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Chemical Compound Review

Zfrn-mec     benzyl N-[(1S)-1-[[(2S)-5...

Synonyms: AC1L2O5T, 65147-22-0, Cbz-phe-arg-mca, Z-Phe-arg-4-nmec
 
 
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High impact information on Cbz-phe-arg-mca

  • However, the presence of a bulky hydrophobic residue at the P2 position (Z-Phe-Arg-AMC, Km = 13.3 mM, and Z-Ile-Leu-Val-Arg-AMC, Km = 24.7 mM) greatly decreased the rate of substrate hydrolysis [1].
  • It does, however, hydrolyse Z-Phe-Arg-AMC, a substrate typically cleaved by cathepsin L and B enzymes [2].
  • Although papain-like enzymes are strongly inhibited by their natural tight-binding inhibitors of the cystatin superfamily, cathepsins B and L may still retain some residual proteolytic activity toward Z-Phe-Arg-AMC in the presence of an excess of kininogen [3].
  • TEX proteases readily cleaved the cathepsin L- and B-specific peptide substrate Z-Phe-Arg-AMC and to a lesser extent, the cathepsin B-specific peptide Z-Arg-Arg-AMC [4].
  • Cell line-specific pH profiles of these cysteine proteinases were determined fluorometrically with benzyloxycarbonyl-phenylalanyl-arginine-amidomethylcoumarine (Z-Phe-Arg-AMC) under saturated conditions [5].
 

Biological context of Cbz-phe-arg-mca

 

Associations of Cbz-phe-arg-mca with other chemical compounds

  • In a series of pairs of lung tumor tissue and non-tumor lung parenchyma from 50 patients, the activity of cathepsin L was measured with Z-Phe-Arg-AMC using the inhibitor CA-074 to delimitate from cathepsin B activity also present in the tissue extracts [7].
 

Gene context of Cbz-phe-arg-mca

  • Short stumpy trypanosomes hydrolyse z-Phe-Arg-AMC 12 fold more actively than either long slenders or procyclics [8].
  • 5. In this work, seven fluorescent, internally quenched, decapeptides have been synthesized using the prototypical cathepsin B selective substrate Z-Phe-Arg-AMC as a lead, and used to identify the structural factors determining the susceptibility of peptides to hydrolysis at acidic and neutral pH values [9].
  • This 24-kDa recombinant protein exhibited a substrate preference for Z-Phe-Arg-AMC (benzyloxycarbonyl-L-phenylalanyl-L-arginine-7-amino-4-methyl-coumarin) compared with Z-Arg-Arg-AMC, and the activity was inhibited by E-64 (L-trans-epoxysuccinylleucylamido(4-quanidino)butane) [10].
  • Cathepsins B and L were measured with the aid of fluorometry, and 7-amido-4-methylocoumarin derivates were used as substrates; Z-Arg-Arg-AMC for cathepsin B, Z-Phe-Arg-AMC for cathepsins B and L together [11].
 

Analytical, diagnostic and therapeutic context of Cbz-phe-arg-mca

References

  1. Characterization of the serine protease and serine protease inhibitor from the tissue-penetrating nematode Anisakis simplex. Morris, S.R., Sakanari, J.A. J. Biol. Chem. (1994) [Pubmed]
  2. Expression and alteration of the S2 subsite of the Leishmania major cathepsin B-like cysteine protease. Chan, V.J., Selzer, P.M., McKerrow, J.H., Sakanari, J.A. Biochem. J. (1999) [Pubmed]
  3. Cathepsin L, but not cathepsin B, is a potential kininogenase. Desmazes, C., Gauthier, F., Lalmanach, G. Biol. Chem. (2001) [Pubmed]
  4. Characterisation of Tc-cpl-1, a cathepsin L-like cysteine protease from Toxocara canis infective larvae. Loukas, A., Selzer, P.M., Maizels, R.M. Mol. Biochem. Parasitol. (1998) [Pubmed]
  5. Tumor-associated cysteine proteinase activities in human melanoma cells and fibroblasts of different origin. Mayer, P., Schmid, H., Schaber, B., Fierlbeck, G. Eur. J. Cell Biol. (1997) [Pubmed]
  6. Characterisation of cysteine proteinases responsible for digestive proteolysis in guts of larval western corn rootworm (Diabrotica virgifera) by expression in the yeast Pichia pastoris. Bown, D.P., Wilkinson, H.S., Jongsma, M.A., Gatehouse, J.A. Insect Biochem. Mol. Biol. (2004) [Pubmed]
  7. Assessment of cathepsin L activity by use of the inhibitor CA-074 compared to cathepsin B activity in human lung tumor tissue. Werle, B., Ebert, W., Klein, W., Spiess, E. Biol. Chem. Hoppe-Seyler (1995) [Pubmed]
  8. Identification of a developmentally regulated cysteine protease of Trypanosoma brucei. Pamer, E.G., So, M., Davis, C.E. Mol. Biochem. Parasitol. (1989) [Pubmed]
  9. Fluorescent, internally quenched, peptides for exploring the pH-dependent substrate specificity of cathepsin B. Ruzza, P., Quintieri, L., Osler, A., Calderan, A., Biondi, B., Floreani, M., Guiotto, A., Borin, G. J. Pept. Sci. (2006) [Pubmed]
  10. Characterization and large-scale expression of the recombinant cysteine proteinase from adult Clonorchis sinensis. Park, S.Y., Lee, K.H., Hwang, Y.B., Kim, K.Y., Park, S.K., Hwang, H.A., Sakanari, J.A., Hong, K.M., Kim, S.I., Park, H. J. Parasitol. (2001) [Pubmed]
  11. Low-density lipoprotein suppresses cathepsins B and L activity in rat mesangial cells. Paczek, L., Teschner, M., Schaefer, R.M., Lao, M., Gradowska, L., Heidland, A. Mineral and electrolyte metabolism. (1996) [Pubmed]
  12. Stimulation of the secretion of latent cysteine proteinase activity by tumor necrosis factor alpha and interleukin-1. Huet, G., Flipo, R.M., Colin, C., Janin, A., Hemon, B., Collyn-d'Hooghe, M., Lafyatis, R., Duquesnoy, B., Degand, P. Arthritis Rheum. (1993) [Pubmed]
 
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