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  • 标题:Role of proteolytic enzymes in biological regulation (a review)
  • 本地全文:下载
  • 作者:H Neurath ; K A Walsh
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1976
  • 卷号:73
  • 期号:11
  • 页码:3825-3832
  • DOI:10.1073/pnas.73.11.3825
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Many enzymes, hormones, and other physiologically active proteins are synthesized as inactive precursors (zymogens) that are subsequently converted to the active form by the selective enzymatic cleavage (limited proteolysis) of peptide bonds. The ultimate agency of activating enzymatic function is limited proteolysis, either in a single activation step or in a consecutive series (cascade). The specificity of each activation reaction is determined by the complementarity of the zymogen substrate and the active site of the attacking protease. The sequence of consecutive activation reactions is regulated by the specificity of each enzyme, whereas the degree of amplification of the initial stimulus is determined by the efficiency of each activating step. Zymogen activation produces a prompt and irreversible response to a physiological stimulus, and is capable of initiating new physiological functions. Typical examples are the precesses of blood coagulation, fibrinolysis, complement activation, hormone production, metamorphosis, fertilazation, supra-molecular assembly, and digestion. The zymogens of the pancreatic serine proteases, in particular, have served as models for detailed studies of the nature of the molecular changes that are involved in the dramatic increase in enzymatic activity that ensues upon limited proteolysis of the zymogen.
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