CMP-N-acetylneuraminate monooxygenase
| CMP-N-acetylneuraminate monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.18.2 | ||||||||
| CAS no. | 116036-67-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a CMP-N-acetylneuraminate monooxygenase (EC 1.14.18.2) is an enzyme that catalyzes the chemical reaction
- CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+ CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O
The 4 substrates of this enzyme are CMP-N-acetylneuraminate, ferrocytochrome b5, O2, and H+, whereas its 3 products are CMP-N-glycoloylneuraminate, ferricytochrome b5, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those 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 o oxygen into the other donor. The systematic name of this enzyme class is CMP-N-acetylneuraminate,ferrocytochrome-b5:oxygen oxidoreductase (N-acetyl-hydroxylating). Other names in common use include CMP-N-acetylneuraminic acid hydroxylase, CMP-Neu5Ac hydroxylase, cytidine monophosphoacetylneuraminate monooxygenase, N-acetylneuraminic monooxygenase, and cytidine-5'-monophosphate-N-acetylneuraminic acid hydroxylase. This enzyme participates in aminosugars metabolism.
References
- Shaw L, Schauer R (1988). "The biosynthesis of N-glycoloylneuraminic acid occurs by hydroxylation of the CMP-glycoside of N-acetylneuraminic acid". Biol. Chem. Hoppe-Seyler. 369 (6): 477–86. doi:10.1515/bchm3.1988.369.1.477. PMID 3202954.
- Kozutsumi Y, Kawano T, Yamakawa T, Suzuki A (November 1990). "Participation of cytochrome b5 in CMP-N-acetylneuraminic acid hydroxylation in mouse liver cytosol". J. Biochem. 108 (5). Tokyo: 704–6. PMID 1964451.
- Schneckenburger P, Shaw L, Schauer R (1994). "Purification, characterization and reconstitution of CMP-N-acetylneuraminate hydroxylase from mouse liver". Glycoconj. J. 11 (3): 194–203. doi:10.1007/BF00731218. PMID 7841794.
- Kawano T, Koyama S, Takematsu H, et al. (1995). "Molecular cloning of cytidine monophospho-N-acetylneuraminic acid hydroxylase. Regulation of species- and tissue-specific expression of N-glycolylneuraminic acid". J. Biol. Chem. 270 (27): 16458–63. doi:10.1074/jbc.270.27.16458. PMID 7608218.
- Lottspeich F, Schauer R (1996). "CMP-N-acetylneuraminic acid hydroxylase: the first cytosolic Rieske iron-sulphur protein to be described in Eukarya". FEBS Lett. 385 (3): 197–200. doi:10.1016/0014-5793(96)00384-5. PMID 8647250.
