Article
Rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Properties of phospho- and dephospho- forms and of two mutants in which Ser32 has been changed by site-directed mutagenesis.
The Journal of biological chemistry - 5 Mar 1992
Kurland I J, el-Maghrabi M R, Correia J J, Pilkis S J
Abstract excerpt
The mechanism by which cAMP-dependent protein kinase-catalyzed phosphorylation modulates the activities of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase was examined after site-specific mutation of the cAMP-dependent phosphorylation site (Ser32) to aspartic acid or alanine. The mutant and wild-type enzymes were overexpressed in Escherichia coli in a rich medium to levels as high as 30 mg/liter and were...
Topics
- Animals
- Circular Dichroism
- Electrophoresis, Polyacrylamide Gel
- Kinetics
- Liver
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Peptide Mapping
- Phosphofructokinase-2