{"title":"The catalytic properties of cathepsin C","authors":"R.J. Planta , Jeannette Gorter, M. Gruber","doi":"10.1016/0926-6569(64)90077-X","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The catalytic properties of the intracellular peptidase cathepsin C (EC 3.4.4.9) were investigated. The enzyme is devoid of the proteolytic activity that had been ascribed to it.</p></span></li><li><span>2.</span><span><p>2. Cathepsin C has a very narrow specificity. Its activity is restricted to the removal of N-terminal dipeptide units that meet a number of rigorous requirements, from amides, esters or polypeptides.</p></span></li><li><span>3.</span><span><p>3. In transamidation reactions cathepsin C shows a narrow specificity not only for the peptide “donor”—as in its hydrolytic activities—but also for the “acceptor” to which the dipeptide units are transferred.</p></span></li><li><span>4.</span><span><p>4. These enzymic properties make a function of cathepsin C in intracellular protein catabolism seem improbable.</p></span></li></ul></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"89 3","pages":"Pages 511-519"},"PeriodicalIF":0.0000,"publicationDate":"1964-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90077-X","citationCount":"31","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/092665696490077X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 31
Abstract
1.
1. The catalytic properties of the intracellular peptidase cathepsin C (EC 3.4.4.9) were investigated. The enzyme is devoid of the proteolytic activity that had been ascribed to it.
2.
2. Cathepsin C has a very narrow specificity. Its activity is restricted to the removal of N-terminal dipeptide units that meet a number of rigorous requirements, from amides, esters or polypeptides.
3.
3. In transamidation reactions cathepsin C shows a narrow specificity not only for the peptide “donor”—as in its hydrolytic activities—but also for the “acceptor” to which the dipeptide units are transferred.
4.
4. These enzymic properties make a function of cathepsin C in intracellular protein catabolism seem improbable.
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