{"title":"组织蛋白酶C的催化性能","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":"{\"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}","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}
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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