Biology:Quinate dehydrogenase

From HandWiki
quinate 5-dehydrogenase
Identifiers
EC number1.1.1.24
CAS number9028-28-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, quinate dehydrogenase (EC 1.1.1.24) is an enzyme that catalyzes the chemical reaction

  1. REDIRECT Template:Chemical reaction

The two substrates of the enzyme are L-quinic acid and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are 3-dehydroquinic acid, reduced NADH, and a proton.[1][2][3]

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 L-quinate:NAD+ 3-oxidoreductase. Other names in common use include quinic dehydrogenase, quinate:NAD oxidoreductase, quinate 5-dehydrogenase, and quinate:NAD+ 5-oxidoreductase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.

References

  1. Enzyme 1.1.1.24 at KEGG Pathway Database.
  2. Gamborg OL (1966). "Aromatic metabolism in plants. III. Quinate dehydrogenase from mung bean cell suspension cultures". Biochim. Biophys. Acta 128: 483–491. doi:10.1016/0926-6593(66)90009-9. 
  3. "Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase". Biochim. Biophys. Acta 15 (2): 268–80. 1954. doi:10.1016/0006-3002(54)90069-4. PMID 13208693.