KEGG   ENZYME: 1.14.99.65
Entry
EC 1.14.99.65               Enzyme                                 

Name
4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein] 3-hydroxylase;
cmlA (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
Miscellaneous
Sysname
4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein],acceptor:oxygen 3-oxidoreductase
Reaction(IUBMB)
4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein] + reduced acceptor + O2 = 2-(4-aminophenyl)-L-seryl-[CmlP-peptidyl-carrier-protein] + acceptor + H2O
Substrate
4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein];
reduced acceptor [CPD:C00030];
O2 [CPD:C00007]
Product
2-(4-aminophenyl)-L-seryl-[CmlP-peptidyl-carrier-protein];
acceptor [CPD:C00028];
H2O [CPD:C00001]
Comment
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.
History
EC 1.14.99.65 created 2019
Orthology
K23752  4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein] 3-hydroxylase
Genes
SVE: SVEN_0921
SPUN: BFF78_28815
Reference
1  [PMID:20713732]
  Authors
Makris TM, Chakrabarti M, Munck E, Lipscomb JD
  Title
A family of diiron monooxygenases catalyzing amino acid beta-hydroxylation in antibiotic biosynthesis.
  Journal
Proc Natl Acad Sci U S A 107:15391-6 (2010)
DOI:10.1073/pnas.1007953107
Other DBs
ExplorEnz - The Enzyme Database: 1.14.99.65
IUBMB Enzyme Nomenclature: 1.14.99.65
ExPASy - ENZYME nomenclature database: 1.14.99.65
BRENDA, the Enzyme Database: 1.14.99.65

DBGET integrated database retrieval system