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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.
- 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.
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