Presentation Title

Structure and function of a unique proteolytic enzyme

Presenter Information

Peter Lyons, Andrews University

Presenter Status

Faculty

Session

C-4

Location

CSH Room 108

Start Date

8-5-2014 3:30 PM

End Date

8-5-2014 4:00 PM

Presentation Abstract

Carboxypeptidases are proteolytic enzymes that are known to modify and degrade bioactive and dietary peptides. While many members of this family of enzymes have been characterized for decades, some members are poorly understood. Carboxypeptidase O (CPO) is one such poorly characterized enzyme. Recent experiments have shown that CPO is highly expressed by intestinal epithelial cells, where it is anchored to cellular membranes by a glycosylphosphatidylinositol group. It is found on the external plasma membrane, suggesting a role in digestion. The identity of associated internal membranes is not clear. Current research is investigating the subcellular localization of CPO and the manner in which this enzyme is regulated.

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May 8th, 3:30 PM May 8th, 4:00 PM

Structure and function of a unique proteolytic enzyme

CSH Room 108

Carboxypeptidases are proteolytic enzymes that are known to modify and degrade bioactive and dietary peptides. While many members of this family of enzymes have been characterized for decades, some members are poorly understood. Carboxypeptidase O (CPO) is one such poorly characterized enzyme. Recent experiments have shown that CPO is highly expressed by intestinal epithelial cells, where it is anchored to cellular membranes by a glycosylphosphatidylinositol group. It is found on the external plasma membrane, suggesting a role in digestion. The identity of associated internal membranes is not clear. Current research is investigating the subcellular localization of CPO and the manner in which this enzyme is regulated.