Presentation Title

P-30 Exploring enzymes: catalytic mechanism and biological function

Presenter Status

Professor, Department of Biology

Preferred Session

Poster Session

Location

Buller Hall Hallways

Start Date

21-10-2022 2:00 PM

End Date

21-10-2022 3:00 PM

Presentation Abstract

Enzymes are critical for the biochemistry of life, as they make chemical reactions happen that could not otherwise occur. The Proteolysis Lab studies a family of enzymes that trims individual amino acids from the carboxy-terminal ends of peptides and proteins. This can be for the purpose of digestion, but is often to regulate the activity of important peptides and proteins. Currently we are exploring the mechanism and function of two such enzymes. Ecm14L is derived from the mushroom Agaricus bisporus. Its function is unknown, but it appears to function through a unique mechanism, in which a tyrosine plays the catalytic role of general base. Carboxypeptidase O (CPO) is an enzyme found in most vertebrates. Several lines of evidence suggest that CPO may be a folate hydrolase, including expression in immune cells, ability to cleave glutamate-extended folate, and activation by glutamate-extended folates. Results from these two lines of inquiry will lead to a deeper understanding of proteolytic function and diversity.

Acknowledgments

Andrews University Faculty Research Grants

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COinS
 
Oct 21st, 2:00 PM Oct 21st, 3:00 PM

P-30 Exploring enzymes: catalytic mechanism and biological function

Buller Hall Hallways

Enzymes are critical for the biochemistry of life, as they make chemical reactions happen that could not otherwise occur. The Proteolysis Lab studies a family of enzymes that trims individual amino acids from the carboxy-terminal ends of peptides and proteins. This can be for the purpose of digestion, but is often to regulate the activity of important peptides and proteins. Currently we are exploring the mechanism and function of two such enzymes. Ecm14L is derived from the mushroom Agaricus bisporus. Its function is unknown, but it appears to function through a unique mechanism, in which a tyrosine plays the catalytic role of general base. Carboxypeptidase O (CPO) is an enzyme found in most vertebrates. Several lines of evidence suggest that CPO may be a folate hydrolase, including expression in immune cells, ability to cleave glutamate-extended folate, and activation by glutamate-extended folates. Results from these two lines of inquiry will lead to a deeper understanding of proteolytic function and diversity.