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Structure and function relationship in prolyl oligopeptidase.

Roos Van Elzen¹, Anne-Marie Lambeir

¹Laboratory of Medical Biochemistry, University of Antwerp - Campus Drie Eiken, Wilrijk, Belgium. roos.vanelzen@ua.ac.be

CNS & Neurological Disorders Drug Targets

|January 13, 2011

Summary

Prolyl oligopeptidase (POP) is a complex serine protease with multifaceted activity. This review details POP

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Area of Science:

Biochemistry
Enzymology
Structural Biology

Background:

Prolyl oligopeptidase (POP) is a unique serine protease.
Its complex behavior and structural architecture have led to speculation about its mechanism.
Recent findings suggest significant conformational changes upon substrate binding.

Purpose of the Study:

To assemble available information into a coherent description of POP's structural composition.
To describe the active site's structural boundaries and catalytic components.
To elucidate substrate specificity based on physico-chemical properties.

Main Methods:

Enzyme kinetic measurements.
Structural analysis of POP.
Evaluation of physico-chemical properties influencing substrate specificity.

Main Results:

POP exhibits multifaceted activity influenced by reaction conditions and substrates.
The active site's location at the interface of catalytic and β-propeller domains is crucial.
Substrate specificity is determined by structural boundaries and surrounding residue properties.

Conclusions:

Understanding POP's structural composition and active site features is key to its catalytic behavior.
Physico-chemical properties of residues around the scissile bond dictate POP specificity.
This comprehensive analysis enhances comprehension of POP's physiological function.