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MetaCyc Pathway: gallate biosynthesis

Enzyme View:

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

Some taxa known to possess this pathway include ? : Arabidopsis thaliana col , Escherichia coli K-12 substr. MG1655 , Juglans regia

Expected Taxonomic Range: Bacteria , Fungi , Viridiplantae

Summary:
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].

Credits:
Created 07-Feb-2011 by Caspi R , SRI International


References

Grundhofer01: Grundhofer P, Niemetz R, Schilling G, Gross GG (2001). "Biosynthesis and subcellular distribution of hydrolyzable tannins." Phytochemistry 57(6);915-27. PMID: 11423141

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

Werner97: Werner I, Bacher A, Eisenreich W (1997). "Retrobiosynthetic NMR studies with 13C-labeled glucose. Formation of gallic acid in plants and fungi." J Biol Chem 272(41);25474-82. PMID: 9325260

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

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

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Chaudhuri86: Chaudhuri S, Lambert JM, McColl LA, Coggins JR (1986). "Purification and characterization of 3-dehydroquinase from Escherichia coli." Biochem J 1986;239(3);699-704. PMID: 2950851

Chaudhuri91: Chaudhuri S, Duncan K, Graham LD, Coggins JR (1991). "Identification of the active-site lysine residues of two biosynthetic 3-dehydroquinases." Biochem J 275 ( Pt 1);1-6. PMID: 1826831

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

Editors93: 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.

Elsemore95: Elsemore DA, Ornston LN (1995). "Unusual ancestry of dehydratases associated with quinate catabolism in Acinetobacter calcoaceticus." J Bacteriol 177(20);5971-8. PMID: 7592351

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

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Kinghorn81: Kinghorn JR, Schweizer M, Giles NH, Kushner SR (1981). "The cloning and analysis of the aroD gene of E. coli K-12." Gene 14(1-2);73-80. PMID: 7021325

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

Larimer83: Larimer FW, Morse CC, Beck AK, Cole KW, Gaertner FH (1983). "Isolation of the ARO1 cluster gene of Saccharomyces cerevisiae." Mol Cell Biol 3(9);1609-14. PMID: 6355828

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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

Mitsuhashi54: 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

Showing only 20 references. To show more, press the button "Show all references".


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Tue Nov 25, 2014, BIOCYC13A.