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Information on EC 1.14.99.67 - alpha-N-dichloroacetyl-p-aminophenylserinol N-oxygenase

for references in articles please use BRENDA:EC1.14.99.67
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IUBMB Comments
The enzyme, isolated from the bacterium Streptomyces venezuelae, is involved in the biosynthesis of the antibiotic chloramphenicol. It contains a carboxylate-bridged binuclear non-heme iron cluster. The components of the native electron chain have not been identified, although the immediate donor is likely to be an iron-sulfur protein. The reaction mechanism involves formation of an extremely stable peroxo intermediate that catalyses three individual two-electron oxidations via a hydroxylamine and a nitroso intermediates without releasing the intermediates. cf. EC 1.14.99.68, 4-aminobenzoate N-oxygenase.
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The expected taxonomic range for this enzyme is: Streptomyces venezuelae
Reaction Schemes
alpha-N-dichloroacetyl-p-aminophenylserinol
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2
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2
alpha-N-dichloroacetyl-p-aminophenylserinol
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2
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2
Synonyms
cmlI, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-N-dichloroacetyl-p-aminophenylserinol + reduced acceptor + 2 O2 = chloramphenicol + acceptor + 2 H2O
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