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Information on EC 1.14.15.37 - luteothin monooxygenase

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IUBMB Comments
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.
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The expected taxonomic range for this enzyme is: Streptomyces
Reaction Schemes
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2
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4
reduced ferredoxin [iron-sulfur] cluster
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4
=
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3
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4
oxidized ferredoxin [iron-sulfur] cluster
Synonyms
AurH, More, multifunctional cytochrome P450 monooxygenase, NorH, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(7R)-7-hydroxyluteothin + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = aureothin + 2 H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
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(1b)
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luteothin + 2 O2 + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ = aureothin + 3 H2O + 4 oxidized ferredoxin [iron-sulfur] cluster
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overall reaction
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luteothin + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = (7R)-7-hydroxyluteothin + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
(1a)
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PATHWAY SOURCE
PATHWAYS
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