| EC |
1.14.99.65 |
| Accepted name: |
4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein] 3-hydroxylase |
| Reaction: |
4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein] + reduced acceptor + O2 = 2-(4-aminophenyl)-L-seryl-[CmlP-peptidyl-carrier-protein] + acceptor + H2O |
| Other name(s): |
cmlA (gene name) |
| Systematic name: |
4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein],acceptor:oxygen 3-oxidoreductase |
| 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. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Makris, T.M., Chakrabarti, M., Munck, E. and Lipscomb, J.D. A family of diiron monooxygenases catalyzing amino acid β-hydroxylation in antibiotic biosynthesis. Proc. Natl. Acad. Sci. USA 107 (2010) 15391–15396. [PMID: 20713732] |
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| [EC 1.14.99.65 created 2019] |
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