Article
Roles of cysteinyl residues of phosphoribulokinase as examined by site-directed mutagenesis.
The Journal of biological chemistry - 5 Jun 1991
Milanez S, Mural R J, Hartman F C
Abstract excerpt
The Calvin Cycle enzyme phosphoribulokinase is activated in higher plants by the reversible reduction of a disulfide bond, which is located at the active site. To determine the possible contribution of the two regulatory residues (Cys16 and Cys55) to catalysis, site-directed mutagenesis has been used to replace each of them in the spinach enzyme with serine or alanine. The only other cysteinyl residues of the...
Topics
- Base Sequence
- Blotting, Western
- Cysteine
- DNA
- Electrophoresis, Polyacrylamide Gel
- Ethylmaleimide
- Kinetics
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Phosphotransferases