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
- REDIRECT Template: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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