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 |
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 |
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.-.-.-