This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Biosynthesis → Aromatic Compounds Biosynthesis|
Gallate is an essential precursor for many plant secondary metabolites, particularly hydrolyzable tannins such as gallo- and ellagitannins [Grundhofer01]. Both plants and fungi produce high concentrations of gallate [Werner97], while bacteria are known to produce small amounts.
An early intermediate of the shikimate pathway, 3-dehydroshikimate, has been implicated as a potential precursor for gallate synthesis in plants [Werner04]. A careful study has revealed that gallate is formed from 3-dehydroshikimate by the action of shikimate dehydrogenase, a multifunctional enzyme that also catalyzes the reversible reduction of 3-dehydroshikimate to shikimate [Muir11]. In the presence of NADPH the enzyme catalyzes reduction of 3-dehydroshikimate, and in the presence of NADP+ it catalyzes its oxidation to 3,5-didehydroshikimate, an unstable compound that undergoes a spontaeous and rapid rearrangement to gallate.
This observation has been confirmed by several methods. Overexpression of cloned shikimate dehydrogenase from Juglans regia in Nicotiana tabacum resulted in increase of over 500% in the accumulation of gallate. In addition, shikimate dehydrogenase enzymes that were purified from several plants, as well as the bacterium Escherichia coli, were shown to produce gallate in vitro [Muir11].
Muir11: Muir, RM, Ibáñez AM, Uratsu SL, Ingham ES, Leslie CA, McGranahan GH (2011). "Mechanism of gallic acid biosynthesis in bacteria (Escherichia coli) and walnut (Juglans regia)." Plant Mol Biol. [Epub ahead of print]. PMID: 21279669
Werner04: Werner RA, Rossmann A, Schwarz C, Bacher A, Schmidt HL, Eisenreich W (2004). "Biosynthesis of gallic acid in Rhus typhina: discrimination between alternative pathways from natural oxygen isotope abundance." Phytochemistry 65(20);2809-13. PMID: 15474568
Adachi08: Adachi O, Ano Y, Toyama H, Matsushita K (2008). "A novel 3-dehydroquinate dehydratase catalyzing extracellular formation of 3-dehydroshikimate by oxidative fermentation of Gluconobacter oxydans IFO 3244." Biosci Biotechnol Biochem 72(6);1475-82. PMID: 18540103
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Duncan86a: Duncan K, Chaudhuri S, Campbell MS, Coggins JR (1986). "The overexpression and complete amino acid sequence of Escherichia coli 3-dehydroquinase." Biochem J 1986;238(2);475-83. PMID: 3541912
Editors, 1993: Editors: Abraham L. Sonenshein, James A. Hoch, Richard Losick (1993). "Bacillus subtilis and Other Gram-Positive Bacteria: Biochemistry, Physiology, and Molecular Genetics." American Society For Microbiology, Washington, DC 20005.
Euverink92: Euverink GJ, Hessels GI, Vrijbloed JW, Coggins JR, Dijkhuizen L (1992). "Purification and characterization of a dual function 3-dehydroquinate dehydratase from Amycolatopsis methanolica." J Gen Microbiol 138(11);2449-57. PMID: 1479361
Kleanthous92: Kleanthous C, Deka R, Davis K, Kelly SM, Cooper A, Harding SE, Price NC, Hawkins AR, Coggins JR (1992). "A comparison of the enzymological and biophysical properties of two distinct classes of dehydroquinase enzymes." Biochem J 282 ( Pt 3);687-95. PMID: 1554351
Leech95: Leech AP, James R, Coggins JR, Kleanthous C (1995). "Mutagenesis of active site residues in type I dehydroquinase from Escherichia coli. Stalled catalysis in a histidine to alanine mutant." J Biol Chem 270(43);25827-36. PMID: 7592767
LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532
MITSUHASHI54a: MITSUHASHI S, DAVIS BD (1954). "Aromatic biosynthesis. XII. Conversion of 5-dehydroquinic acid to 5-dehydroshikimic acid dy 5-dehydroquinase." Biochim Biophys Acta 15(1);54-61. PMID: 13198937
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