(S)-carnitine 3-dehydrogenase
| (S)-carnitine 3-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.254 | ||||||||
| CAS no. | 169277-49-0 | ||||||||
| 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, (S)-carnitine 3-dehydrogenase (EC 1.1.1.254) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are (S)-carnitine and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are 3-dehydrocarnitine, reduced NADH, and a proton.[1][2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-carnitine:NAD+ oxidoreductase.
References
- ^ Enzyme 1.1.1.254 at KEGG Pathway Database.
- ^ Setyahadi S, Ueyama T, Arimoto T, Mori N, Kitamoto Y (1997). "Purification and properties of a new enzyme, D-carnitine dehydrogenase, from Agrobacterium sp. 525a". Biosci. Biotechnol. Biochem. 61 (6): 1055–8. doi:10.1271/bbb.61.1055. PMID 9214773.