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Gene Review

trpA  -  tryptophan synthase subunit alpha

Escherichia coli UTI89

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Disease relevance of trpA


High impact information on trpA


Chemical compound and disease context of trpA


Biological context of trpA

  • The mutagenized fragments were subcloned into the plasmid vector and used to transform to ampicillin resistance (Ampr) a recipient strain containing a UGA mutation in trpA [11].
  • There was a dense pattern of reversion sites within the trpA DNA region where reversion events could occur, suggesting that, in general, most DNA sequences are capable of undergoing spontaneous mutational events during replication that can lead to small deletions and insertions [2].
  • These studies also revealed an unpredicted flexibility in the primary amino acid sequence of the trpA product, the alpha subunit of tryptophan synthase [2].
  • The molecular characterization of the mutation that corrected the Eut- phenotype caused by allele Delta903 showed that the new mutation was a deletion of two nucleotides at the tonB-trpA fusion site [12].
  • In order to elucidate the effect of single amino acid substitutions on the conformation of the tryptophan synthase alpha-subunit from Escherichia coli in solution, 1H NMR spectra of the wild-type and mutant proteins were measured at various pHs [13].

Associations of trpA with chemical compounds


Analytical, diagnostic and therapeutic context of trpA


  1. Mutant 16S ribosomal RNA: a codon-specific translational suppressor. Murgola, E.J., Hijazi, K.A., Göringer, H.U., Dahlberg, A.E. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  2. A molecular characterization of spontaneous frameshift mutagenesis within the trpA gene of Escherichia coli. Hardin, A., Villalta, C.F., Doan, M., Jabri, M., Chockalingham, V., White, S.J., Fowler, R.G. DNA Repair (Amst.) (2007) [Pubmed]
  3. Unfolding properties of tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase. Choi, S.G., Hardman, J.K. J. Biol. Chem. (1995) [Pubmed]
  4. Evidence that glutamic acid 49 of tryptophan synthase alpha subunit is a catalytic residue. Inactive mutant proteins substituted at position 49 bind ligands and transmit ligand-dependent to the beta subunit. Miles, E.W., McPhie, P., Yutani, K. J. Biol. Chem. (1988) [Pubmed]
  5. Yeast gene TRP5: structure, function, regulation. Zalkin, H., Yanofsky, C. J. Biol. Chem. (1982) [Pubmed]
  6. Unfolding-refolding kinetics of the tryptophan synthase alpha subunit by CD and fluorescence measurements. Ogasahara, K., Yutani, K. J. Mol. Biol. (1994) [Pubmed]
  7. Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone. Nishio, K., Morimoto, Y., Ishizuka, M., Ogasahara, K., Tsukihara, T., Yutani, K. Biochemistry (2005) [Pubmed]
  8. Photoaffinity labeling of the indole sites on the Escherichia coli tryptophan synthase alpha-subunit. Brock, P.W., Myers, R., Baker, D.C., Hardman, J.K. Arch. Biochem. Biophys. (1983) [Pubmed]
  9. Fluorescence and folding properties of Tyr mutant tryptophan synthase alpha-subunits from Escherichia coli. Jeong, J.K., Shin, H.J., Kim, J.W., Lee, C.H., Kim, H.D., Lim, W.K. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  10. Comparison of denaturation by guanidine hydrochloride of the wild type tryptophan synthase alpha-subunit of Escherichia coli and two mutant protein (Glu 49 replaced by Met or Gln). Yutani, K., Ogasahara, K., Suzuki, M., Sugino, Y. J. Biochem. (1979) [Pubmed]
  11. Mutations at three sites in the Escherichia coli 23S ribosomal RNA binding region for protein L11 cause UGA-specific suppression and conditional lethality. Murgola, E.J., Xu, W., Arkov, A.L. Nucleic Acids Symp. Ser. (1995) [Pubmed]
  12. Molecular characterization of eutF mutants of Salmonella typhimurium LT2 identifies eutF lesions as partial-loss-of-function tonB alleles. Thomas, M.G., O'Toole, G.A., Escalante-Semerena, J.C. J. Bacteriol. (1999) [Pubmed]
  13. Proton nuclear magnetic resonance studies on the wild-type and single amino acid substituted tryptophan synthase alpha-subunits. Yutani, K., Akutsu, H., Ogasahara, K., Tsujita, T., Kyogoku, Y. Biochemistry (1987) [Pubmed]
  14. Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit. Ogasahara, K., Yutani, K. Biochemistry (1997) [Pubmed]
  15. Role of conserved proline residues in stabilizing tryptophan synthase alpha subunit: analysis by mutants with alanine or glycine. Yutani, K., Hayashi, S., Sugisaki, Y., Ogasahara, K. Proteins (1991) [Pubmed]
  16. Arabidopsis thaliana tryptophan synthase alpha: gene cloning, expression, and subunit interaction. Radwanski, E.R., Zhao, J., Last, R.L. Mol. Gen. Genet. (1995) [Pubmed]
  17. Assignment of tyrosine resonances in the 1H-NMR spectrum of tryptophan synthase alpha-subunit. Monitoring conformational changes due to substitutions at position 49. Sawada, S., Akutsu, H., Ogasahara, K., Yutani, K. Eur. J. Biochem. (1990) [Pubmed]
  18. Comparison of denaturation of tryptophan synthase alpha-subunits from Escherichia coli, Salmonella typhimurium, and an interspecies hybrid. Yutani, K., Sato, T., Ogasahara, K., Miles, E.W. Arch. Biochem. Biophys. (1984) [Pubmed]
  19. Further examination of the intermediate state in the denaturation of the tryptophan synthase alpha subunit. Evidence that the equilibrium denaturation intermediate is a molten globule. Ogasahara, K., Matsushita, E., Yutani, K. J. Mol. Biol. (1993) [Pubmed]
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