ENZYME entry: EC 1.14.15.37
| Accepted Name |
|---|
| Luteothin monooxygenase.
|
| Reaction catalysed |
|---|
| Luteothin + 2 O(2) + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H(+) <=> aureothin + 3 H(2)O + 4 oxidized ferredoxin [iron-sulfur] cluster |
| Comment(s) |
|---|
- The enzyme, characterized from the bacterium Streptomyces thioluteus,
is a bifunctional cytochrome P450 (heme-thiolate) protein that
catalyzes 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 catalyzes a similar reaction that forms
spectinabilin.
|
| Cross-references |
|---|
| BRENDA | 1.14.15.37 |
| EC2PDB | 1.14.15.37 |
| ExplorEnz | 1.14.15.37 |
| PRIAM enzyme-specific profiles | 1.14.15.37 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.14.15.37 |
| IUBMB Enzyme Nomenclature | 1.14.15.37 |
| IntEnz | 1.14.15.37 |
| MEDLINE | Find literature relating to 1.14.15.37 |
| MetaCyc | 1.14.15.37 |
| Rhea expert-curated reactions | 1.14.15.37 |
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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.14.15.-
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