L-pipecolate oxidase
| L-pipecolate oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.3.7 | ||||||||
| CAS no. | 81669-65-0 | ||||||||
| 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 | ||||||||
| |||||||||
L-pipecolate oxidase (EC 1.5.3.7) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are L-pipecolic acid and oxygen. Its products are (2S)-2,3,4,5-tetrahydropyridine-2-carboxylic acid and hydrogen peroxide.[1][2][3]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-pipecolate:oxygen 1,6-oxidoreductase. Other names in common use include pipecolate oxidase, and L-pipecolic acid oxidase.
In water, the product is hydrolysed to L-allysine, which can be converted to L-lysine in the yeasts such as Rhodotorula glutinis in which the enzyme is found.[3]
References
- ^ Enzyme 1.5.3.7 at KEGG Pathway Database.
- ^ Baginsky ML, Rodwell VW (1967). "Metabolism of Pipecolic Acid in a Pseudomonas Species V. Pipecolate Oxidase and Dehydrogenase". J. Bacteriol. 94 (4): 1034–9. doi:10.1128/jb.94.4.1034-1039.1967. PMC 276772. PMID 6051341.
- ^ a b Kinzel JJ, Bhattacharjee JK (1982). "Lysine biosynthesis in Rhodotorula glutinis: properties of pipecolic acid oxidase". J. Bacteriol. 151 (3): 1073–7. doi:10.1128/jb.151.3.1073-1077.1982. PMC 220380. PMID 6809728.