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Gene Review

tnaA  -  tryptophanase

Escherichia coli UTI89

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Disease relevance of tnaA

  • Phylogenetic comparisons suggest that the tna cluster was acquired by intergeneric lateral transfer, either by H. influenzae or a recent ancestor, and that E. coli may have acquired its tnaA gene from a related source [1].
  • Nucleotide sequences in or near lambda prophage homologs were significantly more variable than the sequences in or near trp, tnaA, and thyA genes [2].
  • Characterization of the tryptophanase operon of Proteus vulgaris. Cloning, nucleotide sequence, amino acid homology, and in vitro synthesis of the leader peptide and regulatory analysis [3].
  • In contrast to H. influenzae, most other Haemophilus species lack tna genes [1].
  • Once the strain with a defected tryptophanase gene was obtained, the infection of phage P1 was applied to specifically disrupt the tryptophanase gene of any other strains [4].

High impact information on tnaA

  • The results suggest that indigo formation is due to the combined activities of tryptophanase and naphthalene dioxygenase [5].
  • The mechanism of tryptophan induction of tryptophanase operon expression: tryptophan inhibits release factor-mediated cleavage of TnaC-peptidyl-tRNA(Pro) [6].
  • This ribosome remains stalled at the tna stop codon and blocks the access of Rho factor to the tna transcript, thereby preventing transcription termination [7].
  • In this paper we use an in vitro S-30 cell-free system to analyze the features of tna operon regulation [8].
  • Regulatory studies performed in P. vulgaris, and with a plasmid carrying the P. vulgaris tna operon in E. coli, established that expression of the Proteus operon was induced by tryptophan and was subject to catabolite repression [3].

Chemical compound and disease context of tnaA


Biological context of tnaA

  • A mutant carrying a deletion from bgl through tnaA showed negligible L-tryptophan uptake, in contrast to a strain possessing an intact tna region or to strains carrying point mutations in tna [13].
  • An open reading frame corresponding to the 48-kDa thdF protein was located next to the tnaA gene, which encodes tryptophanase, but was transcribed in the opposite sense [14].
  • The data indicate that substrate-induced conformational changes occur at the enzyme active site that generate a high affinity indole-binding site during catalytic turnover of tryptophanase and are important in the catalytic functioning of the enzyme [10].
  • Virulence against C. elegans required tryptophan and bacterial tryptophanase, the enzyme catalysing the production of indole and other molecules from tryptophan [15].
  • We have identified tryptophanase (which catabolizes tryptophan to pyruvate and indole) as an Rcd binding protein [16].

Anatomical context of tnaA

  • In the present study we use a tnaC-UGA-'lacZ construct lacking the tnaC-tnaA spacer region to analyze the effect of TnaC synthesis on the behavior of the ribosome that translates tnaC [17].
  • The complementation of the tnaA mutant with plasmid-located wild-type tnaA restored the tryptophanase activity, epithelial cells adherence, and biofilm formation on polystyrene [18].

Associations of tnaA with chemical compounds

  • Thus, the lambda-homologous regions may have a significant horizontal component in their evolutionary histories, having undergone genetic exchange, whereas the trp, tnaA, and thyA regions may have solely vertical evolutionary histories [2].
  • Some effects of indole on the interaction of amino acids with tryptophanase [10].
  • The pyridoxal phosphate-dependent enzyme tryptophanase has been investigated using 31P nuclear magnetic resonance at 72.86 MHz [19].
  • Oxindolyl-L-alanine and 2,3-dihydro-L-tryptophan, which are analogs of a proposed reaction intermediate, are potent competitive inhibitors of both tryptophanase and the alpha 2 beta 2 complex of tryptophan synthase (Phillips, R. S., Miles, E. W., and Cohen, L. A. (1984) Biochemistry 23, 6228-6234) [20].
  • Addition of the competitive inhibitor, L-alanine, to tryptophanase produces the quinonoid intermediate [19].

Analytical, diagnostic and therapeutic context of tnaA


  1. The tryptophanase gene cluster of Haemophilus influenzae type b: evidence for horizontal gene transfer. Martin, K., Morlin, G., Smith, A., Nordyke, A., Eisenstark, A., Golomb, M. J. Bacteriol. (1998) [Pubmed]
  2. Conservation and variation of nucleotide sequences in Escherichia coli strains isolated from nature. Harshman, L., Riley, M. J. Bacteriol. (1980) [Pubmed]
  3. Characterization of the tryptophanase operon of Proteus vulgaris. Cloning, nucleotide sequence, amino acid homology, and in vitro synthesis of the leader peptide and regulatory analysis. Kamath, A.V., Yanofsky, C. J. Biol. Chem. (1992) [Pubmed]
  4. Disruption of targeted gene in bacterial chromosome by using a temperature-sensitive plasmid. Chan, E.C. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  5. Expression of naphthalene oxidation genes in Escherichia coli results in the biosynthesis of indigo. Ensley, B.D., Ratzkin, B.J., Osslund, T.D., Simon, M.J., Wackett, L.P., Gibson, D.T. Science (1983) [Pubmed]
  6. The mechanism of tryptophan induction of tryptophanase operon expression: tryptophan inhibits release factor-mediated cleavage of TnaC-peptidyl-tRNA(Pro). Gong, F., Ito, K., Nakamura, Y., Yanofsky, C. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  7. Analysis of tryptophanase operon expression in vitro: accumulation of TnaC-peptidyl-tRNA in a release factor 2-depleted S-30 extract prevents Rho factor action, simulating induction. Gong, F., Yanofsky, C. J. Biol. Chem. (2002) [Pubmed]
  8. Reproducing tna operon regulation in vitro in an S-30 system. Tryptophan induction inhibits cleavage of TnaC peptidyl-tRNA. Gong, F., Yanofsky, C. J. Biol. Chem. (2001) [Pubmed]
  9. 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]
  10. Some effects of indole on the interaction of amino acids with tryptophanase. Kazarinoff, M.N., Snell, E.E. J. Biol. Chem. (1980) [Pubmed]
  11. Structural and functional interdependence of the protomers of Escherichia coli K 12 tryptophanase during binding of pyridoxal 5'-phosphate. Raibaud, O., Goldberg, M.E. J. Biol. Chem. (1976) [Pubmed]
  12. Replacement of lysine 269 by arginine in Escherichia coli tryptophan indole-lyase affects the formation and breakdown of quinonoid complexes. Phillips, R.S., Richter, I., Gollnick, P., Brzovic, P., Dunn, M.F. J. Biol. Chem. (1991) [Pubmed]
  13. Location of the gene for the low-affinity tryptophan-specific permease of Escherichia coli. Edwards, R.M., Yudkin, M.D. Biochem. J. (1982) [Pubmed]
  14. Molecular cloning and sequence of the thdF gene, which is involved in thiophene and furan oxidation by Escherichia coli. Alam, K.Y., Clark, D.P. J. Bacteriol. (1991) [Pubmed]
  15. Paralysis and killing of Caenorhabditis elegans by enteropathogenic Escherichia coli requires the bacterial tryptophanase gene. Anyanful, A., Dolan-Livengood, J.M., Lewis, T., Sheth, S., Dezalia, M.N., Sherman, M.A., Kalman, L.V., Benian, G.M., Kalman, D. Mol. Microbiol. (2005) [Pubmed]
  16. Indole signalling contributes to the stable maintenance of Escherichia coli multicopy plasmids. Chant, E.L., Summers, D.K. Mol. Microbiol. (2007) [Pubmed]
  17. Regulation of the Escherichia coli tna operon: nascent leader peptide control at the tnaC stop codon. Konan, K.V., Yanofsky, C. J. Bacteriol. (1997) [Pubmed]
  18. Isolation of an Escherichia coil strain mutant unable to form biofilm on polystyrene and to adhere to human pneumocyte cells: involvement of tryptophanase. Di Martino, P., Merieau, A., Phillips, R., Orange, N., Hulen, C. Can. J. Microbiol. (2002) [Pubmed]
  19. Phosphorus 31 nuclear magnetic resonance study of tryptophanase. Pyridoxal phosphate-binding site. Schnackerz, K.D., Snell, E.E. J. Biol. Chem. (1983) [Pubmed]
  20. Differential inhibition of tryptophan synthase and of tryptophanase by the two diastereoisomers of 2,3-dihydro-L-tryptophan. Implications for the stereochemistry of the reaction intermediates. Phillips, R.S., Miles, E.W., Cohen, L.A. J. Biol. Chem. (1985) [Pubmed]
  21. Evidence that cysteine 298 is in the active site of tryptophan indole-lyase. Phillips, R.S., Gollnick, P.D. J. Biol. Chem. (1989) [Pubmed]
  22. Cloning, nucleotide sequences, and overexpression in Escherichia coli of tandem copies of a tryptophanase gene in an obligately symbiotic thermophile, Symbiobacterium thermophilum. Hirahara, T., Suzuki, S., Horinouchi, S., Beppu, T. Appl. Environ. Microbiol. (1992) [Pubmed]
  23. Immobilized derivative of pyridoxal 5'-phosphate. Application to affinity chromatography of tryptophanase and tyrosine phenol-lyase. Ikeda, A., Hara, H., Sugimoto, S., Fukui, S. FEBS Lett. (1975) [Pubmed]
  24. Conformational changes in the active site of tryptophanase revealed by the circular dichroism method. Zakomirdina, L.N., Sakharova, I.S., Torchinsky, Y.M. Biochimie (1989) [Pubmed]
  25. Rapid assay for tryptophanase using reversed-phase high-performance liquid chromatography. Krstulovic, A.M., Matzura, C. J. Chromatogr. (1979) [Pubmed]
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