Biology:Choline dehydrogenase
| Choline dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.99.1 | ||||||||
| CAS number | 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 | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, choline dehydrogenase (EC 1.1.99.1) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are choline and an electron acceptor. Its products are glycine betaine aldehyde and the corresponding reduced acceptor.[1][2][3][4] The enzyme is a quinoprotein.[5]
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
- ↑ Enzyme 1.1.99.1 at KEGG Pathway Database.
- ↑ "Preparation and partial purification of soluble choline dehydrogenase from liver mitochondria". Biochem. J. 60 (4): 644–6. 1955. doi:10.1042/bj0600644. PMID 13249959.
- ↑ "Cloning, Expression, and Purification of Choline Dehydrogenase from the Moderate Halophile Halomonas elongata". Appl. Environ. Microbiol. 69 (4): 2126–32. 2003. doi:10.1128/AEM.69.4.2126-2132.2003. PMID 12676692. Bibcode: 2003ApEnM..69.2126G.
- ↑ 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.
- ↑ Minoru Ameyama; Emiko Shinagawa; Kazunobu Matsushita; Koichi Takimoto; Koji Nakashima; Osao Adachi (1985). "Mammalian choline dehydrogenase is a quinoprotein". Agric. Biol. Chem. 49 (12): 3623–3626. doi:10.1271/bbb1961.49.3623.
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