Article
Identification of fructose 6-phosphate- and fructose 1-phosphate-binding residues in the regulatory protein of glucokinase.
The Journal of biological chemistry - 8 Mar 2002
Veiga-da-Cunha Maria, Van Schaftingen Emile
Abstract excerpt
Glucokinase is inhibited in the liver by a regulatory protein (GKRP) whose effects are increased by Fru-6-P and suppressed by Fru-1-P. To identify the binding site of these phosphate esters, we took advantage of the homology of GKRP to the isomerase domain of GlmS (glucosamine-6-phosphate synthase) and created 12 different mutants of rat GKRP. Mutations of three residues predicted to bind to Fru-6-P resulted in...
Topics
- Amino Acid Sequence
- Animals
- Binding Sites
- Cloning, Molecular
- Cysteine
- Dose-Response Relationship, Drug
- Electrophoresis, Polyacrylamide Gel
- Fructosephosphates
- Glucokinase
- Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)
