H2O | ||||||||
| Other name(s): | alkane 1-hydroxylase; ω-hydroxylase; fatty acid ω-hydroxylase; alkane monooxygenase; 1-hydroxylase; alkane hydroxylase | ||||||||
| Systematic name: | alkane,reduced-rubredoxin:oxygen 1-oxidoreductase | ||||||||
| Comments: | Some enzymes in this group are heme-thiolate proteins (P-450). Also hydroxylates fatty acids in the ω-position. | ||||||||
| Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9059-16-9 | ||||||||
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| EC | 1.14.15.30 | ||||||||
| Accepted name: | 3-ketosteroid 9α-monooxygenase | ||||||||
| Reaction: | androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9α-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | ||||||||
| Other name(s): | KshA; 3-ketosteroid 9α-hydroxylase | ||||||||
| Systematic name: | androsta-1,4-diene-3,17-dione,[reduced ferredoxin]:oxygen oxidoreductase (9α-hydroxylating) | ||||||||
| Comments: | The enzyme is involved in the cholesterol degradation pathway of several bacterial pathogens, such as Mycobacterium tuberculosis. It forms a two-component system with a ferredoxin reductase (KshB). The enzyme contains a Rieske-type iron-sulfur center and non-heme iron. The product of the enzyme is unstable, and spontaneously converts to 3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione. | ||||||||
| Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB | ||||||||
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| EC | 1.14.15.31 | ||||||||
| Accepted name: | 2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase | ||||||||
| Reaction: | 2-hydroxy-5-methyl-1-naphthoate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 2,7-dihydroxy-5-methyl-1-naphthoate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | ||||||||
| For diagram of neocarzinostatin biosynthesis, click here | |||||||||
| Other name(s): | NcsB3 | ||||||||
| Systematic name: | 2-hydroxy-5-methyl-1-naphthoate,reduced ferredoxin:oxygen oxidoreductase (7-hydroxylating) | ||||||||
| Comments: | A cytochrome P-450 (heme-thiolate) protein involved in the synthesis of neocarzinostatin in the bacterium Streptomyces carzinostaticus. | ||||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||
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| EC | 1.14.15.32 | ||||||||
| Accepted name: | pentalenene oxygenase | ||||||||
| Reaction: | pentalenene + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + 2 O2 = pentalen-13-al + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O (overall reaction) (1a) pentalenene + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = pentalen-13-ol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O (1b) pentalen-13-ol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = pentalen-13-al + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O |
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| For diagram of humulene-based sequiterpenoid biosynthesis, click here | |||||||||
| Other name(s): | PtlI | ||||||||
| Systematic name: | pentalenene,reduced ferredoxin:oxygen 13-oxidoreductase | ||||||||
| Comments: | A cytochrome P-450 (heme-thiolate) protein found in the bacterium Streptomyces avermitilis. The enzyme is involved in the biosynthesis of pentalenolactone and related antibiotics. | ||||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||
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| EC | 1.14.15.33 | ||||||||
| Accepted name: | pikromycin synthase | ||||||||
| Reaction: | (1) narbomycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = pikromycin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O (2) narbomycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = neopikromycin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O (3) narbomycin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + 2 O2 = novapikromycin + 4 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O (4) 10-deoxymethymycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = methymycin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O (5) 10-deoxymethymycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = neomethymycin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O (6) 10-deoxymethymycin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + 2 O2 = novamethymycin + 4 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O |
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| For diagram of methymycin biosynthesis, click here and for diagram of pikromycin biosynthesis, click here | |||||||||
| Other name(s): | PikC; CYP107L1 | ||||||||
| Systematic name: | narbomycin,reduced ferredoxin:oxygen oxidoreductase (pikromycin-forming) | ||||||||
| Comments: | A cytochrome P-450 (heme-thiolate) protein. Involved in the biosynthesis of a number of bacterial macrolide antibiotics containing a desosamine glycoside unit. With narbomycin it hydroxylates at either C-12 to give pikromycin or C-14 to give neopikromycin or both positions to give narvopikromycin. With 10-deoxymethymycin it hydroxylates at either C-10 to give methymycin or C-12 to give neomethymycin or both positions to give novamethymycin. | ||||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||
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| EC | 1.14.15.34 | ||||||||
| Accepted name: | 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase | ||||||||
| Reaction: | 20-oxo-5-O-β-mycaminosyltylactone + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 5-O-β-mycaminosyltylonolide + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | ||||||||
| For diagram of tylosin biosynthesis, click here | |||||||||
| Glossary: | tylactone = (4R,5S,6S,7S,9R,11E,13E,15S,16R)-7,16-diethyl-4,6-dihydroxy-5,9,13,15-tetramethyl-1-oxacyclohexadeca-11,13-diene-2,10-dione α-D-mycaminose = 3-dimethylamino-3,6-dideoxy-α-D-glucopyranose tylonolide = 2-[(4R,5S,6S,7R,9R,11E,13E,15R,16R)-16-ethyl-4,6-dihydroxy-15-(hydroxymethyl)-5,9,13-trimethyl-2,10-dioxo-1-oxacyclohexadeca-11,13-dien-7-yl]acetaldehyde |
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| Other name(s): | tylH1 (gene name) | ||||||||
| Systematic name: | 20-oxo-5-O-β-mycaminosyltylactone,reduced ferredoxin:oxygen oxidoreductase (23-hydroxylating) | ||||||||
| Comments: | A cytochrome P-450 (heme-thiolate) protein. Involved in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria. | ||||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||
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| EC | 1.14.15.35 | ||||||||
| Accepted name: | 6-deoxyerythronolide B hydroxylase | ||||||||
| Reaction: | 6-deoxyerythronolide B + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = erythronolide B + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | ||||||||
| For diagram of erythromycin biosynthesis, click here | |||||||||
| Other name(s): | DEB hydroxylase; eryF (gene name); P450(eryF); CYP107A1 | ||||||||
| Systematic name: | 6-deoxyerythronolide-B,reduced ferredoxin:oxygen oxidoreductase | ||||||||
| Comments: | A cytochrome P-450 (heme-thiolate) protein isolated from the bacterium Saccharopolyspora erythraea. The enzyme is involved in the biosynthesis of the antibiotic erythromycin. | ||||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||
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| EC | 1.14.15.36 | ||||||||
| Accepted name: | sterol 14α-demethylase (ferredoxin) | ||||||||
| Reaction: | a 14α-methylsteroid + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2 = a Δ14-steroid + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O (overall reaction) (1a) a 14α-methylsteroid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = a 14α-hydroxymethylsteroid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O (1b) a 14α-hydroxymethylsteroid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = a 14α-formylsteroid + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O (1c) a 14α-formylsteroid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = a Δ14-steroid + formate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O |
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| Other name(s): | cyp51 (gene name) | ||||||||
| Systematic name: | sterol,reduced ferredoxin:oxygen oxidoreductase (14-methyl cleaving) | ||||||||
| Comments: | A cytochrome P-450 (heme-thiolate) protein found in several bacterial species. The enzyme, which is involved in sterol biosynthesis, catalyses a hydroxylation and a reduction of the 14α-methyl group, followed by a second hydroxylation, resulting in the elimination of formate and formation of a 14(15) double bond. The enzyme from Methylococcus capsulatus is fused to the ferredoxin by an alanine-rich linker. cf. EC 1.14.14.154, sterol 14α-demethylase. | ||||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||
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| EC | 1.14.15.37 | ||||||||
| Accepted name: | luteothin monooxygenase | ||||||||
| Reaction: | luteothin + 2 O2 + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ = aureothin + 3 H2O + 4 oxidized ferredoxin [iron-sulfur] cluster (overall reaction) (1a) luteothin + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = (7R)-7-hydroxyluteothin + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster (1b) (7R)-7-hydroxyluteothin + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = aureothin + 2 H2O + 2 oxidized ferredoxin [iron-sulfur] cluster |
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| For diagram of aureothin catabolism, click here | |||||||||
| Glossary: | luteothin = 2-[(3E,5E)-3,5-dimethyl-6-(4-nitrophenyl)hexa-3,5-dien-1-yl]-6-methoxy-3,5-dimethyl-4H-pyran-4-one aureothin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E)-2-methyl-3-(4-nitrophenyl)prop-2-en-1-ylidene]oxolan-2-yl]-4H-pyran-4-one spectinabilin = neoaureothin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E,4E,6E)-2,4,6-trimethyl-7-(4-nitrophenyl)hepta-2,4,6-trien-1-ylidene]oxolan-2-yl]-4H-pyran-4-one |
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| Other name(s): | aurH (gene name) | ||||||||
| Systematic name: | luteothin,ferredoxin:oxygen oxidoreductase (aureothin-forming) | ||||||||
| Comments: | The enzyme, characterized from the bacterium Streptomyces thioluteus, is a bifunctional cytochrome P-450 (heme-thiolate) protein that catalyses both the hydroxylation of its substrate and formation of a furan ring, the final step in the biosynthesis of the antibiotic aureothin. In the bacteria Streptomyces orinoci and Streptomyces spectabilis an orthologous enzyme catalyses a similar reaction that forms spectinabilin. | ||||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||
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| EC | 1.14.15.38 | ||||||||
| Accepted name: | N,N-dimethyl phenylurea N-demethylase | ||||||||
| Reaction: | an N,N-dimethyl-N′-phenylurea compound + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = an N-methyl-N′-phenylurea compound + formaldehyde + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | ||||||||
| Other name(s): | pdmAB (gene names) | ||||||||
| Systematic name: | N,N-dimethyl-N′-phenylurea compound,NAD(P)H:oxygen oxidoreductase (formaldehyde-forming) | ||||||||
| Comments: | The enzyme, found in members of the Sphingobium genus, initiates the degradation of N,N-dimethyl-phenylurea herbicides by mono-N-demethylation. The catalytic unit contains a Rieske [2Fe-2S] iron-sulfur cluster, and catalyses the monooxygenation of a methyl group. The resulting N-methoxyl group is unstable and decomposes spontaneously to form formaldehyde. The enzyme associates with additional proteins (a reductase and a [3Fe-4S] type ferredoxin) that are involved in the transfer of electrons from NAD(P)H to the active site. | ||||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||
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| EC | 1.14.15.39 | ||||||||
| Accepted name: | epi-isozizaene 5-monooxygenase | ||||||||
| Reaction: | (+)-epi-isozizaene + 4 reduced [2Fe-2S] ferredoxin + 4 H+ + 2 O2 = albaflavenone + 4 oxidized [2Fe-2S] ferredoxin + 3 H2O (overall reaction) (1a) (+)-epi-isozizaene + 2 reduced [2Fe-2S] ferredoxin + 2 H+ + O2 = (5S)-albaflavenol + 2 oxidized [2Fe-2S] ferredoxin + H2O (1b) (5S)-albaflavenol + 2 reduced [2Fe-2S] ferredoxin + 2 H+ + O2 = albaflavenone + 2 oxidized [2Fe-2S] ferredoxin + 2 H2O (2a) (+)-epi-isozizaene + 2 reduced [2Fe-2S] ferredoxin + 2 H+ + O2 = (5R)-albaflavenol + 2 oxidized [2Fe-2S] ferredoxin + H2O (2b) (5R)-albaflavenol + 2 reduced [2Fe-2S] ferredoxin + 2 H+ + O2 = albaflavenone + 2 oxidized [2Fe-2S] ferredoxin + 2 H2O |
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| For diagram of reaction, click here | |||||||||
| Glossary: | (+)-epi-isozizaene = (3S,3aR,6S)-3,7,7,8-tetramethyl-2,3,4,5,6,7-hexahydro-1H-3a,6-methanoazulene | ||||||||
| Other name(s): | CYP170A1 | ||||||||
| Systematic name: | (+)-epi-isozizaene,reduced-ferredoxin:oxygen oxidoreductase (5-hydroxylating) | ||||||||
| Comments: | This cytochrome-P-450 enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyses two sequential allylic oxidation reactions. The substrate epi-isozizaene, which is formed by the action of EC 4.2.3.37, epi-isozizaene synthase, is first oxidized to yield the epimeric intermediates (5R)-albaflavenol and (5S)-albaflavenol, which can be further oxidized to yield the sesquiterpenoid antibiotic albaflavenone. | ||||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 1207718-51-1 | ||||||||
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