Biology:Choline oxidase
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Short description: Class of enzymes
| 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 | ||||||||
| |||||||||
In enzymology, choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes two consecutive chemical reactions
- REDIRECT Template:Chemical reaction
- REDIRECT Template:Chemical reaction
The two substrates of this enzyme are choline and oxygen. The first reaction gives betaine aldehyde and hydrogen peroxide. The aldehyde intermediate is then further oxidised to trimethylglycine.[1][2]
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.[3][4][5][6]
References
- ↑ Enzyme 1.1.3.17 at KEGG Pathway Database.
- ↑ 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.
- ↑ "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. Bibcode: 2005JAChS.127.2067F.
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