EC - Choline dehydrogenase

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IntEnz Enzyme Nomenclature


Accepted name:
choline dehydrogenase
Other names:
choline oxidase
choline-cytochrome c reductase
choline:(acceptor) oxidoreductase
choline:(acceptor) 1-oxidoreductase
Systematic name:
choline:acceptor 1-oxidoreductase




A quinoprotein. In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyse the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. In plants, the first reaction is catalysed by EC, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC or soluble choline oxidase (EC [4]. The enzyme involved in the second step, EC, betaine-aldehyde dehydrogenase, appears to be the same in plants, animals and bacteria.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00543
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008812
CAS Registry Number: 9028-67-5
UniProtKB/Swiss-Prot: (122) [show] [UniProt]


  1. Ameyama, M., Shinagawa, E., Matsuchita, K., Takimoto, K., Nakashima, K. and Adachi, O.
    Mammalian choline dehydrogenase is a quinoprotein.
    Agric. Biol. Chem. 49 : 3623-3626 (1985).
  2. Ebisuzaki, K. and Williams, J.N.
    Preparation and partial purification of soluble choline dehydrogenase from liver mitochondria.
    Biochem. J. 60 : 644-646 (1955). [PMID: 13249959]
  3. Gadda, G. and McAllister-Wilkins, E.E.
    Cloning, expression, and purification of choline dehydrogenase from the moderate halophile Halomonas elongata.
    Appl. Environ. Microbiol. 69 : 2126-2132 (2003). [PMID: 12676692]
  4. Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T.
    Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica.
    J. Biol. Chem. 278 : 4932-4942 (2003). [PMID: 12466265]

[EC created 1961, modified 1989, modified 2005]