Quinate dehydrogenase

Last updated
quinate 5-dehydrogenase
Identifiers
EC no. 1.1.1.24
CAS no. 9028-28-8
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
Search
PMC articles
PubMed articles
NCBI proteins

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

+ NAD+
 
 
 
H+
Biochem reaction arrow reversible NYYN horiz med.svg
 
H+
 
+ NADH
 

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. ↑ Mitsuhashi S, Davis BD (1954). "Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase". Biochim. Biophys. Acta. 15 (2): 268–80. doi:10.1016/0006-3002(54)90069-4. PMID   13208693.