+ electron
acceptor
L-pipecolate dehydrogenase
| L-pipecolate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.99.3 | ||||||||
| CAS no. | 9076-63-5 | ||||||||
| 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 | ||||||||
| |||||||||
L-pipecolate dehydrogenase (EC 1.5.99.3) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are L-pipecolic acid and an electron acceptor. Its products are (2S)-2,3,4,5-tetrahydropyridine-2-carboxylic acid and the corresponding reduced acceptor.[1][2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is L-pipecolate:acceptor 1,6-oxidoreductase. This enzyme is also called L-pipecolate:(acceptor) 1,6-oxidoreductase. It participates in lysine degradation. The exact nature of the electron acceptor is unknown, unlike for the enzyme L-pipecolate oxidase, which uses oxygen.[2]
References
- ^ Enzyme 1.5.99.3 at KEGG Pathway Database.
- ^ a b Baginsky, Marietta L.; Rodwell, Victor W. (1967). "Metabolism of Pipecolic Acid in a Pseudomonas Species V. Pipecolate Oxidase and Dehydrogenase". Journal of Bacteriology. 94 (4): 1034–1039. doi:10.1128/jb.94.4.1034-1039.1967. PMC 276772. PMID 6051341.