8
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Serine proteases.

      Iubmb Life
      Isoenzymes, genetics, metabolism, Models, Molecular, Protein Binding, Protein Conformation, Serine Endopeptidases, Substrate Specificity

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Over one third of all known proteolytic enzymes are serine proteases. Among these, the trypsins underwent the most predominant genetic expansion yielding the enzymes responsible for digestion, blood coagulation, fibrinolysis, development, fertilization, apoptosis, and immunity. The success of this expansion resides in a highly efficient fold that couples catalysis and regulatory interactions. Added complexity comes from the recent observation of a significant conformational plasticity of the trypsin fold. A new paradigm emerges where two forms of the protease, E* and E, are in allosteric equilibrium and determine biological activity and specificity.

          Related collections

          Author and article information

          Journal
          19180666
          2675663
          10.1002/iub.186

          Chemistry
          Isoenzymes,genetics,metabolism,Models, Molecular,Protein Binding,Protein Conformation,Serine Endopeptidases,Substrate Specificity

          Comments

          Comment on this article