| Entry |
|
|---|
| 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 O2 as oxidant and incorporation or
reduction of oxygen. The oxygen incorporated need not be derived
from O2;
With another compound as one donor, and incorporation of one atom of
oxygen into the other donor
 |
|---|
| 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
 |
|---|
| 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+. |
|---|
| Pathway |
PATH: ec00520 Amino sugar and nucleotide sugar metabolism |
|---|
| Orthology |
KO: K08080 CMP-N-acetylneuraminate monooxygenase |
|---|
| Genes |
PTR: 450121(CMAH)
MCC: 574186(CMAH)
MMU: 12763(Cmah)
RNO: 361245(Cmah)
CFA: 488248
BTA: 537017
ECB: 100067842
MDO: 100024047
XLA: 379989(cmah)
DRE: 431739
SPU: 586677
 |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:3202954]
Shaw L, Schauer R.
The biosynthesis of N-glycoloylneuraminic acid occurs by
hydroxylation of the CMP-glycoside of N-acetylneuraminic acid.
Biol. Chem. Hoppe. Seyler. 369 (1988) 477-86.
Sus scofa [GN:ssc] |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:1964451]
Kozutsumi Y, Kawano T, Yamakawa T, Suzuki A.
Participation of cytochrome b5 in CMP-N-acetylneuraminic acid
hydroxylation in mouse liver cytosol.
J. Biochem. (Tokyo). 108 (1990) 704-6.
Mus musculus [GN:mmu] |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:7841794]
Schneckenburger P, Shaw L, Schauer R.
Purification, characterization and reconstitution of
CMP-N-acetylneuraminate hydroxylase from mouse liver.
Glycoconj. J. 11 (1994) 194-203.
Mus musculus [GN:mmu] |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:7608218]
Kawano T, Koyama S, Takematsu H, Kozutsumi Y, Kawasaki H, Kawashima
S, Kawasaki T, Suzuki A.
Molecular cloning of cytidine monophospho-N-acetylneuraminic acid
hydroxylase. Regulation of species- and tissue-specific expression
of N-glycolylneuraminic acid.
J. Biol. Chem. 270 (1995) 16458-63.
Mus musculus [GN:mmu] |
|---|
Reference
Authors
Title
Journal
Organism
|
5 [PMID:8647250]
Schlenzka W, Shaw L, Kelm S, Schmidt CL, Bill E, Trautwein AX,
Lottspeich F, Schauer R.
CMP-N-acetylneuraminic acid hydroxylase: the first cytosolic Rieske
iron-sulphur protein to be described in Eukarya.
FEBS. Lett. 385 (1996) 197-200.
Mus musculus [GN:mmu], Sus scofa [GN:ssc] |
|---|
| 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 |
|---|
