Article
Enzyme architecture: deconstruction of the enzyme-activating phosphodianion interactions of orotidine 5'-monophosphate decarboxylase.
Journal of the American Chemical Society - 16 Jul 2014
Goldman Lawrence M, Amyes Tina L, Goryanova Bogdana, Gerlt John A, Richard John P
Abstract excerpt
The mechanism for activation of orotidine 5'-monophosphate decarboxylase (OMPDC) by interactions of side chains from Gln215 and Try217 at a gripper loop and R235, adjacent to this loop, with the phosphodianion of OMP was probed by determining the kinetic parameters k(cat) and K(m) for all combinations of single, double, and triple Q215A, Y217F, and R235A mutations. The 12 kcal/mol intrinsic binding energy of the...
Topics
- Amino Acids
- Anions
- Enzymes
- Kinetics
- Models, Molecular
- Molecular Conformation
- Mutation
- Orotidine-5'-Phosphate Decarboxylase
- Protein Binding
- Saccharomyces cerevisiae