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Related Concept Videos

Protein Digestion01:02

Protein Digestion

Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
The Proteasome02:18

The Proteasome

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.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome Structure01:17

The Proteasome Structure

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.
The proteasome is an...
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.
Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...

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Related Experiment Video

Updated: Jun 22, 2026

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes
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The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes

Published on: May 25, 2018

Multifunctional aspartic peptidase prosegments.

Yasumi Horimoto1, Derek R Dee, Rickey Y Yada

  • 1Department of Food Science, University of Guelph, Guelph, Ont., Canada N1G 2W1.

New Biotechnology
|June 4, 2009
PubMed
Summary
This summary is machine-generated.

Aspartic peptidases (APs) are crucial enzymes with roles in food and medicine. Their N-terminal prosegment (PS) is key for proper folding, stability, and activation, impacting disease treatment strategies.

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Published on: May 13, 2020

Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Aspartic peptidases (APs) are enzymes with known structure-function relationships, but their molecular mechanisms require further elucidation.
  • APs are significant in food processing and as therapeutic targets for diseases like hypertension, cancer, Alzheimer's, AIDS, and malaria.
  • Understanding APs is vital for developing effective peptidase inhibitors for disease treatment.

Purpose of the Study:

  • To review current knowledge on the function of the N-terminal prosegment (PS) of aspartic peptidases (APs), particularly within the A1 family.
  • To emphasize the role of the AP PS in protein folding, cellular sorting, and enzyme inhibition.
  • To highlight the importance of the PS in zymogen activation and enzyme stability.

Main Methods:

  • Literature review of existing research on aspartic peptidases and their prosegments.
  • Analysis of studies focusing on the A1 family of aspartic peptidases.
  • Synthesis of information regarding the structural and functional roles of the prosegment domain.

Main Results:

  • The N-terminal prosegment (PS) plays a critical role in the correct folding and stability of aspartic peptidases (APs).
  • The PS influences the pH-dependent activation process and intracellular sorting of AP zymogens.
  • The PS can act as an endogenous inhibitor by blocking the active site before activation.

Conclusions:

  • The prosegment (PS) is essential for the proper maturation and function of aspartic peptidases (APs).
  • Further research into AP PS function can lead to the development of novel therapeutic strategies targeting these enzymes.
  • The review consolidates current understanding, paving the way for future investigations into AP mechanisms.