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Chemical Compound Review

tryptophanate     2-amino-3-(1H-indol-3- yl)propanoate

Synonyms: AC1MJET2, trp(-), CHEBI:32727, AKOS002936196, BAS 00102771, ...
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Disease relevance of tryptacin


High impact information on tryptacin

  • Contrary to current models of excitation and TRP channel function, we demonstrate that the transient phenotype of trp mutants can be explained by CAM regulation of the TRPL channel rather than by the loss of a store-operated conductance leading to depletion of the internal stores [6].
  • Expression in COS cells of two full-length cDNAs encoding human trp homologs, Htrp1 and Htrp3, increased CCE [7].
  • Studies on visual signal transduction in Drosophila led to the hypothesis that a protein encoded in trp may be a component of CCE channels [7].
  • DNA recognition by lac repressor and catabolite activator protein is greatly stimulated, while specific aroH DNA recognition by trp repressor is inhibited [8].
  • The DNA sequence at tL shows striking homologies with trp t', a terminator also strongly affected in vitro by the nusA protein [9].

Chemical compound and disease context of tryptacin


Biological context of tryptacin

  • Because the desamino analogues thus cause derepression of operons under control of the trp repressor, they appear to be 'inducers'. We have determined the crystal structure of the pseudorepressor and refined it to 1.65 A [15].
  • Determinants of repressor/operator recognition from the structure of the trp operator binding site [16].
  • The tandem complex model accounts for the mutational sensitivity of all trp operator base pairs [17].
  • Here we present the high-resolution crystal structure of the trp operator region that is most important in the recognition process [16].
  • The methylation protection assay shows that Trp repressor binds in two successive major grooves of the trpR operator, three successive major grooves of the aroH operator, and four successive major grooves of the trp operator [18].

Anatomical context of tryptacin

  • Abolishing Ca2+ influx in wild-type photoreceptors mimicked inactivation, while raising Ca2+ by blocking Na+/Ca2+ exchange prevented inactivation in trp [19].
  • This and the possibility that trp leader RNA is translated suggest a model for regulation of transcription termination that is based on ribosome movement along the RNA and a shift between alternative RNA base-pairing configuration [20].
  • Human PDI was expressed to the Escherichia coli periplasm, by using a plasmid encoded ompA-PDI fusion under the control of the trp promoter [21].
  • The product expressed from the trp promoter system had high antiviral activity and displayed biological effects similar to those of Namalwa interferon on natural killer cell activity and in a Daudi cell growth inhibition assay [22].
  • Isolation, cloning, and characterisation of a trp homologue from squid (Loligo forbesi) photoreceptor membranes [23].

Associations of tryptacin with other chemical compounds

  • As well as being a major charge carrier for the light-induced current, Ca2+ influx via the trp-dependent channels appears to be required for refilling Ca2+ stores sensitive to inositol 1,4,5-trisphosphate and for feedback regulation (light adaptation) of the transduction cascade [24].
  • An atomic view of the L-tryptophan binding site of trp repressor [25].
  • Alternative secondary structures of leader RNAs and the regulation of the trp, phe, his, thr, and leu operons [11].
  • The lesion was shown by DNA sequencing to be a G to C transversion at nucleotide 5528 of the trp operon, resulting in a Gly to Arg switch at codon 281 [26].
  • Analysis of the trp cage peptides by circular dichroism and NMR indicated that the structure and stability of the trp cage miniprotein was controllable based on the conformational bias of the proline derivative [27].

Gene context of tryptacin

  • To explain the residual photoresponse that remains in the trp mutant, a third TRP-related subunit has previously been proposed to function with TRPL [28].
  • We report that anti-INAD antibodies coimmunoprecipitate TRP, identified by its electrophoretic mobility, cross reactivity with anti-TRP antibody, and absence in a null allele trp mutant [29].
  • Whole-cell recordings revealed that light-sensitive Ca2+ channels encoded by the trp gene were constitutively active in rdgA photoreceptors [30].
  • The trp (transient receptor potential) gene encodes a Ca2+ channel responsible for the major component of the phospholipase C (PLC) mediated light response in Drosophila [19].
  • Nucleotide sequence and expression of Escherichia coli trpR, the structural gene for the trp aporepressor [31].

Analytical, diagnostic and therapeutic context of tryptacin


  1. Frameshifting in the expression of the E. coli trpR gene occurs by the bypassing of a segment of its coding sequence. Benhar, I., Engelberg-Kulka, H. Cell (1993) [Pubmed]
  2. The regulatory region of the trp operon of Serratia marcescens. Miozzari, G.F., Yanofsky, C. Nature (1978) [Pubmed]
  3. DNA specificity determinants of Escherichia coli tryptophan repressor binding. Bass, S., Sugiono, P., Arvidson, D.N., Gunsalus, R.P., Youderian, P. Genes Dev. (1987) [Pubmed]
  4. New insights into regulation of the tryptophan biosynthetic operon in Gram-positive bacteria. Gutierrez-Preciado, A., Jensen, R.A., Yanofsky, C., Merino, E. Trends Genet. (2005) [Pubmed]
  5. Dissecting independent channel and scaffolding roles of the Drosophila transient receptor potential channel. Wang, T., Jiao, Y., Montell, C. J. Cell Biol. (2005) [Pubmed]
  6. Calmodulin regulation of Drosophila light-activated channels and receptor function mediates termination of the light response in vivo. Scott, K., Sun, Y., Beckingham, K., Zuker, C.S. Cell (1997) [Pubmed]
  7. trp, a novel mammalian gene family essential for agonist-activated capacitative Ca2+ entry. Zhu, X., Jiang, M., Peyton, M., Boulay, G., Hurst, R., Stefani, E., Birnbaumer, L. Cell (1996) [Pubmed]
  8. DNA dynamic flexibility and protein recognition: differential stimulation by bacterial histone-like protein HU. Flashner, Y., Gralla, J.D. Cell (1988) [Pubmed]
  9. Pausing and attenuation of in vitro transcription in the rrnB operon of E. coli. Kingston, R.E., Chamberlin, M.J. Cell (1981) [Pubmed]
  10. Complexity in regulation of tryptophan biosynthesis in Bacillus subtilis. Gollnick, P., Babitzke, P., Antson, A., Yanofsky, C. Annu. Rev. Genet. (2005) [Pubmed]
  11. Alternative secondary structures of leader RNAs and the regulation of the trp, phe, his, thr, and leu operons. Keller, E.B., Calvo, J.M. Proc. Natl. Acad. Sci. U.S.A. (1979) [Pubmed]
  12. Folding and stability of trp aporepressor from Escherichia coli. Gittelman, M.S., Matthews, C.R. Biochemistry (1990) [Pubmed]
  13. Mutagenicity of nitrosated alpha-amino acid derivatives N-acetyl-N'-nitrosotryptophan and its methyl ester in bacteria. Venitt, S., Crofton-Sleigh, C., Ooi, S.L., Bonnett, R. Carcinogenesis (1980) [Pubmed]
  14. Structure and stability of an early folding intermediate of Escherichia coli trp aporepressor measured by far-UV stopped-flow circular dichroism and 8-anilino-1-naphthalene sulfonate binding. Mann, C.J., Matthews, C.R. Biochemistry (1993) [Pubmed]
  15. The structure of trp pseudorepressor at 1.65A shows why indole propionate acts as a trp 'inducer'. Lawson, C.L., Sigler, P.B. Nature (1988) [Pubmed]
  16. Determinants of repressor/operator recognition from the structure of the trp operator binding site. Shakked, Z., Guzikevich-Guerstein, G., Frolow, F., Rabinovich, D., Joachimiak, A., Sigler, P.B. Nature (1994) [Pubmed]
  17. Tandem binding in crystals of a trp repressor/operator half-site complex. Lawson, C.L., Carey, J. Nature (1993) [Pubmed]
  18. Escherichia coli tryptophan repressor binds multiple sites within the aroH and trp operators. Kumamoto, A.A., Miller, W.G., Gunsalus, R.P. Genes Dev. (1987) [Pubmed]
  19. Calcium influx via TRP channels is required to maintain PIP2 levels in Drosophila photoreceptors. Hardie, R.C., Raghu, P., Moore, S., Juusola, M., Baines, R.A., Sweeney, S.T. Neuron (2001) [Pubmed]
  20. Transcription termination at the trp operon attenuators of Escherichia coli and Salmonella typhimurium: RNA secondary structure and regulation of termination. Lee, F., Yanofsky, C. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
  21. Human protein disulfide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coli. Humphreys, D.P., Weir, N., Mountain, A., Lund, P.A. J. Biol. Chem. (1995) [Pubmed]
  22. Chemical synthesis of a human interferon-alpha 2 gene and its expression in Escherichia coli. Edge, M.D., Greene, A.R., Heathcliffe, G.R., Moore, V.E., Faulkner, N.J., Camble, R., Petter, N.N., Trueman, P., Schuch, W., Hennam, J. Nucleic Acids Res. (1983) [Pubmed]
  23. Isolation, cloning, and characterisation of a trp homologue from squid (Loligo forbesi) photoreceptor membranes. Monk, P.D., Carne, A., Liu, S.H., Ford, J.W., Keen, J.N., Findlay, J.B. J. Neurochem. (1996) [Pubmed]
  24. Novel Ca2+ channels underlying transduction in Drosophila photoreceptors: implications for phosphoinositide-mediated Ca2+ mobilization. Hardie, R.C., Minke, B. Trends Neurosci. (1993) [Pubmed]
  25. An atomic view of the L-tryptophan binding site of trp repressor. Lawson, C.L. Nat. Struct. Biol. (1996) [Pubmed]
  26. 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. Zhao, G.P., Somerville, R.L. J. Biol. Chem. (1992) [Pubmed]
  27. Stereoelectronic tuning of the structure and stability of the trp cage miniprotein. Naduthambi, D., Zondlo, N.J. J. Am. Chem. Soc. (2006) [Pubmed]
  28. TRPgamma, a drosophila TRP-related subunit, forms a regulated cation channel with TRPL. Xu, X.Z., Chien, F., Butler, A., Salkoff, L., Montell, C. Neuron (2000) [Pubmed]
  29. Regulation of the TRP Ca2+ channel by INAD in Drosophila photoreceptors. Shieh, B.H., Zhu, M.Y. Neuron (1996) [Pubmed]
  30. Constitutive activity of the light-sensitive channels TRP and TRPL in the Drosophila diacylglycerol kinase mutant, rdgA. Raghu, P., Usher, K., Jonas, S., Chyb, S., Polyanovsky, A., Hardie, R.C. Neuron (2000) [Pubmed]
  31. Nucleotide sequence and expression of Escherichia coli trpR, the structural gene for the trp aporepressor. Gunsalus, R.P., Yanofsky, C. Proc. Natl. Acad. Sci. U.S.A. (1980) [Pubmed]
  32. MtrB from Bacillus subtilis binds specifically to trp leader RNA in a tryptophan-dependent manner. Otridge, J., Gollnick, P. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  33. The trp RNA-binding attenuation protein (TRAP) from Bacillus subtilis binds to unstacked trp leader RNA. Baumann, C., Xirasagar, S., Gollnick, P. J. Biol. Chem. (1997) [Pubmed]
  34. Characterization of a Ca2+ release-activated nonselective cation current regulating membrane potential and [Ca2+]i oscillations in transgenically derived beta-cells. Roe, M.W., Worley, J.F., Qian, F., Tamarina, N., Mittal, A.A., Dralyuk, F., Blair, N.T., Mertz, R.J., Philipson, L.H., Dukes, I.D. J. Biol. Chem. (1998) [Pubmed]
  35. Ligand-mediated conformational changes in Trp repressor protein of Escherichia coli probed through limited proteolysis and the use of specific antibodies. Tsapakos, M.J., Haydock, P.V., Hermodson, M., Somerville, R.L. J. Biol. Chem. (1985) [Pubmed]
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