KEGG   ENZYME: 1.14.15.37
Entry
EC 1.14.15.37               Enzyme                                 
Name
luteothin monooxygenase;
aurH (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
luteothin,ferredoxin:oxygen oxidoreductase (aureothin-forming)
Reaction(IUBMB)
luteothin + 2 O2 + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ = aureothin + 3 H2O + 4 oxidized ferredoxin [iron-sulfur] cluster (overall reaction) [RN:R12324];
(1a) luteothin + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = (7R)-7-hydroxyluteothin + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster [RN:R12325];
(1b) (7R)-7-hydroxyluteothin + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = aureothin + 2 H2O + 2 oxidized ferredoxin [iron-sulfur] cluster [RN:R12326]
Reaction(KEGG)
Substrate
luteothin [CPD:C22079];
O2 [CPD:C00007];
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138];
H+ [CPD:C00080];
(7R)-7-hydroxyluteothin [CPD:C22080]
Product
aureothin [CPD:C15689];
H2O [CPD:C00001];
oxidized ferredoxin [iron-sulfur] cluster [CPD:C00139];
(7R)-7-hydroxyluteothin [CPD:C22080]
Comment
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.
History
EC 1.14.15.37 created 2019
Orthology
K23364  luteothin monooxygenase
Reference
1  [PMID:15612710]
  Authors
He J, Muller M, Hertweck C
  Title
Formation of the aureothin tetrahydrofuran ring by a bifunctional cytochrome p450 monooxygenase.
  Journal
J Am Chem Soc 126:16742-3 (2004)
DOI:10.1021/ja046104h
  Sequence
Reference
2  [PMID:17763486]
  Authors
Traitcheva N, Jenke-Kodama H, He J, Dittmann E, Hertweck C
  Title
Non-colinear polyketide biosynthesis in the aureothin and neoaureothin pathways: an evolutionary perspective.
  Journal
Chembiochem 8:1841-9 (2007)
DOI:10.1002/cbic.200700309
Other DBs
ExplorEnz - The Enzyme Database: 1.14.15.37
IUBMB Enzyme Nomenclature: 1.14.15.37
ExPASy - ENZYME nomenclature database: 1.14.15.37
BRENDA, the Enzyme Database: 1.14.15.37

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