KEGG   ENZYME: 1.14.18.2Help
Entry
EC 1.14.18.2                Enzyme                                 

Name
CMP-N-acetylneuraminate monooxygenase;
CMP-N-acetylneuraminic acid hydroxylase;
CMP-Neu5Ac hydroxylase;
cytidine monophosphoacetylneuraminate monooxygenase;
N-acetylneuraminic monooxygenase;
cytidine-5'-monophosphate-N-acetylneuraminic acid hydroxylase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With another compound as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
CMP-N-acetylneuraminate,ferrocytochrome-b5:oxygen oxidoreductase (N-acetyl-hydroxylating)
Reaction(IUBMB)
CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+ = CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O [RN:R01115]
Reaction(KEGG)
R01115;
(other) R01803
Show
Substrate
CMP-N-acetylneuraminate [CPD:C00128];
ferrocytochrome b5 [CPD:C00999];
O2 [CPD:C00007];
H+ [CPD:C00080]
Product
CMP-N-glycoloylneuraminate [CPD:C03691];
ferricytochrome b5 [CPD:C00996];
H2O [CPD:C00001]
Comment
This enzyme contains both a Rieske-type [2Fe-2S] cluster and a second iron site. The ferricytochrome b5 produced is reduced by NADH and cytochrome-b5 reductase (EC 1.6.2.2). The enzyme can be activated by Fe2+ or Fe3+.
History
EC 1.14.18.2 created 1992 as EC 1.14.13.45, transferred 2003 to EC 1.14.18.2
Pathway
ec00520  Amino sugar and nucleotide sugar metabolism
Orthology
K08080  CMP-N-acetylneuraminate monooxygenase
Genes
PTR: 450121(CMAH)
PPS: 100978297(CMAH)
GGO: 101153123(CMAH)
PON: 100450703(CMAH)
NLE: 100581695
MCC: 574186(CMAH)
MCF: 102142214
CSAB: 103222034
RRO: 104663792
RBB: 108533655
MMU: 12763(Cmah)
RNO: 361245(Cmah)
CGE: 100689391(Cmah)
NGI: 103745175
HGL: 101718101
CCAN: 109687273
OCU: 100350827
TUP: 102469254
CFA: 488248
AML: 100468655
UMR: 103665030
FCA: 100750220(CMAH)
PTG: 102967256
AJU: 106968428
BTA: 537017
BOM: 102272785
BIU: 109577194
PHD: 102338808
OAS: 101106806
SSC: 396918(CMAH)
CFR: 102517286
CDK: 105089138
BACU: 102997685
LVE: 103073783
OOR: 101281745
ECB: 100067842
EPZ: 103541420
EAI: 106837858
PALE: 102894513
LAV: 104846471
TMU: 101341508
MDO: 100024047
SHR: 100929712
OAA: 100082782
ACS: 100560576
PVT: 110072915
XLA: 379989(cmahp.L)
XTR: 100216283(cmahp)
NPR: 108786896
DRE: 431739(cmah)
IPU: 108279485
AMEX: 103035192
TRU: 777967
LCO: 109138214
NCC: 104948164
PRET: 103459632
NFU: 107374035
BPEC: 110172371
SFM: 108936309
LCM: 102366592
SPU: 586677
SKO: 100367349
HCM: HCD_04105
 » show all
Taxonomy
Reference
1  [PMID:3202954]
  Authors
Shaw L, Schauer R.
  Title
The biosynthesis of N-glycoloylneuraminic acid occurs by hydroxylation of the CMP-glycoside of N-acetylneuraminic acid.
  Journal
Biol Chem Hoppe Seyler 369:477-86 (1988)
Reference
2  [PMID:1964451]
  Authors
Kozutsumi Y, Kawano T, Yamakawa T, Suzuki A.
  Title
Participation of cytochrome b5 in CMP-N-acetylneuraminic acid hydroxylation in mouse liver cytosol.
  Journal
J Biochem (Tokyo) 108:704-6 (1990)
Reference
3  [PMID:7841794]
  Authors
Schneckenburger P, Shaw L, Schauer R.
  Title
Purification, characterization and reconstitution of CMP-N-acetylneuraminate hydroxylase from mouse liver.
  Journal
Glycoconj J 11:194-203 (1994)
Reference
4  [PMID:7608218]
  Authors
Kawano T, Koyama S, Takematsu H, Kozutsumi Y, Kawasaki H, Kawashima S, Kawasaki T, Suzuki A.
  Title
Molecular cloning of cytidine monophospho-N-acetylneuraminic acid hydroxylase. Regulation of species- and tissue-specific expression of N-glycolylneuraminic acid.
  Journal
J Biol Chem 270:16458-63 (1995)
DOI:10.1074/jbc.270.27.16458
  Sequence
[mmu:12763]
Reference
5  [PMID:8647250]
  Authors
Schlenzka W, Shaw L, Kelm S, Schmidt CL, Bill E, Trautwein AX, Lottspeich F, Schauer R.
  Title
CMP-N-acetylneuraminic acid hydroxylase: the first cytosolic Rieske iron-sulphur protein to be described in Eukarya.
  Journal
FEBS Lett 385:197-200 (1996)
DOI:10.1016/0014-5793(96)00384-5
  Sequence
[ssc:396918]
Other DBs
ExplorEnz - The Enzyme Database: 1.14.18.2
IUBMB Enzyme Nomenclature: 1.14.18.2
ExPASy - ENZYME nomenclature database: 1.14.18.2
BRENDA, the Enzyme Database: 1.14.18.2
CAS: 116036-67-0

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