Biology:Choline oxidase
From HandWiki
| Choline oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Choline oxidase dimer, Arthrobacter globiformis | |||||||||
| Identifiers | |||||||||
| EC number | 1.1.3.17 | ||||||||
| CAS number | 9028-67-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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In enzymology, a choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes the chemical reaction
- choline + O2 [math]\displaystyle{ \rightleftharpoons }[/math] betaine aldehyde + H2O2
Thus, the two substrates of this enzyme are choline and O2, whereas its two products are betaine aldehyde and H2O2.
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
- "Purification and characterization of choline oxidase from Arthrobacter globiformis". J. Biochem. (Tokyo) 82 (6): 1741–9. December 1977. doi:10.1093/oxfordjournals.jbchem.a131872. PMID 599154.
- "Choline oxidase, a catabolic enzyme in Arthrobacter pascens, facilitates adaptation to osmotic stress in Escherichia coli". J. Bacteriol. 173 (2): 472–8. 1991. doi:10.1128/jb.173.2.472-478.1991. PMID 1987142.
- "Structural characterization and mapping of the covalently linked FAD cofactor in choline oxidase from Arthrobacter globiformis". Biochemistry 42 (23): 7188–94. 2003. doi:10.1021/bi0274266. PMID 12795615.
- "The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase". Arch. Biochem. Biophys. 430 (2): 264–73. 2004. doi:10.1016/j.abb.2004.07.011. PMID 15369826.
- "On the catalytic mechanism of choline oxidase". J. Am. Chem. Soc. 127 (7): 2067–74. 2005. 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.
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