Biology:L-pipecolate oxidase
From HandWiki
| L-pipecolate oxidase | |||||||||
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| Identifiers | |||||||||
| EC number | 1.5.3.7 | ||||||||
| CAS number | 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 | ||||||||
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In enzymology, a L-pipecolate oxidase (EC 1.5.3.7) is an enzyme that catalyzes the chemical reaction
- L-pipecolate + O2 [math]\displaystyle{ \rightleftharpoons }[/math] 2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
Thus, the two substrates of this enzyme are L-pipecolate and O2, whereas its two products are 2,3,4,5-tetrahydropyridine-2-carboxylate and H2O2.
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. This enzyme participates in lysine degradation.
References
- "Metabolism of Pipecolic Acid in a Pseudomonas Species V. Pipecolate Oxidase and Dehydrogenase". J. Bacteriol. 94 (4): 1034–9. 1967. PMID 6051341.
- "Lysine biosynthesis in Rhodotorula glutinis: properties of pipecolic acid oxidase". J. Bacteriol. 151 (3): 1073–7. 1982. PMID 6809728.
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