Article
Thermal repair of tryptophan synthase mutations in a regulatory intersubunit salt bridge. Evidence from arrhenius plots, absorption spectra, and primary kinetic isotope effects.
The Journal of biological chemistry - 7 Jul 2000
Fan Y X, McPhie P, Miles E W
Abstract excerpt
This work is aimed at understanding how protein structure and conformation regulate activity and allosteric communication in the tryptophan synthase alpha(2)beta(2) complex from Salmonella typhimurium. Previous crystallographic and kinetic results suggest that both monovalent cations and a salt bridge between alpha subunit Asp(56) and beta subunit Lys(167) play allosteric roles. Here we show that mutation of...
Topics
- Allosteric Regulation
- Bacterial Proteins
- Cations, Monovalent
- Enzyme Activation
- Glycerophosphates
- Indoles
- Kinetics
- Mutation
- Protein Conformation
- Salmonella typhimurium
- Serine
