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Chemical Compound Review

AC1L97VW     benzylN-[(1S)-4- (diaminomethylideneamino)...

Synonyms: 136132-67-7
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High impact information on C02334

  • SmCL1 exhibited only a low affinity for the cathepsin B diagnostic substrate Z-Arg-Arg-NHMec while SmCL2 failed to cleave this substrate [1].
  • The kinetic rate of Z-Arg-Arg-NHMec conversion was monitored and the assay optimized for enzyme stability, cell viability and sensitivity [2].
  • Cys and N-AcCys also inhibited the fragmentation of histone H4 by CB and their concentration-dependent inhibitory profiles were qualitatively similar to those observed with Z-Arg-Arg-NHMec [3].
  • The enzyme hydrolyses a wide range of peptide substrates characteristic of chymotrypsin-like, trypsin-like, peptidylglutamylpeptide-hydrolysing activities determined by fluorogenic peptides, Z-Gly-Gly-Leu-NHMec, Z-Arg-Arg-NHMec and Z-Leu-Leu-Glu-beta NA, respectively [4].
  • The specific substrates for cathepsin B (Z-Arg-Arg-NHMec) and cathepsin H (Arg-NHMec) were not hydrolysed by trypanopain-Tc under the conditions tested [5].

Biological context of C02334


Associations of C02334 with other chemical compounds

  • Both the secreted cathepsin L from adult fluke and the 29-kDa proteolytic activity of NEJ ES show a common pH optimum of 7.5, a cysteine protease inhibition profile, and preference for the N-benzyloxycarbonyl (Z)-Phe-Arg-NHMec fluorogenic substrate over Z-Arg-Arg-NHMec and Z-Arg-NHMec [7].

Gene context of C02334

  • The two-chain and single-chain forms of ox cathepsin B were separated by ion exchange chromatography and shown to have similar catalytic activities against the substrates Z-Phe-Arg-4-methyl-7-coumarylamide (Z-Phe-Arg-NHMec) and Z-Arg-Arg-NHMec and rates of inhibition by L-3-carboxy-trans-2,3-epoxypropionyl-leucylamido-(4- guanidino)butane (E-64) [8].


  1. Molecular modeling and substrate specificity of discrete cruzipain-like and cathepsin L-like cysteine proteinases of the human blood fluke Schistosoma mansoni. Brady, C.P., Brinkworth, R.I., Dalton, J.P., Dowd, A.J., Verity, C.K., Brindley, P.J. Arch. Biochem. Biophys. (2000) [Pubmed]
  2. Exocytosis of active cathepsin B enzyme activity at pH 7.0, inhibition and molecular mass. Linebaugh, B.E., Sameni, M., Day, N.A., Sloane, B.F., Keppler, D. Eur. J. Biochem. (1999) [Pubmed]
  3. Regulation of cathepsin B activity by cysteine and related thiols. Krepela, E., Procházka, J., Kárová, B. Biol. Chem. (1999) [Pubmed]
  4. Characterization of a multicatalytic proteinase complex (20S proteasome) from Trypanosoma brucei brucei. Lomo, P.O., Coetzer, T.H., Lonsdale-Eccles, J.D. Immunopharmacology (1997) [Pubmed]
  5. Characterisation of a cysteine protease from bloodstream forms of Trypanosoma congolense. Mbawa, Z.R., Gumm, I.D., Shaw, E., Lonsdale-Eccles, J.D. Eur. J. Biochem. (1992) [Pubmed]
  6. Endopeptidase variations among different life-cycle stages of African trypanosomes. Mbawa, Z.R., Gumm, I.D., Fish, W.R., Lonsdale-Eccles, J.D. Eur. J. Biochem. (1991) [Pubmed]
  7. Fasciola hepatica: characterization and cloning of the major cathepsin B protease secreted by newly excysted juvenile liver fluke. Wilson, L.R., Good, R.T., Panaccio, M., Wijffels, G.L., Sandeman, R.M., Spithill, T.W. Exp. Parasitol. (1998) [Pubmed]
  8. Species variations amongst lysosomal cysteine proteinases. Mason, R.W. Biomed. Biochim. Acta (1986) [Pubmed]
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