choline oxidase
{{infobox enzyme
| Name = Choline oxidase
| EC_number = 1.1.3.17
| CAS_number = 9028-67-5
| GO_code =
| image = 4mjw.jpg
| width = 270
| caption = Choline oxidase dimer, Arthrobacter globiformis
}}
In enzymology, a choline oxidase ({{EC number|1.1.3.17}}) is an enzyme that catalyzes the chemical reaction
:choline + O2 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
{{reflist|1}}
- {{cite journal |vauthors=Ikuta S, Imamura S, Misaki H, Horiuti Y | location = Tokyo | title = Purification and characterization of choline oxidase from Arthrobacter globiformis | journal = J. Biochem. | volume = 82| pages = 1741–9 | pmid = 599154 | issue = 6 | date=December 1977 | doi=10.1093/oxfordjournals.jbchem.a131872}}
- {{cite journal |vauthors=Rozwadowski KL, Khachatourians GG, Selvaraj G | date = 1991 | title = Choline oxidase, a catabolic enzyme in Arthrobacter pascens, facilitates adaptation to osmotic stress in Escherichia coli | journal = J. Bacteriol. | volume = 173 | pages = 472–8 | pmid = 1987142 | issue = 2 | doi = 10.1128/jb.173.2.472-478.1991 | pmc = 207035 }}
- {{cite journal |vauthors=Rand T, Halkier T, Hansen OC | date = 2003 | title = Structural characterization and mapping of the covalently linked FAD cofactor in choline oxidase from Arthrobacter globiformis | journal = Biochemistry | volume = 42 | pages = 7188–94 | pmid = 12795615 | doi = 10.1021/bi0274266 | issue = 23 }}
- {{cite journal |vauthors=Gadda G, Powell NL, Menon P | date = 2004 | title = The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase | journal = Arch. Biochem. Biophys. | volume = 430 | pages = 264–73 | pmid = 15369826 | doi = 10.1016/j.abb.2004.07.011 | issue = 2 }}
- {{cite journal |vauthors=Fan F, Gadda G | date = 2005 | title = On the catalytic mechanism of choline oxidase | journal = J. Am. Chem. Soc. | volume = 127 | pages = 2067–74 | pmid = 15713082 | doi = 10.1021/ja044541q | issue = 7 }}
- {{cite journal | author = Takabe T | date = 2003 | title = Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica | journal = J. Biol. Chem. | volume = 278 | pages = 4932–42 | pmid = 12466265 | doi = 10.1074/jbc.M210970200 | last2 = Tanaka | first2 = Y | last3 = Aoki | first3 = K | last4 = Hibino | first4 = T | last5 = Jikuya | first5 = H | last6 = Takano | first6 = J | last7 = Takabe | first7 = T | last8 = Takabe | first8 = T | issue = 7 | doi-access = free }}
{{Alcohol oxidoreductases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}
Category:Enzymes of known structure
{{1.1-enzyme-stub}}