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

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IntEnz Enzyme Nomenclature
EC 1.14.99.65

Names

Accepted name:
4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein] 3-hydroxylase
Systematic name:
4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein],acceptor:oxygen 3-oxidoreductase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Makris, T. M., Chakrabarti, M., Munck, E., Lipscomb, J. D.
    A family of diiron monooxygenases catalyzing amino acid beta-hydroxylation in antibiotic biosynthesis.
    Proc. Natl. Acad. Sci. U.S.A. 107 : 15391-15396 (2010). [PMID: 20713732]

[EC 1.14.99.65 created 2019]