Note: a dashed line (without arrowheads) between two compound names is meant to imply that the two names are just different instantiations of the same compound -- i.e. one may be a specific name and the other a general name, or they may both represent the same compound in different stages of a polymerization-type pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
Chorismate is the principal common precursor of the aromatic amino acids tryptophan, tyrosine and phenylalanine, as well as the essential compounds tetrahydrofolate, ubiquinone-8, menaquinone-8 and enterobactin (enterochelin). The pathway from D-erythrose-4-phosphate to chorismate is known as the common pathway, or shikimate pathway. A review of the elucidation of the common pathway and its terminal pathway branches to the aromatic amino acids can be found in the reference below.
Review: Pittard, J. and J. Yang (2008) "Biosynthesis of the Aromatic Aminio Acids." EcoSal 126.96.36.199 [ECOSAL]
Subpathways: octaprenyl diphosphate biosynthesis, ubiquinol-8 biosynthesis (prokaryotic), superpathway of aromatic amino acid biosynthesis, superpathway of ubiquinol-8 biosynthesis (prokaryotic), enterobactin biosynthesis, 1,4-dihydroxy-2-naphthoate biosynthesis, demethylmenaquinol-8 biosynthesis I, menaquinol-8 biosynthesis, superpathway of tetrahydrofolate biosynthesis, tetrahydrofolate biosynthesis, 6-hydroxymethyl-dihydropterin diphosphate biosynthesis I, 4-aminobenzoate biosynthesis, 2,3-dihydroxybenzoate biosynthesis, L-tryptophan biosynthesis, L-phenylalanine biosynthesis I, L-tyrosine biosynthesis I, chorismate biosynthesis I, 3-dehydroquinate biosynthesis I, chorismate biosynthesis from 3-dehydroquinate
Achari97: Achari A, Somers DO, Champness JN, Bryant PK, Rosemond J, Stammers DK (1997). "Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase." Nat Struct Biol 4(6);490-7. PMID: 9187658
Adachi74: Adachi O, Kohn LD, Miles EW (1974). "Crystalline alpha2 beta2 complexes of tryptophan synthetase of Escherichia coli. A comparison between the native complex and the reconstituted complex." J Biol Chem 249(24);7756-63. PMID: 4609974
Akanuma05: Akanuma S, Miyagawa H, Kitamura K, Yamagishi A (2005). "A detailed unfolding pathway of a (beta/alpha)8-barrel protein as studied by molecular dynamics simulations." Proteins 58(3);538-46. PMID: 15614829
Akowski97: Akowski JP, Bauerle R (1997). "Steady-state kinetics and inhibitor binding of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (tryptophan sensitive) from Escherichia coli." Biochemistry 1997;36(50);15817-22. PMID: 9398312
Al12: Al Mamun AA, Lombardo MJ, Shee C, Lisewski AM, Gonzalez C, Lin D, Nehring RB, Saint-Ruf C, Gibson JL, Frisch RL, Lichtarge O, Hastings PJ, Rosenberg SM (2012). "Identity and function of a large gene network underlying mutagenic repair of DNA breaks." Science 338(6112);1344-8. PMID: 23224554
Almo94: Almo SC, Smith DL, Danishefsky AT, Ringe D (1994). "The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli." Protein Eng 7(3);405-12. PMID: 7909946
Anderson88a: Anderson KS, Sikorski JA, Johnson KA (1988). "Evaluation of 5-enolpyruvoylshikimate-3-phosphate synthase substrate and inhibitor binding by stopped-flow and equilibrium fluorescence measurements." Biochemistry 1988;27(5);1604-10. PMID: 3284585
Anderson91: Anderson KS, Kati WM, Ye Q-Z, Liu J, Walsh CT, Benesi AJ (1991). "Isolation and structure elucidation of the 4-amino-4-deoxychorismate intermediate in the PABA enzymatic pathway." J. Am. Chem. Soc. 113, 3198-3200.
Appleman90: Appleman JR, Howell EE, Kraut J, Blakley RL (1990). "Role of aspartate 27 of dihydrofolate reductase from Escherichia coli in interconversion of active and inactive enzyme conformers and binding of NADPH." J Biol Chem 1990;265(10);5579-84. PMID: 2108144
Arai05: Arai M, Iwakura M (2005). "Probing the interactions between the folding elements early in the folding of Escherichia coli dihydrofolate reductase by systematic sequence perturbation analysis." J Mol Biol 347(2);337-53. PMID: 15740745
Arai07: Arai M, Kondrashkina E, Kayatekin C, Matthews CR, Iwakura M, Bilsel O (2007). "Microsecond Hydrophobic Collapse in the Folding of Escherichia coli Dihydrofolate Reductase, an alpha/beta-Type Protein." J Mol Biol 368(1);219-29. PMID: 17331539
Arifuzzaman06: 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 (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699
Armstrong89: Armstrong SK, Pettis GS, Forrester LJ, McIntosh MA (1989). "The Escherichia coli enterobactin biosynthesis gene, entD: nucleotide sequence and membrane localization of its protein product." Mol Microbiol 3(6);757-66. PMID: 2526281
Arora13: Arora K, Brooks CL (2013). "Multiple intermediates, diverse conformations, and cooperative conformational changes underlie the catalytic hydride transfer reaction of dihydrofolate reductase." Top Curr Chem 337;165-87. PMID: 23420416
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