CMP-N-acetylneuraminate monooxygenase

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CMP-N-acetylneuraminate monooxygenase

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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⁺

\rightleftharpoons

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.

v t e Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate	Prolyl hydroxylase HIF prolyl-hydroxylase EGLN1 EGLN2 EGLN3 P4HTM Lysyl hydroxylase AlkB ALKBH1 FTO
1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 14α-demethylase 24-hydroxycholesterol 7α-hydroxylase
1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1
1.14.15: reduced iron–sulfur protein	11B1 11B2 11A1
1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase
1.14.17: reduced ascorbate	Dopamine beta-hydroxylase
1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1
1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2 Ecdysone 20-monooxygenase Deoxyhypusine monooxygenase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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