Article
Orotidine 5'-monophosphate decarboxylase: transition state stabilization from remote protein-phosphodianion interactions.
Biochemistry - 12 Jun 2012
Amyes Tina L, Ming Shonoi A, Goldman Lawrence M, Wood B McKay, Desai Bijoy J, Gerlt John A, Richard John P
Abstract excerpt
Mutants of orotidine 5'-monophosphate decarboxylase containing all possible single (Q215A, Y217F, and R235A), double, and triple substitutions of the side chains that interact with the phosphodianion group of the substrate orotidine 5'-monophosphate have been prepared. Essentially the entire effect of these mutations on the decarboxylation of the truncated neutral substrate 1-(β-d-erythrofuranosyl)orotic acid...
Topics
- Anions
- Binding Sites
- Gene Expression Regulation, Fungal
- Kinetics
- Models, Molecular
- Mutation
- Orotidine-5'-Phosphate Decarboxylase
- Phosphites
- Protein Conformation
- Substrate Specificity