choline dehydrogenase
{{Short description|Class of enzymes}}
{{Infobox enzyme
| Name = Choline dehydrogenase
| EC_number = 14.03.2001
| CAS_number = 9028-67-5
| GO_code = 0008812
| image =
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In enzymology, a choline dehydrogenase ({{EC number|1.1.99.1}}) is an enzyme that catalyzes the chemical reaction
:choline + acceptor betaine aldehyde + reduced acceptor
Thus, the two substrates of this enzyme are choline and acceptor, whereas its two products are betaine aldehyde and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is choline:acceptor 1-oxidoreductase. Other names in common use include choline oxidase, choline-cytochrome c reductase, choline:(acceptor) oxidoreductase, and choline:(acceptor) 1-oxidoreductase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, PQQ.
References
{{Reflist}}
- {{cite journal | author = Minoru Ameyama | author2=Emiko Shinagawa | author3=Kazunobu Matsushita | author4=Koichi Takimoto | author5=Koji Nakashima | author6=Osao Adachi | date = 1985 | title = Mammalian choline dehydrogenase is a quinoprotein | journal = Agric. Biol. Chem. | volume = 49 | pages = 3623–3626 | doi = 10.1271/bbb1961.49.3623 | issue = 12 | doi-access = free }}
- {{cite journal |vauthors=Ebisuzaki K, Williams JN | date = 1955 | title = Preparation and partial purification of soluble choline dehydrogenase from liver mitochondria | journal = Biochem. J. | volume = 60 | pages = 644–6 | pmid = 13249959 | issue = 4 | pmc = 1216163 | doi = 10.1042/bj0600644 }}
- {{cite journal |vauthors=Gadda G, McAllister-Wilkins EE | date = 2003 | title = Cloning, Expression, and Purification of Choline Dehydrogenase from the Moderate Halophile Halomonas elongata | journal = Appl. Environ. Microbiol. | volume = 69 | pages = 2126–32 | pmid = 12676692 | doi = 10.1128/AEM.69.4.2126-2132.2003 | issue = 4 | pmc = 154813 }}
- {{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}}
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Category:Pyrroloquinoline quinone enzymes
Category:Enzymes of unknown structure
{{1.1-enzyme-stub}}