Quinate/shikimate dehydrogenase

Quinate/shikimate dehydrogenase
Identifiers
EC number	1.1.1.282
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

Quinate/shikimate dehydrogenase (EC 1.1.1.282, YdiB) is an enzyme with systematic name L-quinate:NAD(P)⁺ 3-oxidoreductase.^[1][2] This enzyme catalyses the following chemical reaction

(1) L-quinate + NAD(P)⁺ $\rightleftharpoons$ 3-dehydroquinate + NAD(P)H + H⁺

(2) shikimate + NAD(P)⁺ $\rightleftharpoons$ 3-dehydroshikimate + NAD(P)H + H⁺

This is the second shikimate dehydrogenase enzyme found in Escherichia coli and differs from EC 1.1.1.25, shikimate dehydrogenase, in that it can use both quinate and shikimate as substrate, and either NAD⁺ or NADP⁺ as acceptor.

References

1. Michel, G., Roszak, A.W., Sauvé, V., Maclean, J., Matte, A., Coggins, J.R., Cygler, M. and Lapthorn, A.J. (2003). "Structures of shikimate dehydrogenase AroE and its paralog YdiB. A common structural framework for different activities". J. Biol. Chem. 278: 19463–19472. doi:10.1074/jbc.M300794200. PMID 12637497.
2. Benach, J., Lee, I., Edstrom, W., Kuzin, A.P., Chiang, Y., Acton, T.B., Montelione, G.T. and Hunt, J.F. (2003). "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 (21): 19176–19182. doi:10.1074/jbc.M301348200. PMID 12624088.

External links

• Quinate/shikimate dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH)