Quinate/shikimate dehydrogenase
Quinate/shikimate dehydrogenase | |||||||||
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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 | ||||||||
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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)+ 3-dehydroquinate + NAD(P)H + H+
- (2) shikimate + NAD(P)+ 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
- ↑ Michel, G.; Roszak, A.W.; Sauvé, V.; Maclean, J.; Matte, A.; Coggins, J.R.; Cygler, M.; 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.
- ↑ Benach, J.; Lee, I.; Edstrom, W.; Kuzin, A.P.; Chiang, Y.; Acton, T.B.; Montelione, G.T.; 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)
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