Quinate/shikimate dehydrogenase
| Quinate/shikimate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 | ||||||||
| |||||||||
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
[edit]- ^ Michel G, Roszak AW, Sauvé V, Maclean J, Matte A, Coggins JR, Cygler M, Lapthorn AJ (May 2003). "Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities". The Journal of Biological Chemistry. 278 (21): 19463–72. doi:10.1074/jbc.M300794200. PMID 12637497.
- ^ Benach J, Lee I, Edstrom W, Kuzin AP, Chiang Y, Acton TB, Montelione GT, Hunt JF (May 2003). "The 2.3-A crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase". The Journal of Biological Chemistry. 278 (21): 19176–82. doi:10.1074/jbc.M301348200. PMID 12624088.
External links
[edit]- Quinate/shikimate+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
