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Caspases

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.

The Proteasome

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

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 Proteasome

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 Proteasome Structure

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...

Lysosomal Hydrolases

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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Updated: Jul 5, 2026

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

Papain-like cysteine proteases.

¹Mount Sinai School of Medicine, New York, New York, USA.

Current Protocols in Protein Science

|April 23, 2008

Summary

Cysteine proteases, particularly papain-like proteases (C1 family), are vital enzymes found across diverse organisms. This review details mammalian cathepsins, covering their localization, mechanisms, and substrate specificities.

Area of Science:

Biochemistry
Molecular Biology
Enzymology

Background:

Cysteine proteases utilize a nucleophilic cysteine residue for substrate cleavage.
Papain-like cysteine proteases (C1 family) are widespread and essential enzymes.
Mammalian C1 family proteases are commonly referred to as cathepsins.

Purpose of the Study:

To provide a comprehensive overview of mammalian cathepsins.
To elucidate the catalytic mechanisms and substrate specificities of cathepsins.
To detail the subcellular and tissue localization of various cathepsins.

Main Methods:

Literature review and synthesis of existing research on cathepsins.
Analysis of catalytic mechanisms based on biochemical studies.

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Compilation of data on tissue and subcellular distribution.

Main Results:

Cathepsins exhibit diverse subcellular and tissue localization patterns.
Detailed catalytic mechanisms involving the active site cysteine residue are described.
Substrate specificities vary among different cathepsin types, reflecting their distinct functions.

Conclusions:

Cathepsins are a crucial group of cysteine proteases with significant biological roles.
Understanding cathepsin properties is key to comprehending various physiological and pathological processes.
This review consolidates essential information on cathepsins for researchers.