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(NAS Colloquium) Proteolytic Processing and Physiological Regulation (1999) / Chapter Skim
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Proteolytic enzymes, past and future
Pages 10962-10963

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From page 10962...
... Other landmarks included the discovery of natural and synthetic protease inhibitors such as disopropylfluoro phos phate, which introduced an organic phosphate label into the active site of serine proteases. Chemical characterization of active sites together with x-ray structure analysis of proteases showed that they can be grouped into families of common mechanism, similar structural features, and hence common evolutionary origin.
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From page 10963...
... In every known instance, the timing, placement, and mode of action of the virus encoded protease are somehow adapted to the conditions under which it operates within the viral environment. Two examples follow: in herpes viruses such as cytomegalovirus, the structure of the protease reveals a catalytic triad of His/His/Ser instead of the conventional Asp/His/Ser of the mammalian serine proteases and a single beta barrel structure per monomer instead of two in the mammalian serine proteases (13~.
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Key Terms

  • proteolytic processing
  • serine proteases
  • protease inhibitors
  • physiological regulation
  • protein chemistry

  • catalytic triad
  • mammalian serine
  • enzyme precursor
  • conformational changes
  • nascent polypeptide

  • cell cycle
  • polypeptide chains
  • permit interaction
  • constant solubility
  • held february

  • major impetus
  • active site
  • viral proteases
  • metallo protease
  • triad characteristic

  • thousand proteolytic
  • active sites
  • rapidly expanding
  • following papers
  • barrel structure

  • mutagenesis allows
  • proteolysis accompanying
  • structure analysis
  • zymogen activation
  • unique combinations


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