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
PRODPCO85_07960
PAZEKSS91_05185
PIZLAB08_R08700
PHOMKJF94_01685
CCAGSR908_04150
NTPCRH09_21930
NOZDMB37_12270
RHARHA1_ro02976 RHA1_ro06104
RERRER_18460
REYO5Y_08865
REBXU06_09100
RQIC1M55_09345
ROPROP_61610
ROAPd630_LPD02745 Pd630_LPD07213
RPYY013_04225
RBYCEJ39_15060
RHBNY08_1916
RAVAAT18_13960
RFAA3L23_00262
RHSA3Q41_03152
RHWBFN03_03395
RRZCS378_03630
RHUA3Q40_00454
RHQIM25_18430
RHODAOT96_19705
RRT4535765_02684
RCRNCTC10994_00410
RTMG4H71_16460
RKOJWS14_15730 JWS14_33265
RGOKYT97_09335
ROZCBI38_09210 CBI38_20250
RPSKJWS13_10695
RGORNMQ04_11250
RHOPD8W71_12780
REQREQ_23830
PDEFP9209_18800
GORKTR9_2685
GTABCM27_14235
GRUGCWB2_10440
GAVC5O27_17105
GODGKZ92_10145
GHNMVF96_13975
GAMIIHQ52_13385
SVESVEN_0924
SVTSVTN_15810
SCWTU94_04925
SLDT261_0698
STSIA4E84_22085
SLSSLINC_0379
SPUNBFF78_28800
SALFSMD44_00070 SMD44_08645
SHAWCEB94_22265
SCHACP983_38620
SSPBCP982_34675
STUIGCM10017668_03430
SHUNDWB77_07159
SAUHSU9_026770
SAOVG3H79_36260
SCOAQU709_42085
SFPQUY26_00155 QUY26_01020
KALKALB_4450
KUTJJ691_11490(cmlI)
 » 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 68:7651-7654 (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

DBGET integrated database retrieval system