| EC |
1.14.99.67 |
| Accepted name: |
α-N-dichloroacetyl-p-aminophenylserinol N-oxygenase |
| Reaction: |
α-N-dichloroacetyl-p-aminophenylserinol + reduced acceptor + 2 O2 = chloramphenicol + acceptor + 2 H2O |
| Glossary: |
α-N-dichloroacetyl-p-aminophenylserinol = N-[(1R,2R)-1-(4-aminophenyl)-1,3-dihydroxypropan-2-yl]-2,2-dichloroacetamide |
| Other name(s): |
cmlI (gene name) |
| Systematic name: |
α-N-dichloroacetyl-p-aminophenylserinol,acceptor:oxygen oxidoreductase (N-hydroxylating) |
| 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: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Lu, H., Chanco, E. and Zhao, H. CmlI is an N-oxygenase in the biosynthesis of chloramphenicol. Tetrahedron 68 (2012) 7651–7654. [DOI] [PMID: 24347692] |
| 2. |
Makris, T.M., Vu, V.V., Meier, K.K., Komor, A.J., Rivard, B.S., Munck, E., Que, L., Jr. and Lipscomb, J.D. An unusual peroxo intermediate of the arylamine oxygenase of the chloramphenicol biosynthetic pathway. J. Am. Chem. Soc. 137 (2015) 1608–1617. [DOI] [PMID: 25564306] |
| 3. |
Komor, A.J., Rivard, B.S., Fan, R., Guo, Y., Que, L., Jr. and Lipscomb, J.D. CmlI N-oxygenase catalyzes the final three steps in chloramphenicol biosynthesis without dissociation of intermediates. Biochemistry 56 (2017) 4940–4950. [DOI] [PMID: 28823151] |
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| [EC 1.14.99.67 created 2020] |
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