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Related Concept Videos

Caspases01:24

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside cells.
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Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
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Demonstration of Proteolytic Activation of the Epithelial Sodium Channel (ENaC) by Combining Current Measurements with Detection of Cleavage Fragments
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Serine proteases.

Enrico Di Cera1

  • 1Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Box 8231, St. Louis, MO 63110, USA. enrico@wustl.edu

IUBMB Life
|January 31, 2009
PubMed
Summary
This summary is machine-generated.

Serine proteases, particularly trypsins, are crucial enzymes involved in many biological processes. Their fold

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Serine proteases represent over a third of known proteolytic enzymes.
  • Trypsin enzymes have undergone significant genetic expansion, impacting diverse biological functions.
  • The trypsin fold is known for its efficiency in coupling catalysis and regulatory interactions.

Purpose of the Study:

  • To explore the conformational plasticity of the trypsin fold.
  • To investigate the emerging paradigm of protease allosteric equilibrium.
  • To understand how protease forms influence biological activity and specificity.

Main Methods:

  • Allosteric equilibrium analysis
  • Conformational plasticity studies
  • Protease activity assays

Main Results:

  • Trypsin fold exhibits significant conformational plasticity.
  • Two protease forms, E* and E, exist in allosteric equilibrium.
  • This equilibrium dictates protease biological activity and specificity.

Conclusions:

  • A new paradigm suggests trypsin activity is governed by an allosteric equilibrium between two conformational states.
  • Understanding this plasticity is key to deciphering trypsin function in various biological systems.
  • This highlights the dynamic nature of enzyme structure-function relationships.