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Gene Review

tnaA  -  tryptophanase

Escherichia coli CFT073

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Disease relevance of tnaA

  • When a tnaA-disrupted E. coli strain expressing the altered cysE gene was transformed with a plasmid carrying the bcr gene, the transformant exhibited more L-cysteine production than cells carrying the vector only [1].
  • The structure shares the same fold with and has similar quaternary structure to Proteus vulgaris tryptophanase and tyrosine-phenol lyase, but is found in a closed conformation when compared with these two enzymes [2].

High impact information on tnaA

  • Apo- and holoenzyme are inactivated at the same rate, and inactivation of both is correlated with modification of 2 arginine residues/tryptophanase monomer [3].
  • Tryptophanase from Escherichia coli B/1t7-A is inactivated by the arginine-specific reagent, phenylglyoxal, in potassium phosphate buffer at pH 7.8 AND 25 degrees [3].
  • We have identified tryptophanase (which catabolizes tryptophan to pyruvate and indole) as an Rcd binding protein [4].
  • Furthermore, the stabilization of multicopy plasmids by Rcd is shown to be tryptophanase dependent, and a tryptophanase-deficient strain is resistant to growth inhibition by Rcd overexpression [4].
  • Kinetics of tryptophanase inactivation/activation by sudden removal/addition of potassium ions with the aid of a crown ether or cryptand [5].

Chemical compound and disease context of tnaA


Biological context of tnaA

  • Portions of the genomes (including the tnaA and thyA genes, the trp operon, and one other unassigned segment) appear to have evolved in concert with the genome as a whole [9].
  • The tryptophanase structure, solved in its apo form, does not have covalent PLP bound in the active site, but two sulfate ions [2].

Associations of tnaA with chemical compounds


Other interactions of tnaA


  1. Effect of drug transporter genes on cysteine export and overproduction in Escherichia coli. Yamada, S., Awano, N., Inubushi, K., Maeda, E., Nakamori, S., Nishino, K., Yamaguchi, A., Takagi, H. Appl. Environ. Microbiol. (2006) [Pubmed]
  2. Structure of Escherichia coli tryptophanase. Ku, S.Y., Yip, P., Howell, P.L. Acta Crystallogr. D Biol. Crystallogr. (2006) [Pubmed]
  3. Essential arginine residues in tryptophanase from Escherichia coli. Kazarinoff, M.N., Snell, E.E. J. Biol. Chem. (1977) [Pubmed]
  4. Indole signalling contributes to the stable maintenance of Escherichia coli multicopy plasmids. Chant, E.L., Summers, D.K. Mol. Microbiol. (2007) [Pubmed]
  5. Kinetics of tryptophanase inactivation/activation by sudden removal/addition of potassium ions with the aid of a crown ether or cryptand. Behbahani-Nejad, I., Suelter, C.H., Dye, J.L. Curr. Top. Cell. Regul. (1984) [Pubmed]
  6. Unstable mutations that relieve catabolite repression of tryptophanase synthesis by Escherichia coli. Yudkin, M.D. J. Bacteriol. (1977) [Pubmed]
  7. Immunochemical studies on the evolution of tryptophanase and the two subunits of tryptophan synthetase of Escherichia coli K 12. Chaffotte, A.F., Zakin, M.M., Goldberg, M.E. Biochem. Biophys. Res. Commun. (1980) [Pubmed]
  8. Protein expression in Escherichia coli S17-1 biofilms: impact of indole. Collet, A., Vilain, S., Cosette, P., Junter, G.A., Jouenne, T., Phillips, R.S., Di Martino, P. Antonie Van Leeuwenhoek (2007) [Pubmed]
  9. Conservation and variation of nucleotide sequences within related bacterial genomes: enterobacteria. Riley, M., Anilionis, A. J. Bacteriol. (1980) [Pubmed]
  10. Modulation of gene expression by drugs affecting deoxyribonucleic acid gyrase. Sanzey, B. J. Bacteriol. (1979) [Pubmed]
  11. Sequence studies on D-serine dehydratase of Escherichia coli. Primary structure of the tryptic phosphopyridoxyl peptide and of the N-terminus. Schiltz, E., Schnackerz, K.D. Eur. J. Biochem. (1976) [Pubmed]
  12. Effect of cyclic adenosine-3',5'-monophosphate on the simultaneous synthesis of beta-galactosidase and tryptophanase in Escherichia coli. Pavlasová, E., Stejskalová, E., Novotný, C., Sikyta, B. Folia Microbiol. (Praha) (1980) [Pubmed]
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