Species variations amongst lysosomal cysteine proteinases.
Properties of cathepsin L from rat liver lysosomes were compared with those of a similar enzyme, cathepsin S from beef spleen. Major characteristics of cathepsin L are the high activity against Z-Phe-Arg-methylcoumarylamide and sensitivity to the fast reacting irreversible inhibitor Z-Phe-Phe-diazomethane. In contrast, cathepsin S hydrolyzes Z-Phe-Arg-methylcoumarylamide only slowly and Z-Phe-Phe-diazomethane cannot be regarded as a potent inhibitor of this enzyme. The differences in the substrate specificity of cathepsin L from rat liver and cathepsin S from beef spleen are discussed in comparison with the substrate specificity of cathepsin B from rat and human liver and beef spleen.
D000818:Animals; D002401:Cathepsin B; D056668:Cathepsin L; D002403:Cathepsins / Q000378:metabolism*; D002417:Cattle; D003546:Cysteine Endopeptidases; D010450:Endopeptidases; D006801:Humans; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008247:Lysosomes / Q000201:enzymology*; D051381:Rats; D013045:Species Specificity; D013154:Spleen / Q000201:enzymology; D013379:Substrate Specificity
D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D002401:Cathepsin B; C534281:CTSL protein, human; D056668:Cathepsin L; C534280:Ctsl protein, rat; C028217:cathepsin S