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BRENDA support

Information on EC 1.14.99.65 - 4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein] 3-hydroxylase

for references in articles please use BRENDA:EC1.14.99.65

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IUBMB Comments

The enzyme, characterized from the bacterium Streptomyces venezuelae, participates in the biosynthesis of the antibiotic chloramphenicol. It carries an oxygen-bridged dinuclear iron cluster. The native electron donor remains unknown, and the enzyme was assayed in vitro using sodium dithionite. The enzyme only acts on its substrate when it is loaded onto the peptidyl-carrier domain of the CmlP non-ribosomal peptide synthase.

The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein]
+
+
=
2-(4-aminophenyl)-L-seryl-[CmlP-peptidyl-carrier-protein]
+
+

Synonyms
cmlA, more

REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein] + reduced acceptor + O2 = 2-(4-aminophenyl)-L-seryl-[CmlP-peptidyl-carrier-protein] + acceptor + H2O
show the reaction diagram
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PATHWAY SOURCE
PATHWAYS
MetaCyc
chloramphenicol biosynthesis
Highest Expressing Human Cell Lines
Cell Line Links Gene Links