Choline dehydrogenase

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choline dehydrogenase
Identifiers
EC number1.1.99.1
CAS number9028-67-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a choline dehydrogenase (EC 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[edit]

  • Minoru Ameyama; Emiko Shinagawa; Kazunobu Matsushita; Koichi Takimoto; Koji Nakashima; Osao Adachi (1985). "Mammalian choline dehydrogenase is a quinoprotein". Agric. Biol. Chem. 49 (12): 3623&ndash, 3626. doi:10.1271/bbb1961.49.3623.
  • Ebisuzaki K, Williams JN (1955). "Preparation and partial purification of soluble choline dehydrogenase from liver mitochondria". Biochem. J. 60 (4): 644&ndash, 6. PMC 1216163. PMID 13249959.
  • Gadda G, McAllister-Wilkins EE (2003). "Cloning, Expression, and Purification of Choline Dehydrogenase from the Moderate Halophile Halomonas elongata". Appl. Environ. Microbiol. 69 (4): 2126&ndash, 32. doi:10.1128/AEM.69.4.2126-2132.2003. PMC 154813. PMID 12676692.
  • 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&ndash, 42. doi:10.1074/jbc.M210970200. PMID 12466265.