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Structure, function and biological relevance of prolyl oligopeptidase
Zoltán Szeltner1, László Polgár
1Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, H-1518 Budapest 112, P.O. Box 7, Hungary.
Current Protein & Peptide Science
|March 14, 2008
Summary
Prolyl oligopeptidase (POP) is a cytosolic enzyme with a unique structure that limits its substrate size. Research explores its role in cognitive functions, signaling pathways, and potential therapeutic applications for neurological disorders and celiac sprue.
Area of Science:
- Biochemistry
- Enzymology
- Structural Biology
Background:
- Prolyl oligopeptidase (POP) belongs to a serine peptidase family with limited peptide hydrolysis capacity.
- Its structure features a peptidase domain and a beta-propeller domain that restricts access to the active site.
Purpose of the Study:
- To review the substrate selection mechanism, binding mode, and catalytic mechanism of POP.
- To explore the diverse biological roles and potential therapeutic applications of POP.
Main Methods:
- Structural analysis of prolyl oligopeptidase (POP).
- Review of experimental studies on POP's involvement in biological processes and therapeutic strategies.
Main Results:
- POP's structure, particularly the beta-propeller domain, dictates its substrate specificity by excluding larger peptides.
- POP is implicated in cognitive and psychiatric processes, inositol phosphate signaling, and metabolizing bioactive peptides.
Conclusions:
- POP's precise cellular function remains under investigation, with ongoing research into its role in neurological disorders like Alzheimer's disease.
- Recombinant bacterial POPs show promise as therapeutics for celiac sprue.
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