Article
Hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Use of site-directed mutagenesis to evaluate the roles of His-258 and His-392 in catalysis.
The Journal of biological chemistry - 15 Sept 1990
Tauler A, Lin K, Pilkis S J
Abstract excerpt
The current model for hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase divides the protein into two functional domains: an N-terminal kinase domain and a carboxyl-terminal bisphosphatase domain. Site-directed mutagenesis was used to evaluate the role of two putative bisphosphatase act...
Topics
- Amino Acid Sequence
- Animals
- Base Sequence
- Binding Sites
- Escherichia coli
- Histidine
- Kinetics
- Liver
- Models, Structural
- Molecular Sequence Data
- Multienzyme Complexes
- Mutation
- Oligonucleotide Probes
- Phosphofructokinase-2
- Phosphoric Monoester Hydrolases
- Phosphorylation
- Phosphotransferases
- Recombinant Proteins