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Related Concept Videos

Lysosomal Hydrolases01:22

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
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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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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.
Lysosomes01:31

Lysosomes

Lysosomes are membrane-enclosed spherical sacs derived from the Golgi apparatus. The most important function of the lysosome is degrading macromolecules and biological polymers that are released during membrane trafficking events such as the secretory, endocytic, autophagic, and phagocytic pathways. The degradation is carried out by several hydrolytic enzymes active in an acidic environment of the lysosomal lumen. These acid hydrolases are involved in cellular processes such as cell signaling,...
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The Proteasome Structure

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Related Experiment Video

Updated: Jul 6, 2026

Demonstration of Proteolytic Activation of the Epithelial Sodium Channel (ENaC) by Combining Current Measurements with Detection of Cleavage Fragments
08:56

Demonstration of Proteolytic Activation of the Epithelial Sodium Channel (ENaC) by Combining Current Measurements with Detection of Cleavage Fragments

Published on: July 5, 2014

Highly active and selective endopeptidases with programmed substrate specificities.

Navin Varadarajan1, Sarah Rodriguez, Bum-Yeol Hwang

  • 1Institute for Cell and Molecular Biology, University of Texas, Austin, Texas 78712, USA.

Nature Chemical Biology
|April 9, 2008
PubMed
Summary
This summary is machine-generated.

Researchers engineered novel endopeptidases with high catalytic efficiency for diverse peptide sequences. These artificial proteases exhibit unique specificities, like recognizing GluArg, expanding enzymatic capabilities beyond natural proteases.

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Related Experiment Videos

Last Updated: Jul 6, 2026

Demonstration of Proteolytic Activation of the Epithelial Sodium Channel (ENaC) by Combining Current Measurements with Detection of Cleavage Fragments
08:56

Demonstration of Proteolytic Activation of the Epithelial Sodium Channel (ENaC) by Combining Current Measurements with Detection of Cleavage Fragments

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Defining Substrate Specificities for Lipase and Phospholipase Candidates
08:59

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

Area of Science:

  • Biochemistry
  • Enzymology
  • Protein Engineering

Background:

  • Proteases are enzymes that cleave peptide bonds.
  • Natural proteases exhibit specific recognition patterns for substrates.
  • Engineering proteases offers opportunities to expand enzymatic functions.

Purpose of the Study:

  • To create a family of engineered endopeptidases with high selectivity and catalytic efficiency.
  • To program protease variants for novel substrate recognition, including altered amino acid properties.
  • To explore the genetic basis of engineered protease function.

Main Methods:

  • Utilized a selection-counterselection substrate screening method.
  • Employed libraries to identify protease variants with desired specificities.
  • Analyzed amino acid substitutions responsible for altered protease function.

Main Results:

  • Developed engineered endopeptidases with high catalytic efficiency (kcat/KM > 10(40 M(- 1) s(- 1)).
  • Achieved programmed recognition of amino acids with altered charge, size, and hydrophobicity.
  • Discovered a novel GluArg specificity not observed in natural proteases.
  • Identified epistatic amino acid substitutions in the artificial protease family.

Conclusions:

  • Engineered endopeptidases demonstrate significant advancements in enzymatic function and specificity.
  • Artificial proteases can be programmed to recognize non-natural substrate features.
  • This work expands the toolkit of engineered enzymes for diverse applications.