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Pathway Description
Tryptophan Metabolism
Escherichia coli
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2015-03-22
Last Updated: 2024-12-22
The biosynthesis of L-tryptophan begins with L-glutamine interacting with a chorismate through a anthranilate synthase which results in a L-glutamic acid, a pyruvic acid, a hydrogen ion and a 2-aminobenzoic acid. The aminobenzoic acid interacts with a phosphoribosyl pyrophosphate through an anthranilate synthase component II resulting in a pyrophosphate and a N-(5-phosphoribosyl)-anthranilate. The latter compound is then metabolized by an indole-3-glycerol phosphate synthase / phosphoribosylanthranilate isomerase resulting in a 1-(o-carboxyphenylamino)-1-deoxyribulose 5'-phosphate. This compound then interacts with a hydrogen ion through a indole-3-glycerol phosphate synthase / phosphoribosylanthranilate isomerase resulting in the release of carbon dioxide, a water molecule and a (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate. The latter compound then interacts with a D-glyceraldehyde 3-phosphate and an Indole. The indole interacts with an L-serine through a tryptophan synthase, β subunit dimer resulting in a water molecule and an L-tryptophan.
The metabolism of L-tryptophan starts with L-tryptophan being dehydrogenated by a tryptophanase / L-cysteine desulfhydrase resulting in the release of a hydrogen ion, an Indole and a 2-aminoacrylic acid. The latter compound is isomerized into a 2-iminopropanoate. This compound then interacts with a water molecule and a hydrogen ion spontaneously resulting in the release of an Ammonium and a pyruvic acid. The pyruvic acid then interacts with a coenzyme A through a NAD driven pyruvate dehydrogenase complex resulting in the release of a NADH, a carbon dioxide and an Acetyl-CoA
References
Tryptophan Metabolism References
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Lane AN, Kirschner K: Mechanism of the physiological reaction catalyzed by tryptophan synthase from Escherichia coli. Biochemistry. 1991 Jan 15;30(2):479-84.
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Yanofsky C: The different roles of tryptophan transfer RNA in regulating trp operon expression in E. coli versus B. subtilis. Trends Genet. 2004 Aug;20(8):367-74. doi: 10.1016/j.tig.2004.06.007.
Pubmed: 15262409
Yanofsky C: RNA-based regulation of genes of tryptophan synthesis and degradation, in bacteria. RNA. 2007 Aug;13(8):1141-54. doi: 10.1261/rna.620507. Epub 2007 Jun 29.
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Pubmed: 1917834
Yanofsky C, Platt T, Crawford IP, Nichols BP, Christie GE, Horowitz H, VanCleemput M, Wu AM: The complete nucleotide sequence of the tryptophan operon of Escherichia coli. Nucleic Acids Res. 1981 Dec 21;9(24):6647-68. doi: 10.1093/nar/9.24.6647.
Pubmed: 7038627
Nichols BP, van Cleemput M, Yanofsky C: Nucleotide sequence of Escherichia coli trpE. Anthranilate synthetase component I contains no tryptophan residues. J Mol Biol. 1981 Feb 15;146(1):45-54. doi: 10.1016/0022-2836(81)90365-x.
Pubmed: 7021857
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Horowitz H, Christie GE, Platt T: Nucleotide sequence of the trpD gene, encoding anthranilate synthetase component II of Escherichia coli. J Mol Biol. 1982 Apr 5;156(2):245-56. doi: 10.1016/0022-2836(82)90326-6.
Pubmed: 6283099
Christie GE, Platt T: Gene structure in the tryptophan operon of Escherichia coli. Nucleotide sequence of trpC and the flanking intercistronic regions. J Mol Biol. 1980 Oct 5;142(4):519-30. doi: 10.1016/0022-2836(80)90261-2.
Pubmed: 7007653
Horowitz H, Van Arsdell J, Platt T: Nucleotide sequence of the trpD and trpC genes of Salmonella typhimurium. J Mol Biol. 1983 Oct 5;169(4):775-97. doi: 10.1016/s0022-2836(83)80136-3.
Pubmed: 6355484
Guest JR, Drapeau GR, Carlton BC, Yanofsky C: The amino acid sequence of the A protein (alpha subunit) of the tryptophan synthetase of Escherichia coli. J Biol Chem. 1967 Nov 25;242(22):5442-6.
Pubmed: 4863752
Nichols BP, Yanofsky C: Nucleotide sequences of trpA of Salmonella typhimurium and Escherichia coli: an evolutionary comparison. Proc Natl Acad Sci U S A. 1979 Oct;76(10):5244-8. doi: 10.1073/pnas.76.10.5244.
Pubmed: 388433
Zhao GP, Somerville RL: Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive "hinge" region diminishes substrate binding and alters solubility. J Biol Chem. 1992 Jan 5;267(1):526-41.
Pubmed: 1309752
Milkman R, Bridges MM: Molecular evolution of the Escherichia coli chromosome. IV. Sequence comparisons. Genetics. 1993 Mar;133(3):455-68.
Pubmed: 8095913
Deeley MC, Yanofsky C: Nucleotide sequence of the structural gene for tryptophanase of Escherichia coli K-12. J Bacteriol. 1981 Sep;147(3):787-96.
Pubmed: 6268608
Tokushige M, Tsujimoto N, Oda T, Honda T, Yumoto N, Ito S, Yamamoto M, Kim EH, Hiragi Y: Role of cysteine residues in tryptophanase for monovalent cation-induced activation. Biochimie. 1989 Jun;71(6):711-20. doi: 10.1016/0300-9084(89)90087-4.
Pubmed: 2502187
Burland V, Plunkett G 3rd, Daniels DL, Blattner FR: DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication. Genomics. 1993 Jun;16(3):551-61. doi: 10.1006/geno.1993.1230.
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Misumi Y, Ogata S, Ohkubo K, Hirose S, Ikehara Y: Primary structure of human placental 5'-nucleotidase and identification of the glycolipid anchor in the mature form. Eur J Biochem. 1990 Aug 17;191(3):563-9. doi: 10.1111/j.1432-1033.1990.tb19158.x.
Pubmed: 2129526
Hansen KR, Resta R, Webb CF, Thompson LF: Isolation and characterization of the promoter of the human 5'-nucleotidase (CD73)-encoding gene. Gene. 1995 Dec 29;167(1-2):307-12. doi: 10.1016/0378-1119(95)00574-9.
Pubmed: 8566797
Knapp K, Zebisch M, Pippel J, El-Tayeb A, Muller CE, Strater N: Crystal structure of the human ecto-5'-nucleotidase (CD73): insights into the regulation of purinergic signaling. Structure. 2012 Dec 5;20(12):2161-73. doi: 10.1016/j.str.2012.10.001. Epub 2012 Nov 8.
Pubmed: 23142347
This pathway was propagated using PathWhiz -
Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.
Propagated from SMP0000835
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