Perillyl-alcohol dehydrogenase

perillyl-alcohol dehydrogenase
Identifiers
EC no.1.1.1.144
CAS no.37250-73-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, perillyl-alcohol dehydrogenase (EC 1.1.1.144) is an enzyme that catalyzes the chemical reaction

 
 
 
H+
 
H+
 
(-)-perillaldehyde
 

The two substrates of this enzyme are (-)-perillyl alcohol and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are (-)-perillaldehyde, 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 perillyl-alcohol:NAD+ oxidoreductase. This enzyme is also called perillyl alcohol dehydrogenase. This enzyme participates in limonene and pinene degradation.

References

  1. ^ Enzyme 1.1.1.144 at KEGG Pathway Database.
  2. ^ Ballal NR, Bhattacharyya PK, Rangachari PN (1966). "Perillyl alcohol dehydrogenase from a soil pseudomonad". Biochem. Biophys. Res. Commun. 23 (4): 473–8. Bibcode:1966BBRC...23..473B. doi:10.1016/0006-291X(66)90752-2. PMID 4289759.