Abstract

Branched chain keto dehydrogenase of Pseudomonas putida is an unusual enzyme whose activity is stimulated by L-valine. The enzyme has been purified to a specific activity of 10 units/mg protein. The purified enzyme contains 4 subunis with molecular weights of 49k, 46k, 39k, and 37k. The 49k protein has been isolated and identified as lipoamide dehydrogenase. The objective of the current year will be to isolate and identify the remainding subunits. The transacylase subunit will be identified by its specific labeling with N-ethyl(2,3-14C) maleimide in the presence of 2-ketoisovalerate. The dehydrogenase (E1) subunit will be identified by its reaction with ferricyanide and the release of radioactive carbon dioxide from 2-keto(1-14C) isovalerate.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases (NIADDK)
Type
Research Project (R01)
Project #
5R01AM021737-07
Application #
3151407
Study Section
(SSS)
Project Start
1979-07-01
Project End
1987-06-30
Budget Start
1985-07-01
Budget End
1986-06-30
Support Year
7
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of Oklahoma Health Sciences Center
Department
Type
School of Medicine & Dentistry
DUNS #
937727907
City
Oklahoma City
State
OK
Country
United States
Zip Code
73117