Article
Kinetic and conformational effects of lysine substitutions for arginines 35 and 87 in the active site of staphylococcal nuclease.
Biochemistry - 17 Apr 1990
Pourmotabbed T, Dell'Acqua M, Gerlt J A, Stanczyk S M, Bolton P H
Abstract excerpt
The high-resolution X-ray crystal structure of staphylococcal nuclease (SNase) suggests that the guanidinium groups of Arg 35 and Arg 87 participate as electrophilic catalysts in the attack of water on the substrate phosphodiester. Both arginine residues have been replaced with "conservative" lys...
Topics
- Arginine
- Binding Sites
- Calcium
- Catalysis
- Escherichia coli
- Hot Temperature
- Kinetics
- Lysine
- Magnetic Resonance Spectroscopy
- Micrococcal Nuclease
- Mutation
- Protein Conformation
- Protein Denaturation