The catalytic properties of cathepsin C

R.J. Planta , Jeannette Gorter, M. Gruber
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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.

组织蛋白酶C的催化性能
1.1. 研究了胞内肽酶组织蛋白酶C (EC 3.4.4.9)的催化性能。这种酶缺乏被认为具有的蛋白水解活性。组织蛋白酶C具有非常狭窄的特异性。它的活性仅限于从酰胺、酯或多肽中去除n端二肽单元,这些二肽单元符合一些严格的要求。在转胺反应中,组织蛋白酶C不仅对肽“供体”(如其水解活性)有狭窄的特异性,而且对二肽单元转移到的“受体”也有狭窄的特异性。这些酶的特性使得组织蛋白酶C在细胞内蛋白质分解代谢中的作用看起来不太可能。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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