“CMP-N-acetylneuraminate monooxygenase”的意思、由来-开放百科全书

词条

CMP-N-acetylneuraminate monooxygenase

释义

References

{{enzyme
| Name = CMP-N-acetylneuraminate monooxygenase
| EC_number = 1.14.18.2
| CAS_number = 116036-67-0
| IUBMB_EC_number = 1/14/18/2
| GO_code = 0030338
| image =
| width =
| caption =
}}

In enzymology, a CMP-N-acetylneuraminate monooxygenase ({{EC number|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

{{cite journal | doi = 10.1515/bchm3.1988.369.1.477 | vauthors = Shaw L, Schauer R | year = 1988 | title = The biosynthesis of N-glycoloylneuraminic acid occurs by hydroxylation of the CMP-glycoside of N-acetylneuraminic acid | journal = Biol. Chem. Hoppe-Seyler | volume = 369 | pages = 477–86 | pmid = 3202954 | issue = 6 }}
{{cite journal | vauthors = Kozutsumi Y, Kawano T, Yamakawa T, Suzuki A | location = Tokyo | title = Participation of cytochrome b5 in CMP-N-acetylneuraminic acid hydroxylation in mouse liver cytosol | journal = J. Biochem. | volume = 108| pages = 704–6 | pmid = 1964451 | issue = 5 | date=November 1990}}
{{cite journal | vauthors = Schneckenburger P, Shaw L, Schauer R | year = 1994 | title = Purification, characterization and reconstitution of CMP-N-acetylneuraminate hydroxylase from mouse liver | journal = Glycoconj. J. | volume = 11 | pages = 194–203 | pmid = 7841794 | doi = 10.1007/BF00731218 | issue = 3 }}
{{cite journal | vauthors = Kawano T, Koyama S, Takematsu H | display-authors = etal | year = 1995 | 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. | volume = 270 | pages = 16458–63 | pmid = 7608218 | issue = 27 | doi=10.1074/jbc.270.27.16458}}
{{cite journal | vauthors = Lottspeich F, Schauer R | year = 1996 | title = CMP-N-acetylneuraminic acid hydroxylase: the first cytosolic Rieske iron-sulphur protein to be described in Eukarya | journal = FEBS Lett. | volume = 385 | pages = 197–200 | pmid = 8647250 | doi = 10.1016/0014-5793(96)00384-5 | issue = 3 }}

2 : EC 1.14.18|Enzymes of unknown structure

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