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Chemical Compound Review

CHEMBL154085     naphthalene-2-carboxamide

Synonyms: SureCN546633, AG-C-04232, ACMC-20ak76, TimTec1_000199, NSC-171209, ...
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High impact information on NSC171209

  • In contrast, dipeptide nucleophiles did not significantly accelerate the cathepsin B-catalyzed cleavage of either the p-nitroanilide or the 2-naphthylamide of N alpha-benzoylarginine, suggesting that the hydrolysis of these amide substrates was acylation rate-limiting [1].
  • Isolated hepatocytes were incubated with vinblastine to induce autophagosome accumulation; the cells were then homogenized and treated with the cathepsin C substrate glycyl-l-phenylalanine 2-naphthylamide to cause osmotic disruption of the lysosomes [2].
  • The specificity of the synthetic substrate Gly-[L-Asp]4-L-Lys 2-naphthylamide originally developed for the assay of enteropeptidase (EC, was investigated with partially purified aminopeptidase [3].
  • When Z-Gly-Gly-Leu-Nap (where -Nap represents 2-naphthylamide) was substituted for the above substrate, no NE-catalysed hydrolysis occurred, but Z-Leu-Leu-Glu-Nap was readily hydrolysed by NE [4].
  • The pH-dependences of kcat, Km and kcat./Km for the hydrolysis at 25 degrees C at I 0.1 of L-arginine 2-naphthylamide catalysed by cathepsin H from bovine spleen were determined in the pH range approx. 4-8 [5].

Biological context of NSC171209

  • Intralysosomal hydrolysis of glycyl-L-phenylalanine 2-naphthylamide [6].
  • The effect of temperature on the apparent Km of L-leucyl-4-methoxy 2-naphthylamide and th dipeptide phenylalanyl-glycine was small, especially between 10 and 25 C. The apparent Km varied only between 36.7 and 49.8 microM at these temperatures and the six common genotypes did not differ in temperature-dependent substrate affinities [7].
  • A single round of random mutagenesis followed by screening for hydrolytic activity for oleoyl 2-naphthylamide as compared with that for oleoyl 2-naphthyl ester identified five mutants with 1.7-2.0-fold increased relative amidase activities [8].

Anatomical context of NSC171209


Associations of NSC171209 with other chemical compounds


Gene context of NSC171209


  1. Steady state kinetic evidence for an acyl-enzyme intermediate in reactions catalyzed by bovine spleen cathepsin B. Bajkowski, A.S., Frankfater, A. J. Biol. Chem. (1983) [Pubmed]
  2. Purification and characterization of autophagosomes from rat hepatocytes. Strømhaug, P.E., Berg, T.O., Fengsrud, M., Seglen, P.O. Biochem. J. (1998) [Pubmed]
  3. Specificity studies on enteropeptidase substrates related to the N-terminus of trypsinogen. Jenö, P., Green, J.R., Lentze, M.J. Biochem. J. (1987) [Pubmed]
  4. A high-molecular-mass neutral endopeptidase-24.5 from human lung. Zolfaghari, R., Baker, C.R., Canizaro, P.C., Amirgholami, A., Bĕhal, F.J. Biochem. J. (1987) [Pubmed]
  5. A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and -161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic studies up to pH 8 of the hydrolysis of N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide catalysed by cathepsin B and of L-arginine 2-naphthylamide catalysed by cathepsin H. Willenbrock, F., Brocklehurst, K. Biochem. J. (1985) [Pubmed]
  6. Intralysosomal hydrolysis of glycyl-L-phenylalanine 2-naphthylamide. Jadot, M., Colmant, C., Wattiaux-De Coninck, S., Wattiaux, R. Biochem. J. (1984) [Pubmed]
  7. Biochemical studies of aminopeptidase polymorphism in Mytilus edulis. II. Dependence of reaction rate on physical factors and enzyme concentration. Koehn, R.K., Siebenaller, J.F. Biochem. Genet. (1981) [Pubmed]
  8. Directed evolution of Pseudomonas aeruginosa lipase for improved amide-hydrolyzing activity. Fujii, R., Nakagawa, Y., Hiratake, J., Sogabe, A., Sakata, K. Protein Eng. Des. Sel. (2005) [Pubmed]
  9. Activation of the multicatalytic proteinase from rat skeletal muscle by fatty acids or sodium dodecyl sulphate. Dahlmann, B., Rutschmann, M., Kuehn, L., Reinauer, H. Biochem. J. (1985) [Pubmed]
  10. Use of glycyl-L-phenylalanine 2-naphthylamide, a lysosome-disrupting cathepsin C substrate, to distinguish between lysosomes and prelysosomal endocytic vacuoles. Berg, T.O., Strømhaug, E., Løvdal, T., Seglen, O., Berg, T. Biochem. J. (1994) [Pubmed]
  11. Studies on cathepsin B in human articular cartilage. Bayliss, M.T., Ali, S.Y. Biochem. J. (1978) [Pubmed]
  12. Purification and characterization of a metallo-endoproteinase from mouse kidney. Beynon, R.J., Shannon, J.D., Bond, J.S. Biochem. J. (1981) [Pubmed]
  13. Purification and properties of thiol protease inhibitor from rat liver cytosol. Hirado, M., Iwata, D., Niinobe, M., Fujii, S. Biochim. Biophys. Acta (1981) [Pubmed]
  14. Proteins of the kidney microvillar membrane. Aspartate aminopeptidase: purification by immunoadsorbent chromatography and properties of the detergent- and proteinase-solubilized forms. Danielsen, E.M., Norén, O., Sjöström, H., Ingram, J., Kenny, A.J. Biochem. J. (1980) [Pubmed]
  15. Cation-independent mannose 6-phosphate and 78 kDa receptors for lysosomal enzyme targeting are located in different cell compartments. González-Noriega, A., Michalak, C., Antonio Sosa Melgarejo, J. Biochim. Biophys. Acta (2005) [Pubmed]
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