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
Search PMC articles PubMed articles NCBI proteins

In enzymology, a choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes the chemical reaction

choline + O₂ ${\displaystyle \rightleftharpoons }$ 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

• Ikuta S, Imamura S, Misaki H, Horiuti Y (December 1977). "Purification and characterization of choline oxidase from Arthrobacter globiformis". J. Biochem. Tokyo. 82 (6): 1741–9. doi:10.1093/oxfordjournals.jbchem.a131872. 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. 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. 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.

This page was last edited on 26 August 2023, at 13:31