Choline oxidase
| Choline oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Choline oxidase dimer, Arthrobacter globiformis | |||||||||
| Identifiers | |||||||||
| EC no. | 1.1.3.17 | ||||||||
| CAS no. | 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
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.
- ^ 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. doi:10.1128/jb.173.2.472-478.1991. 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. Bibcode:2005JAChS.127.2067F. doi:10.1021/ja044541q. PMID 15713082.