Home  |  Contact
Due to maintenance work, this service and ftp://ftp.expasy.org will be unavailable from Tuesday August 23rd 18:00 until Wednesday August 24th 08:00 CEST. Apologies for the inconvenience.

ENZYME entry: EC 1.14.15.37

Accepted Name
luteothin monooxygenase.
Reaction catalysed
4 H(+) + luteothin + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] <=> aureothin + 3 H2O + 4 oxidized [2Fe-2S]-[ferredoxin]
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

View entry in original ENZYME format
View entry in raw text format (no links)
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.15.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-