This is a competitive renewal application to provide continued support for collaborative studies on the enzymatic mechanisms of tyrosine phenol-lyase. This enzyme uses 5'-periodical phosphate (PLP) as a cofactor, and it is involved in several amino acid modification reactions including transaminations, decarboxylations and beta and gamma eliminations. Several biologically active metabolites involved in a variety of important biological processes, including neurotransmission, depend on similar enzymes. In the present studies the collaborators will continue on their previous course and will generate three dimensional structures of wild-type tyrosine phenol-lyase with substrates and substrate analogs. The structural results of these studies will guide additional experiments for the generation of variant forms of the enzyme. In addition, kinetic studies using multiple isotope effects will be done to identify the rate limiting step in tyrosine phenol-lyase mediated catalysis.

Agency
National Institute of Health (NIH)
Institute
Fogarty International Center (FIC)
Type
Small Research Grants (R03)
Project #
2R03TW000106-04
Application #
2627556
Study Section
International and Cooperative Projects 1 Study Section (ICP)
Project Start
1993-09-01
Project End
2001-06-30
Budget Start
1998-07-01
Budget End
1999-06-30
Support Year
4
Fiscal Year
1998
Total Cost
Indirect Cost
Name
University of Georgia
Department
Chemistry
Type
Other Domestic Higher Education
DUNS #
City
Athens
State
GA
Country
United States
Zip Code
30602