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Pathway Description
Chorismate Biosynthesis
Escherichia coli
Metabolic Pathway
Chorismate is an intermediate in tyrosine, phenylalanine and tryptophan synthesis and a precursor for folic acid, ubiquinone, enterochelin and menaquinone. Three enzymes catalyze the first step in chorismate biosynthesis. Synthesis may be reduced by feedback inhibition of tyrosine, phenylalanine and tryptophan to the enzymes. The biosynthesis of chorismate starts with D-Erythrose-4-phosphate getting transformed into 3-deoxy-D-arabino-heptulosonate-7-phosphate through a phospho-2-dehydro-3-deoxyheptonate aldolase. This is followed by a 3-dehydroquinate synthase converting the 3-deoxy-D-arabino-heptulosonate-7-phosphate into a 3-dehydroquinate which in turn is conveted to 3-dehydroshikimate through a 3-dehydroquinate dehydratase. At this point 3-dehydroshikimate can be turned into Shikimic acid through 2 different reactions involving Quinate/shikimate dehydrogenase and shikimate dehydrogenase 2. Shikimic acid is phosphorylated by Shikimate kinase 2 into shikimate 3-phosphate. Shikimate 3- phophate and a phosphoenolpyruvic acid are then joined through a 3-phosphoshikimate 1-carboxyvinyltransferase to produce a 5-enoylpyruvyl-shikimate 3-phosphate while releasing a phosphate. This in turn produces our final product Chorismate through a chorismate synthase.
References
Chorismate Biosynthesis References
Abdel-Meguid SS, Smith WW, Bild GS: Crystallization of 5-enolpyruvylshikimate 3-phosphate synthase from Escherichia coli. J Mol Biol. 1985 Dec 5;186(3):673.
Pubmed: 3912512
Akowski JP, Bauerle R: Steady-state kinetics and inhibitor binding of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (tryptophan sensitive) from Escherichia coli. Biochemistry. 1997 Dec 16;36(50):15817-22. doi: 10.1021/bi971135t.
Pubmed: 9398312
Anderson KS, Sikorski JA, Johnson KA: Evaluation of 5-enolpyruvoylshikimate-3-phosphate synthase substrate and inhibitor binding by stopped-flow and equilibrium fluorescence measurements. Biochemistry. 1988 Mar 8;27(5):1604-10.
Pubmed: 3284585
Anton IA, Coggins JR: Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase. Biochem J. 1988 Jan 15;249(2):319-26.
Pubmed: 3277621
Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H: Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 2006 May;16(5):686-91. doi: 10.1101/gr.4527806. Epub 2006 Apr 10.
Pubmed: 16606699
Baasov T, Knowles JR: Is the first enzyme of the shikimate pathway, 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (tyrosine sensitive), a copper metalloenzyme? J Bacteriol. 1989 Nov;171(11):6155-60.
Pubmed: 2572582
Benach J, Lee I, Edstrom W, Kuzin AP, Chiang Y, Acton TB, Montelione GT, Hunt JF: 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. J Biol Chem. 2003 May 23;278(21):19176-82. doi: 10.1074/jbc.M301348200. Epub 2003 Mar 6.
Pubmed: 12624088
Bender SL, Mehdi S, Knowles JR: Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis. Biochemistry. 1989 Sep 19;28(19):7555-60.
Pubmed: 2514789
Berlyn MB, Giles NH: Organization of enzymes in the polyaromatic synthetic pathway: separability in bacteria. J Bacteriol. 1969 Jul;99(1):222-30.
Pubmed: 4979440
Berti PJ, Chindemi P: Catalytic residues and an electrostatic sandwich that promote enolpyruvyl shikimate 3-phosphate synthase (AroA) catalysis. Biochemistry. 2009 May 5;48(17):3699-707. doi: 10.1021/bi802251s.
Pubmed: 19271774
Bondinell WE, Vnek J, Knowles PF, Sprecher M, Sprinson DB: On the mechanism of 5-enolpyruvylshikimate 3-phosphate synthetase. J Biol Chem. 1971 Oct 25;246(20):6191-6.
Pubmed: 4942558
Bornemann S, Theoclitou ME, Brune M, Webb MR, Thorneley RN, Abell C: A Secondary beta Deuterium Kinetic Isotope Effect in the Chorismate Synthase Reaction. Bioorg Chem. 2000 Aug;28(4):191-204. doi: 10.1006/bioo.2000.1174.
Pubmed: 11034781
Bornemann S: Flavoenzymes that catalyse reactions with no net redox change. Nat Prod Rep. 2002 Dec;19(6):761-72.
Pubmed: 12521268
Bornemann S, Balasubramanian S, Coggins JR, Abell C, Lowe DJ, Thorneley RN: Escherichia coli chorismate synthase: a deuterium kinetic-isotope effect under single-turnover and steady-state conditions shows that a flavin intermediate forms before the C-(6proR)-H bond is cleaved. Biochem J. 1995 Feb 1;305 ( Pt 3):707-10.
Pubmed: 7848266
Bornemann S, Ramjee MK, Balasubramanian S, Abell C, Coggins JR, Lowe DJ, Thorneley RN: Escherichia coli chorismate synthase catalyzes the conversion of (6S)-6-fluoro-5-enolpyruvylshikimate-3-phosphate to 6-fluorochorismate. Implications for the enzyme mechanism and the antimicrobial action of (6S)-6-fluoroshikimate. J Biol Chem. 1995 Sep 29;270(39):22811-5.
Pubmed: 7559411
Bornemann S, Lowe DJ, Thorneley RN: The transient kinetics of Escherichia coli chorismate synthase: substrate consumption, product formation, phosphate dissociation, and characterization of a flavin intermediate. Biochemistry. 1996 Jul 30;35(30):9907-16. doi: 10.1021/bi952958q.
Pubmed: 8703965
Bornemann S, Lowe DJ, Thorneley RN: Escherichia coli chorismate synthase. Biochem Soc Trans. 1996 Feb;24(1):84-8.
Pubmed: 8674765
Camakaris J, Pittard J: Repression of 3-deoxy-D-arabinoheptulosonic acid-7-phosphate synthetase (trp) and enzymes of the tryptophan pathway in Escherichia coli K-12. J Bacteriol. 1971 Aug;107(2):406-14.
Pubmed: 4939760
Camakaris J, Pittard J: Purification and properties of 3-deoxy-D-arabionheptulosonic acid-7-phosphate synthetase (trp) from Escherichia coli. J Bacteriol. 1974 Nov;120(2):590-7.
Pubmed: 4218228
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