Quinate dehydrogenase

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

L-quinate + NAD⁺ ${\displaystyle \rightleftharpoons }$ 3-dehydroquinate + NADH + H⁺

Thus, the two substrates of this enzyme are L-quinate and NAD⁺, whereas its 3 products are 3-dehydroquinate, NADH, and H⁺.

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.

• 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.
• 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.