IUBMB Enzyme Nomenclature

EC 1.1.1.24

Accepted name: quinate/shikimate dehydrogenase (NAD+)

Reaction: L-quinate + NAD+ = 3-dehydroquinate + NADH + H+

For diagram of rection, click here

Glossary: quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram. The use of the term '5-dehydroquinate' for this compound is based on an earlier system of numbering.

Other name(s): quinate dehydrogenase (ambiguous); quinic dehydrogenase (ambiguous); quinate:NAD oxidoreductase; quinate 5-dehydrogenase (ambiguous); quinate:NAD+ 5-oxidoreductase

Systematic name: L-quinate:NAD+ 3-oxidoreductase

Comments: The enzyme, found mostly in bacteria (mostly, but not exclusively in Gram-positive bacteria), fungi, and plants, participates in the degradation of quinate and shikimate with a strong preference for NAD+ as a cofactor. While the enzyme can act on both quinate and shikimate, activity is higher with the former. cf. EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+], and EC 1.1.1.25, shikimate dehydrogenase (NADP+).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-28-8

References:

1. Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase. Biochim. Biophys. Acta 15 (1954) 268-280. [PMID: 13208693]

2. Gamborg, O.L. Aromatic metabolism in plants. III. Quinate dehydrogenase from mung bean cell suspension cultures. Biochim. Biophys. Acta 128 (1966) 483-491.

3. Hawkins, A.R., Giles, N.H. and Kinghorn, J.R. Genetical and biochemical aspects of quinate breakdown in the filamentous fungus Aspergillus nidulans. Biochem. Genet. 20 (1982) 271-286. [PMID: 7049157]

4. Singh, S., Stavrinides, J., Christendat, D. and Guttman, D.S. A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass. Mol. Biol. Evol. 25 (2008) 2221-2232. [PMID: 18669580]

5. Teramoto, H., Inui, M. and Yukawa, H. Regulation of expression of genes involved in quinate and shikimate utilization in Corynebacterium glutamicum. Appl. Environ. Microbiol. 75 (2009) 3461-3468. [PMID: 19376919]

6. Kubota, T., Tanaka, Y., Hiraga, K., Inui, M. and Yukawa, H. Characterization of shikimate dehydrogenase homologues of Corynebacterium glutamicum. Appl. Microbiol. Biotechnol. 97 (2013) 8139-8149. [PMID: 23306642]

7. Peek, J. and Christendat, D. The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework. Arch. Biochem. Biophys. 566 (2015) 85-99. [PMID: 25524738]

[EC 1.1.1.24 created 1961, modified 1976, modified 2004, modified 2021]


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