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ICE processing and kinetic mechanism

D A Giegel1

  • 1Biochemistry Section, Parke-Davis Pharmaceutical Research, Division of Warner-Lambert Company, Ann Arbor, Michigan 48105, USA.

Journal of Cellular Biochemistry
|January 1, 1997
PubMed
Summary

Interleukin-1 beta converting enzyme (ICE) catalysis involves rate-limiting acylation and deacylation steps, reducing overall reaction rates. The study also explores sequence identities and prodomain roles in human ICE-like proteases.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Protease research

Background:

  • Interleukin-1 beta converting enzyme (ICE) is a target for pharmaceutical inhibitor development.
  • Understanding the kinetics of individual catalytic steps in ICE is crucial but limited.
  • Eight human ICE-like proteases share significant sequence identity, particularly in active domains.

Purpose of the Study:

  • To elucidate the rate-limiting steps in Interleukin-1 beta converting enzyme (ICE) catalysis.
  • To compare the catalytic efficiency of ICE with other proteases.
  • To investigate the sequence variability and potential regulatory roles of prodomains in ICE-like proteases.

Main Methods:

  • Kinetic analysis of acylation and deacylation steps in ICE catalysis.
  • Comparative analysis of reaction rates with papain and its optimized substrate.
  • Sequence identity comparison across full-length human ICE-like proteases and their active domains.

Main Results:

  • Both acylation and deacylation steps are partially rate-limiting in ICE catalysis.
  • The overall reaction rate of ICE is less than 3% of papain's rate with its optimal substrate.
  • Sequence identity varies, with greater conservation in active domains than in N-terminal prodomains.

Conclusions:

  • The individual chemical steps in ICE catalysis are not fully efficient, limiting overall enzyme activity.
  • Significant sequence variability exists among human ICE-like proteases, particularly in their prodomains.
  • N-terminal prodomains may play a regulatory role in the processing of ICE family members.

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