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Your query returned 3 entries. Printable version
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 | ||||
References: |
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EC | 2.1.1.353 | ||||
Accepted name: | demethylluteothin O-methyltransferase | ||||
Reaction: | S-adenosyl-L-methionine + demethylluteothin = S-adenosyl-L-homocysteine + luteothin | ||||
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): | aurI (gene name) | ||||
Systematic name: | S-adenosyl-L-methionine:demethylluteothin O-methyltransferase | ||||
Comments: | The enzyme, characterized from the bacterium Streptomyces thioluteus, participates in the biosynthesis of the antibiotic aureothin. An orthologous enzyme in the bacteria Streptomyces orinoci and Streptomyces spectabilis catalyses a similar reaction in the biosynthesis of spectinabilin. | ||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||
References: |
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EC | 2.3.1.290 | ||||
Accepted name: | spectinabilin polyketide synthase system | ||||
Reaction: | 4-nitrobenzoyl-CoA + malonyl-CoA + 6 (S)-methylmalonyl-CoA + 6 NADPH + 4 H+ = demethyldeoxyspectinabilin + 7 CO2 + 8 CoA + 6 NADP+ + 5 H2O | ||||
Glossary: | demethyldeoxyspectinabilin = 2-hydroxy-3,5-dimethyl-6-[(3E,5E,7E,9E)-3,5,7,9-tetramethyl-10-(4-nitrophenyl)deca-3,5,7,9-tetraen-1-yl]pyran-4-one spectinabilin = 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]pyran-4-one |
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Other name(s): | norAA’BC (gene names); spectinabilin polyketide synthase complex | ||||
Systematic name: | malonyl-CoA/(S)-methylmalonyl-CoA:4-nitrobenzoyl-CoA (methyl)malonyltransferase (demethyldeoxyspectinabilin-forming) | ||||
Comments: | This polyketide synthase, characterized from the bacteria Streptomyces orinoci and Streptomyces spectabilis, generates the backbone of the antibiotic spectinabilin. It is composed of 6 modules that total 28 domains and is encoded by four genes. The enzyme accepts the unusual starter unit 4-nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA. The first module (encoded by norA) is used twice in an iterative fashion, so that the seven Claisen condensation reactions are catalysed by only six modules. The iteration becomes possible by the transfer of the [acp]-bound polyketide intermediate back to the ketosynthase (KS) domain on the opposite polyketide synthase strand (polyketides are homodimeric). | ||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||
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