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[Thiol peptide hydrolases from animal tissues, their structure and function].
Molekuliarnaia Biologiia
|September 1, 1986
Summary
This review summarizes thiol (cysteine) peptide hydrolases, focusing on lysosomal cathepsins B, H, and L. It details their structure, functions in protein processing, and regulation by inhibitors.
Area of Science:
- Biochemistry
- Enzymology
Context:
- Thiol (cysteine) peptide hydrolases are a diverse group of intracellular enzymes found in animal tissues.
- Lysosomal thiol peptide hydrolases, including cathepsins B, H, and L, are well-characterized and share structural similarities with papain.
Purpose:
- To summarize existing data on the properties, structure, and biological functions of thiol peptide hydrolases.
- To explore the roles of these enzymes in various cellular processes and their regulation.
Summary:
- The review covers both endo- and exopeptidases within this enzyme class.
- It highlights the structural homology of cathepsins to papain and discusses calcium-dependent neutral proteinases.
- Key biological functions, including protein turnover, post-translational modification, and metabolic regulation, are examined.
Impact:
- Provides a comprehensive overview of thiol peptide hydrolases for researchers in enzymology and molecular biology.
- Facilitates understanding of enzyme regulation and endogenous inhibitor roles.
- Contributes to the knowledge base for studying protein processing and cellular regulation.
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