Expression and Purification of Selenomethionyl Prolidase from Alteromonas spJD6.5

摘要

Prolidase from Alteromonas spJD6.5 catalytically hydrolyzes a variety of 6-type CW nerve agents at a significant rate. However, this enzyme fails to hydrolyze V-type CW nerve agents. Logic-based design to obtain enzyme variants with novel catalytic capabilities in prolidase is the long-term objective of our goal. Elucidation of the three dimensional structure of prolidase is a key prerequisite to undertake this study. As a first step towards this goal, selenium-tagged prolidase was produced to initiate the structural studies of prolidase. Purification and characterization results of selenomethionyl prolidase are summarized in this report.