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Gene Review

TRB@  -  T cell receptor, beta cluster

Bos taurus

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Disease relevance of TRB@

  • IR spectra were collected for the single-chain (beta-trypsin) and once-cleaved, double-chain (alpha-trypsin) forms as well as at various times during the course of autolysis and also for zymogen, trypsinogen, and beta-trypsin inhibited with diisopropyl fluorophosphate [1].
  • We describe here the high-level expression of bovine trypsinogen in E. coli, its refolding and activation to beta-trypsin, and the selective incorporation of (15)N-labeled alanine through supplementation of the growth medium [2].
  • For all seven protein systems considered (HIV-1 protease, dihydrodipicolinate reductase, Rnase T1, streptavidin, pp60c-Src SH2 domain, Hsp90 molecular chaperone, and bovine beta-trypsin) the binding enthalpy of 25 small molecular weight peptide and nonpeptide ligands can be accounted for with a standard error of +/-0.3 kcal x mol(-1) [3].

High impact information on TRB@

  • The effects of double mutations on k(a), k(lim), and k(app) were small with uPA and nonexistent with beta-trypsin [4].
  • The contribution of a covalent bond to the stability of complexes of serine proteinases with inhibitors of the serpin family was evaluated by comparing the affinities of beta-trypsin and the catalytic serine-modified derivative, beta-anhydrotrypsin, for several serpin and non-serpin (Kunitz) inhibitors [5].
  • Berenil (4,4'-diazoamino-bis-benzamidine), a parabolic competitive inhibitor of beta-trypsin, was a hyperbolic competitive inhibitor of azo-beta-trypsin [6].
  • Identification of the substrate activation site of beta-trypsin by a 1:1 reaction with p-diazoniumbenzamidine chloride was confirmed by spectral analysis [6].
  • The topology of the metal ion binding site in subunit III is predicted from sequence homologies and modeling experiments based on the known crystallographic three-dimensional structures of the equivalent sites in porcine elastase 1 and bovine beta-trypsin [7].

Biological context of TRB@


Anatomical context of TRB@

  • C1 inactivator was hydrolyzed at three different regions on the molecule whereas beta-trypsin cleaved two regions in common with leukocyte elastase [13].

Associations of TRB@ with chemical compounds

  • Transient removal of proflavine inhibition of bovine beta-trypsin by the bovine basic pancreatic trypsin inhibitor (Kunitz). A case for "chronosteric effects" [14].
  • Intact third domains (positions 131 to 186) isolated from the two allelic forms of ovomucoid interact with bovine beta-trypsin in a similar but not identical manner; the complex with the glycine form dissociates more rapidly [15].
  • The high-resolution X-ray structures have been determined for ten complexes formed between bovine beta-trypsin and P1 variants (Gly, Asp, Glu, Gln, Thr, Met, Lys, His, Phe, Trp) of bovine pancreatic trypsin inhibitor (BPTI) [16].
  • Arginine and lysine derivatives are equally good substrates for b. beta-trypsin; b. thrombin and h.u. kallikrein prefer substrates containing arginine side chains; h. urokinase prefers substrate containing lysine [17].
  • 1-(N-Amino-n-hexyl)carbamoylimidazole hydrochloride was synthesized and shown to be a potent irreversible inhibitor of human urokinase (EC, pig kidney-cell plasminogen activator (EC 3.4.21.-), human plasmin (EC and bovine pancreatic beta-trypsin (EC [18].

Enzymatic interactions of TRB@

  • 5. Solutions of aprotinin, modified aprotinin with the Lys15-Ala16 peptide bond cleaved and mixtures of both species were incubated with 10 mol% porcine beta-trypsin [19].

Other interactions of TRB@


Analytical, diagnostic and therapeutic context of TRB@


  1. Comparison of various molecular forms of bovine trypsin: correlation of infrared spectra with X-ray crystal structures. Prestrelski, S.J., Byler, D.M., Liebman, M.N. Biochemistry (1991) [Pubmed]
  2. High-level bacterial expression and 15N-alanine-labeling of bovine trypsin. Application to the study of trypsin-inhibitor complexes and trypsinogen activation by NMR spectroscopy. Peterson, F.C., Gordon, N.C., Gettins, P.G. Biochemistry (2001) [Pubmed]
  3. Structural parameterization of the binding enthalpy of small ligands. Luque, I., Freire, E. Proteins (2002) [Pubmed]
  4. The contribution of the exosite residues of plasminogen activator inhibitor-1 to proteinase inhibition. Ibarra, C.A., Blouse, G.E., Christian, T.D., Shore, J.D. J. Biol. Chem. (2004) [Pubmed]
  5. Role of the catalytic serine in the interactions of serine proteinases with protein inhibitors of the serpin family. Contribution of a covalent interaction to the binding energy of serpin-proteinase complexes. Olson, S.T., Bock, P.E., Kvassman, J., Shore, J.D., Lawrence, D.A., Ginsburg, D., Björk, I. J. Biol. Chem. (1995) [Pubmed]
  6. Tyrosine 151 is part of the substrate activation binding site of bovine trypsin. Identification by covalent labeling with p-diazoniumbenzamidine and kinetic characterization of Tyr-151-(p-benzamidino)-azo-beta-trypsin. Oliveira, M.G., Rogana, E., Rosa, J.C., Reinhold, B.B., Andrade, M.H., Greene, L.J., Mares-Guia, M. J. Biol. Chem. (1993) [Pubmed]
  7. Binding of terbium and of an elastase inhibitor to bovine pancreatic subunit III, an inactive protease E. Chapus, C., Kerfelec, B., Dimicoli, J.L. J. Biol. Chem. (1990) [Pubmed]
  8. The refined crystal structure of bovine beta-trypsin at 1.8 A resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0. Bode, W., Schwager, P. J. Mol. Biol. (1975) [Pubmed]
  9. Ligand-induced changes in the conformational stability of bovine trypsinogen and their implications for the protein function. Bulaj, G., Otlewski, J. J. Mol. Biol. (1995) [Pubmed]
  10. Role of catalytic residues in the formation of a tetrahedral adduct in the acylation reaction of bovine beta-trypsin. A molecular orbital study. Nakagawa, S., Umeyama, H. J. Mol. Biol. (1984) [Pubmed]
  11. Single peptide bond hydrolysis/resynthesis in squash inhibitors of serine proteinases. 1. Kinetics and thermodynamics of the interaction between squash inhibitors and bovine beta-trypsin. Otlewski, J., Zbyryt, T. Biochemistry (1994) [Pubmed]
  12. Alanine point-mutations in the reactive region of bovine pancreatic trypsin inhibitor: effects on the kinetics and thermodynamics of binding to beta-trypsin and alpha-chymotrypsin. Castro, M.J., Anderson, S. Biochemistry (1996) [Pubmed]
  13. Proteolytic cleavage and inactivation of alpha 2-plasmin inhibitor and C1 inactivator by human polymorphonuclear leukocyte elastase. Brower, M.S., Harpel, P.C. J. Biol. Chem. (1982) [Pubmed]
  14. Transient removal of proflavine inhibition of bovine beta-trypsin by the bovine basic pancreatic trypsin inhibitor (Kunitz). A case for "chronosteric effects". Antonini, E., Ascenzi, P., Bolognesi, M., Menegatti, E., Guarneri, M. J. Biol. Chem. (1983) [Pubmed]
  15. A Ser162/Gly162 polymorphism in Japanese quail ovomucoid. Bogard, W.C., Kato, I., Laskowski, M. J. Biol. Chem. (1980) [Pubmed]
  16. The crystal structures of the complexes between bovine beta-trypsin and ten P1 variants of BPTI. Helland, R., Otlewski, J., Sundheim, O., Dadlez, M., Smalås, A.O. J. Mol. Biol. (1999) [Pubmed]
  17. Catalytic properties of serine proteases. 2. Comparison between human urinary kallikrein and human urokinase, bovine beta-trypsin, bovine thrombin, and bovine alpha-chymotrypsin. Ascenzi, P., Menegatti, E., Guarneri, M., Bortolotti, F., Antonini, E. Biochemistry (1982) [Pubmed]
  18. The irreversible inhibition of urokinase, kidney-cell plasminogen activator, plasmin and beta-trypsin by 1-(N-6-amino-n-hexyl)carbamoylimidazole. Walker, B., Elmore, D.T. Biochem. J. (1984) [Pubmed]
  19. The pH dependence of the equilibrium constant KHyd for the hydrolysis of the Lys15-Ala16 reactive-site peptide bond in bovine pancreatic trypsin inhibitor (aprotinin). Siekmann, J., Wenzel, H.R., Matuszak, E., von Goldammer, E., Tschesche, H. J. Protein Chem. (1988) [Pubmed]
  20. Catalytic properties of human urinary kallikrein. Antonini, E., Ascenzi, P., Menegatti, E., Bortolotti, F., Guarneri, M. Biochemistry (1982) [Pubmed]
  21. Modelling of the serine-proteinase fold by X-ray and neutron scattering and sedimentation analyses: occurrence of the fold in factor D of the complement system. Perkins, S.J., Smith, K.F., Kilpatrick, J.M., Volanakis, J.E., Sim, R.B. Biochem. J. (1993) [Pubmed]
  22. The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes. Bode, W., Greyling, H.J., Huber, R., Otlewski, J., Wilusz, T. FEBS Lett. (1989) [Pubmed]
  23. The complete amino acid sequence of bovine cathepsin S and a partial sequence of bovine cathepsin L. Ritonja, A., Colić, A., Dolenc, I., Ogrinc, T., Podobnik, M., Turk, V. FEBS Lett. (1991) [Pubmed]
  24. Binding of porcine pancreatic secretory trypsin inhibitor to bovine beta-trypsin: a kinetic study. Ascenzi, P., Amiconi, G., Bolognesi, M., Menegatti, E., Guarneri, M. Biopolymers (1986) [Pubmed]
  25. The refined crystal structure of bovine beta-trypsin at 1.8 A resolution. I. Crystallization, data collection and application of patterson search technique. Fehlhammer, H., Bode, W. J. Mol. Biol. (1975) [Pubmed]
  26. Active site titration of bovine beta-trypsin by N alpha-(N,N-dimethylcarbamoyl)-alpha-aza-lysine p-nitrophenyl ester: kinetic and crystallographic analysis. Sartori, P., Djinovic Carugo, K., Ferraccioli, R., Balliano, G., Milla, P., Ascenzi, P., Bolognesi, M. FEBS Lett. (1995) [Pubmed]
  27. Autolysis of beta-trypsin at pH 3.0. Dias, C.L., Rogana, E. Braz. J. Med. Biol. Res. (1986) [Pubmed]
  28. Urea-induced denaturation of beta-trypsin: an evidence for a molten globule state. Brumano, M.H., Oliveira, M.G. Protein Pept. Lett. (2004) [Pubmed]
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