1.14.15.37: luteothin monooxygenase

This is an abbreviated version!
For detailed information about luteothin monooxygenase, go to the full flat file.

Reaction

+ 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ =

+ 2 H2O + 2 oxidized ferredoxin [iron-sulfur] cluster

Synonyms

AurH, More, multifunctional cytochrome P450 monooxygenase, NorH

ECTree

1 Oxidoreductases

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor

1.14.15.37 luteothin monooxygenase

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2	AA Sequence
2	Cloned(Commentary)
2	Cofactor
1	Crystallization (Commentary)
2	General Information
1	Inhibitors
1	Metals/Ions
1	Natural Substrates/ Products (Substrates)
5	Organism
2	Pathway
1	Protein Variants
3	Reaction
5	Reference
9	Substrates and Products (Substrate)
1	Subunits
7	Synonyms
1	Systematic Name

Systematic Name

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Systematic Name on EC 1.14.15.37 - luteothin monooxygenase

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luteothin,ferredoxin:oxygen oxidoreductase (aureothin-forming)

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.