ExplorEnz: EC 1.1.1.282

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1.1.1.282

Accepted name:

quinate/shikimate dehydrogenase [NAD(P)⁺]

Reaction:

(1) L-quinate + NAD(P)⁺ = 3-dehydroquinate + NAD(P)H + H⁺
(2) shikimate + NAD(P)⁺ = 3-dehydroshikimate + NAD(P)H + H⁺

For diagram of shikimate and chorismate biosynthesis, 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):

YdiB; quinate/shikimate dehydrogenase (ambiguous)

Systematic name:

L-quinate:NAD(P)⁺ 3-oxidoreductase

Comments:

This is the second shikimate dehydrogenase enzyme found in Escherichia coli. It can use both quinate and shikimate as substrates and either NAD⁺ or NADP⁺ as acceptor. The low catalytic efficiency with both quinate and shikimate suggests that neither may be the physiological substrate. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD⁺), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.25, shikimate dehydrogenase (NADP⁺).

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Michel, G., Roszak, A.W., Sauvé, V., Maclean, J., Matte, A., Coggins, J.R., Cygler, M. and Lapthorn, A.J. Structures of shikimate dehydrogenase AroE and its paralog YdiB. A common structural framework for different activities. J. Biol. Chem. 278 (2003) 19463–19472. [DOI] [PMID: 12637497]
2.	Benach, J., Lee, I., Edstrom, W., Kuzin, A.P., Chiang, Y., Acton, T.B., Montelione, G.T. and Hunt, J.F. The 2.3-Å crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase. J. Biol. Chem. 278 (2003) 19176–19182. [DOI] [PMID: 12624088]

[EC 1.1.1.282 created 2004, modified 2021]