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
Amino sugar and nucleotide sugar metabolism
Biosynthesis of secondary metabolites
Orthology
K08080  
CMP-N-acetylneuraminate monooxygenase
Genes
PTR: 
450121(CMAH)
PPS: 
100978297(CMAH)
GGO: 
PON: 
MCC: 
574186(CMAH)
MCF: 
MMU: 
12763(Cmah)
RNO: 
361245(Cmah)
CGE: 
100689391(Cmah)
HGL: 
TUP: 
CFA: 
AML: 
FCA: 
100750220(CMAH)
PTG: 
BTA: 
BOM: 
PHD: 
CHX: 
OAS: 
SSC: 
396918(CMAH)
CFR: 
BACU: 
LVE: 
ECB: 
PALE: 
MDO: 
SHR: 
OAA: 
ACS: 
XLA: 
379989(cmahp)
XTR: 
100216283(cmahp)
DRE: 
431739(cmah)
TRU: 
MZE: 
XMA: 
LCM: 
BFO: 
SPU: 
OTA: 
MIS: 
HFE: 
HBI: 
HCM: 
HHM: 
NKR: 
 » 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 (1988) 477-86.
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 (1990) 704-6.
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 (1994) 194-203.
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 (1995) 16458-63.
  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 (1996) 197-200.
  Sequence
[ssc:396918]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
116036-67-0

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