Choline oxidase

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is choline:oxygen 1-oxidoreductase. This enzyme participates in glycine, serine, and threonine metabolism. It employs one cofactor, FAD.

References

Ikuta S, Imamura S, Misaki H, Horiuti Y. "Purification and characterization of choline oxidase from Arthrobacter globiformis". J. Tokyo. Biochem. (6): 1741–9. PMID 599154.
Rozwadowski KL, Khachatourians GG, Selvaraj G (1991). "Choline oxidase, a catabolic enzyme in Arthrobacter pascens, facilitates adaptation to osmotic stress in Escherichia coli". J. Bacteriol. 173 (2): 472–8. PMC 207035. PMID 1987142.
Rand T, Halkier T, Hansen OC (2003). "Structural characterization and mapping of the covalently linked FAD cofactor in choline oxidase from Arthrobacter globiformis". Biochemistry. 42 (23): 7188–94. doi:10.1021/bi0274266. PMID 12795615.
Gadda G, Powell NL, Menon P (2004). "The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase". Arch. Biochem. Biophys. 430 (2): 264–73. doi:10.1016/j.abb.2004.07.011. PMID 15369826.
Fan F, Gadda G (2005). "On the catalytic mechanism of choline oxidase". J. Am. Chem. Soc. 127 (7): 2067–74. doi:10.1021/ja044541q. PMID 15713082.
Takabe T; Tanaka, Y; Aoki, K; Hibino, T; Jikuya, H; Takano, J; Takabe, T; Takabe, T (2003). "Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica". J. Biol. Chem. 278 (7): 4932–42. doi:10.1074/jbc.M210970200. PMID 12466265.

Oxidoreductases: alcohol oxidoreductases (EC 1.1)

1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Phosphogluconate dehydrogenase Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3 Beta 3-beta-HSD NSDHL 11 Beta HSD11B1 HSD11B2 17 Beta

1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)

1.1.3: oxygen acceptor	Glucose oxidase L-gulonolactone oxidase Xanthine oxidase

1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)

1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase

1.1.99: other acceptors	Choline dehydrogenase L2HGDH

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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