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Pathway Description
Tyrosine Biosynthesis
Escherichia coli
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2015-03-15
Last Updated: 2024-09-05
Tyrosine is one of the amino acid used in protein synthesis. The tyrosine biosynthesis pathways is connected with the chorismate biosynthesis pathway. Chorismate biosynthesis produce the chorismate, which can further be converted to prephenate by T-protein. Combined with cofactor, NAD, prephenate has been further converted to 4-Hydroxyphenylpyruvic acid by T-protein with generated NADH and carbon dioxide. Tyrosine aminotransferase catalyzes 4-Hydroxyphenylpyruvic acid to tyrosine, and also converts glutamic acid to oxoglutaric acid. Tyrosine will be further catalyzed into various molecules such as 2-iminoacetate, p-Cresol, 5'Deoxyadenosine and L-Methionine; or it will be exported from cell via the lysine exporter.
References
Tyrosine Biosynthesis References
Gelfand DH, Steinberg RA: Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases. J Bacteriol. 1977 Apr;130(1):429-40.
Pubmed: 15983
Tsirka SA, Sklaviadis TK, Kyriakidis DA: Non-competitive inhibition of ornithine decarboxylase by a phosphopeptide and phosphoamino acids. Biochim Biophys Acta. 1986 Dec 10;884(3):482-9.
Pubmed: 3096379
Kim SC, Min BE, Hwang HG, Seo SW, Jung GY: Pathway optimization by re-design of untranslated regions for L-tyrosine production in Escherichia coli. Sci Rep. 2015 Sep 8;5:13853. doi: 10.1038/srep13853.
Pubmed: 26346938
Hudson GS, Davidson BE: Nucleotide sequence and transcription of the phenylalanine and tyrosine operons of Escherichia coli K12. J Mol Biol. 1984 Dec 25;180(4):1023-51. doi: 10.1016/0022-2836(84)90269-9.
Pubmed: 6396419
Yamamoto Y, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kimura S, Kitagawa M, Makino K, Miki T, Mitsuhashi N, Mizobuchi K, Mori H, Nakade S, Nakamura Y, Nashimoto H, Oshima T, Oyama S, Saito N, Sampei G, Satoh Y, Sivasundaram S, Tagami H, Horiuchi T, et al.: Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features. DNA Res. 1997 Apr 28;4(2):91-113. doi: 10.1093/dnares/4.2.91.
Pubmed: 9205837
Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. doi: 10.1126/science.277.5331.1453.
Pubmed: 9278503
Fotheringham IG, Dacey SA, Taylor PP, Smith TJ, Hunter MG, Finlay ME, Primrose SB, Parker DM, Edwards RM: The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes. Biochem J. 1986 Mar 15;234(3):593-604. doi: 10.1042/bj2340593.
Pubmed: 3521591
Kuramitsu S, Inoue K, Ogawa T, Ogawa H, Kagamiyama H: Aromatic amino acid aminotransferase of Escherichia coli: nucleotide sequence of the tyrB gene. Biochem Biophys Res Commun. 1985 Nov 27;133(1):134-9. doi: 10.1016/0006-291x(85)91851-0.
Pubmed: 3907634
Yang J, Pittard J: Molecular analysis of the regulatory region of the Escherichia coli K-12 tyrB gene. J Bacteriol. 1987 Oct;169(10):4710-5. doi: 10.1128/jb.169.10.4710-4715.1987.
Pubmed: 3308851
Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. doi: 10.1093/dnares/3.3.137.
Pubmed: 8905232
Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. doi: 10.1038/msb4100049. Epub 2006 Feb 21.
Pubmed: 16738553
Vander Horn PB, Backstrom AD, Stewart V, Begley TP: Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in Escherichia coli K-12. J Bacteriol. 1993 Feb;175(4):982-92. doi: 10.1128/jb.175.4.982-992.1993.
Pubmed: 8432721
Blattner FR, Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL: Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes. Nucleic Acids Res. 1993 Nov 25;21(23):5408-17. doi: 10.1093/nar/21.23.5408.
Pubmed: 8265357
Dassa J, Marck C, Boquet PL: The complete nucleotide sequence of the Escherichia coli gene appA reveals significant homology between pH 2.5 acid phosphatase and glucose-1-phosphatase. J Bacteriol. 1990 Sep;172(9):5497-500. doi: 10.1128/jb.172.9.5497-5500.1990.
Pubmed: 2168385
Touati E, Danchin A: The structure of the promoter and amino terminal region of the pH 2.5 acid phosphatase structural gene (appA) of E. coli: a negative control of transcription mediated by cyclic AMP. Biochimie. 1987 Mar;69(3):215-21. doi: 10.1016/0300-9084(87)90045-9.
Pubmed: 3038201
Dassa J, Fsihi H, Marck C, Dion M, Kieffer-Bontemps M, Boquet PL: A new oxygen-regulated operon in Escherichia coli comprises the genes for a putative third cytochrome oxidase and for pH 2.5 acid phosphatase (appA) Mol Gen Genet. 1991 Oct;229(3):341-52. doi: 10.1007/bf00267454.
Pubmed: 1658595
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 SMP0000826
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