Shikimate dehydrogenase

From Wikipedia, the free encyclopedia

In enzymology, a shikimate dehydrogenase (EC 1.1.1.25) is an enzyme that catalyzes the chemical reaction

shikimate + NADP⁺ $\rightleftharpoons$ 3-dehydroshikimate + NADPH + H⁺

Thus, the two substrates of this enzyme are shikimate and NADP⁺, whereas its 3 products are 3-dehydroshikimate, NADPH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is shikimate:NADP+ 3-oxidoreductase. Other names in common use include dehydroshikimic reductase, shikimate oxidoreductase, shikimate:NADP+ oxidoreductase, 5-dehydroshikimate reductase, shikimate 5-dehydrogenase, 5-dehydroshikimic reductase, DHS reductase, shikimate:NADP+ 5-oxidoreductase, and AroE. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes 1NPD, 1NVT, 1NYT, 1O9B, 1P74, 1P77, 1VI2, 1WXD, 2CY0, 2D5C, 2EV9, 2GPT, 2HK7, 2HK8, 2HK9, and 2NLO.

[edit] References

IUBMB entry for 1.1.1.25
BRENDA references for 1.1.1.25 (Recommended.)
PubMed references for 1.1.1.25
PubMed Central references for 1.1.1.25
Google Scholar references for 1.1.1.25
BALINSKY D, DAVIES DD (1961). "Aromatic biosynthesis in higher plants. 1. Preparation and properties of dehydroshikimic reductase". Biochem. J. 80: 292–6. PMID 13686342.
MITSUHASHI S, DAVIS BD (1954). "Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase". Biochim. Biophys. Acta. 15: 268–80. doi:10.1016/0006-3002(54)90069-4. PMID 13208693.
YANIV H, GILVARG C (1955). "Aromatic biosynthesis. XIV. 5-Dehydroshikimic reductase". J. Biol. Chem. 213: 787–95. PMID 14367339.
Chaudhuri S, Coggins JR (1985). "The purification of shikimate dehydrogenase from Escherichia coli". Biochem. J. 226: 217–23. PMID 3883995.
Anton IA, Coggins JR (1988). "Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase". Biochem. J. 249: 319–26. PMID 3277621.
Ye S, Von Delft F, Brooun A, Knuth MW, Swanson RV, McRee DE (2003). "The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode". J. Bacteriol. 185: 4144–51. doi:10.1128/JB.185.14.4144-4151.2003. PMID 12837789.