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(NAS Colloquium) Proteolytic Processing and Physiological Regulation (1999) / Chapter Skim
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Kinetic stability as a mechanism for protease longevity
Pages 11008-11014

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From page 11008...
... Whereas this has required the convolution of a pro region to facilitate folding, the result has been the optimization of native-state properties independent of their consequences on thermodynamic stability. Structural and mutational data lead to a model for catalysis of folding in which the pro region binds to a conserved ,B-hairpin in the ALP C-terminal domain, stabilizing the folding transition state and the native state.
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From page 11009...
... Release of active ALP requires that the Pro region be removed by proteolysis. Once Pro is degraded, the active protease becomes kinetically trapped in the metastable N state, with the high barrier preventing unfolding to the more thermodynamically favored unfolded states.
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From page 11010...
... Sequence comparisons with homologous pro-proteases suggest that the Pro structure may be a common pro region fold. Primary sequence alignments of Pro and eight related pro regions (Fig.
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From page 11011...
... . Kinetic and thermodynamic analyses suggest that the folding transition state and the native state must share many structural features.
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From page 11012...
... In fact, there may be a functional an initial fast rate equal to the rate of pro folding alone synergism between the multiple proteases secreted simulta followed by a slower rate for pro-mediated folding of aLP. neously by the host, Lysobacter enzymogenes, in cleaving each During in cis folding, formation of the active site allows the other's pro regions.
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From page 11013...
... Glycine content appears to be a common feature distinguishing homologous proteases to ALP that have pro regions from those that do not (Table 1~. The Streptomyces griseus proteases, along with several other pro region-containing homologues, have 16-20~o glycines, whereas the mammalian digestive enzymes and other members of the trypsin serine protease family without pro regions have 6-12% glycines.
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From page 11014...
... 11014 Colloquium Paper: Cunningham et al.
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Key Terms

  • native state
  • pro regions
  • transition state
  • kinetic stability
  • folding barrier

  • griseus protease
  • active site
  • folding transition
  • unfolded states
  • alp folding

  • inhibitory complex
  • pro structure
  • protease active
  • serine protease
  • metastable native

  • mature protease
  • unpublished data
  • extracellular bacterial
  • hughes medical
  • active alp

  • foldase activity
  • medical institute
  • complex structure
  • native conformation
  • bacterial proteases

  • lysobacter enzymogenes
  • pro foldase
  • howard hughes
  • rigid native
  • sequence homology


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