Article
Structurally and catalytically important residues in the phosphate binding loop of adenylate kinase of Escherichia coli.
Biochemistry - 14 Aug 1990
Reinstein J, Schlichting I, Wittinghofer A
Abstract excerpt
Amino acids in the phosphate binding loop of adenylate kinase of Escherichia coli were mutated by site-directed mutagenesis. The mutant proteins with a Pro-9----Gly (P9G) and with a Lys-13----Gln (K13Q) exchange were overexpressed and purified. They were characterized by steady-state kinetics, fl...
Topics
- Adenylate Kinase
- Amino Acid Sequence
- Base Sequence
- Enzyme Stability
- Escherichia coli
- Kinetics
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Mutation
- Phosphates
- Protein Conformation
- Substrate Specificity
- Temperature
- Thermodynamics
- X-Ray Diffraction