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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
BRENDA1.14.15.37
EC2PDB1.14.15.37
ExplorEnz1.14.15.37
PRIAM enzyme-specific profiles1.14.15.37
KEGG Ligand Database for Enzyme Nomenclature1.14.15.37
IUBMB Enzyme Nomenclature1.14.15.37
IntEnz1.14.15.37
MEDLINEFind literature relating to 1.14.15.37
MetaCyc1.14.15.37
Rhea expert-curated reactions1.14.15.37

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