L-pipecolate oxidase

L-pipecolate oxidase
Identifiers
EC no.1.5.3.7
CAS no.81669-65-0
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

L-pipecolate oxidase (EC 1.5.3.7) is an enzyme that catalyzes the chemical reaction

 
O2
H2O2
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
O2
H2O2
 
2D representation of the chemical structure of Q82559861.
(2S)-2,3,4,5-tetrahydropyridine-2-carboxylic acid

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]

2D representation of the chemical structure of Q82559861.
product
 
H2O
 
Reversible left-right reaction arrow with minor forward substrate(s) from top left and minor reverse product(s) to bottom left
H2O
 
 
 
 
 
Rightward reaction arrow
 
 
 

References

  1. ↑ Enzyme 1.5.3.7 at KEGG Pathway Database.
  2. ↑ 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.
  3. 1 2 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.