Article
The role of electrostatic interactions in the mechanism of peptide bond hydrolysis by a Ser-Lys catalytic dyad.
Protein engineering - 1 Dec 1991
Slilaty S N, Vu H K
Abstract excerpt
General-base catalysis in the active site of serine proteases is carried out by the imidazole side chain of a histidine. During formation of the transition state, an adjacent carboxylic acid group stabilizes the positive charge that forms on the general-base catalyst and as a result contributes several orders of magnitude to the catalytic efficiency of these enzymes. In the recently discovered family of...
Topics
- Bacterial Proteins
- Binding Sites
- Escherichia coli
- Hydrogen-Ion Concentration
- Kinetics
- Lysine
- Models, Chemical
- Mutagenesis, Site-Directed
- Mutation
- Protons
- Rec A Recombinases