Methionine aminopeptidase (MAP) is an enzyme that catalyzes the removal of amino-terminal methionine from a newly made protein facilitating the development of a mature polypeptide. MAP contains two cobalt ions which are 2.9 A apart; these cobalt ions and their environment are the focus of this study. We report the successful purification of a significant amount of the active enzyme from an E. coli strain (obtained from Prof. Brian Mathews at the University of Oregon) that has been engineered to over-produce MAP. We also report preliminary experiments designed to address questions of how tightly the cobalt ions are bound within the protein’s active site, and to explore the spectroscopic properties of cobalt in MAP.
Stephen Shargo, ’98
Sponsor: Cynthia Strong