KEGG   ENZYME: 1.14.99.67
Entry
EC 1.14.99.67               Enzyme                                 

Name
alpha-N-dichloroacetyl-p-aminophenylserinol N-oxygenase;
cmlI (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
Miscellaneous
Sysname
alpha-N-dichloroacetyl-p-aminophenylserinol,acceptor:oxygen oxidoreductase (N-hydroxylating)
Reaction(IUBMB)
alpha-N-dichloroacetyl-p-aminophenylserinol + reduced acceptor + 2 O2 = chloramphenicol + acceptor + 2 H2O [RN:R12674]
Reaction(KEGG)
R12674
Substrate
alpha-N-dichloroacetyl-p-aminophenylserinol [CPD:C22323];
reduced acceptor [CPD:C00030];
O2 [CPD:C00007]
Product
chloramphenicol [CPD:C00918];
acceptor [CPD:C00028];
H2O [CPD:C00001]
Comment
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.
History
EC 1.14.99.67 created 2020
Orthology
K24704  alpha-N-dichloroacetyl-p-aminophenylserinol N-oxygenase
Genes
NTP: CRH09_21930
NOZ: DMB37_12270
RHA: RHA1_ro02976 RHA1_ro06104
RER: RER_18460
REY: O5Y_08865
REB: XU06_09100
ROP: ROP_61610
ROA: Pd630_LPD02745 Pd630_LPD07213
REQ: REQ_23830
RPY: Y013_04225
RHB: NY08_1916
GOR: KTR9_2685
SVE: SVEN_0924
SLD: T261_0698
KAL: KALB_4450
 » show all
Reference
1  [PMID:24347692]
  Authors
Lu H, Chanco E, Zhao H.
  Title
CmlI is an N-oxygenase in the biosynthesis of chloramphenicol.
  Journal
Tetrahedron 68 (2012)
DOI:10.1016/j.tet.2012.06.036
Reference
2  [PMID:25564306]
  Authors
Makris TM, Vu VV, Meier KK, Komor AJ, Rivard BS, Munck E, Que L Jr, Lipscomb JD.
  Title
An unusual peroxo intermediate of the arylamine oxygenase of the chloramphenicol biosynthetic pathway.
  Journal
J Am Chem Soc 137:1608-17 (2015)
DOI:10.1021/ja511649n
Reference
3  [PMID:28823151]
  Authors
Komor AJ, Rivard BS, Fan R, Guo Y, Que L Jr, Lipscomb JD.
  Title
CmlI N-Oxygenase Catalyzes the Final Three Steps in Chloramphenicol Biosynthesis without Dissociation of Intermediates.
  Journal
Biochemistry 56:4940-4950 (2017)
DOI:10.1021/acs.biochem.7b00695
Other DBs
ExplorEnz - The Enzyme Database: 1.14.99.67
IUBMB Enzyme Nomenclature: 1.14.99.67
ExPASy - ENZYME nomenclature database: 1.14.99.67
BRENDA, the Enzyme Database: 1.14.99.67

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