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
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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.