EC 1.14.99.67 - α-N-dichloroacetyl-p-aminophenylserinol N-oxygenase

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IntEnz Enzyme Nomenclature
EC 1.14.99.67

Names

Accepted name:
α-N-dichloroacetyl-p-aminophenylserinol N-oxygenase
Systematic name:
α-N-dichloroacetyl-p-aminophenylserinol,acceptor:oxygen oxidoreductase (N-hydroxylating)

Reaction

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.

Links to other databases

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

References

  1. Lu, H., Chanco, E. and Zhao, H.
    CmlI is an N-oxygenase in the biosynthesis of chloramphenicol.
    Tetrahedron 68 : 7651-7654 (2012). [PMID: 24347692]
  2. Makris, T. M., Vu, V. V., Meier, K. K., Komor, A. J., Rivard, B. S., Munck, E., Que, L., Lipscomb, J. D.
    An unusual peroxo intermediate of the arylamine oxygenase of the chloramphenicol biosynthetic pathway.
    J Am Chem Soc 137 : 1608-1617 (2015). [PMID: 25564306]
  3. Komor, A. J., Rivard, B. S., Fan, R., Guo, Y., Que, L., Lipscomb, J. D.
    CmlI N-Oxygenase Catalyzes the Final Three Steps in Chloramphenicol Biosynthesis without Dissociation of Intermediates.
    Biochemistry 56 : 4940-4950 (2017). [PMID: 28823151]

[EC 1.14.99.67 created 2020]