EC Number |
Reaction |
Reference |
---|
2.7.1.1 | ATP + D-glucose = ADP + D-glucose 6-phosphate |
cutting-edge high-resolution nuclear magnetic resonance methods are used to explore the kinetic properties of glucokinase. Glucokinase samples a range of conformational states in the absence of glucose. In the presence of glucose or a small-molecule activator, the enzyme population shifts towards a more narrow, well-structured ensemble of states |
723509 |
2.7.1.1 | ATP + D-glucose = ADP + D-glucose 6-phosphate |
positive cooperation, mechanism |
663409 |
2.7.1.1 | ATP + D-glucose = ADP + D-glucose 6-phosphate |
using intrinsic tryptophan fluorescence a conformational change induced by the binding of adenine nucleotides to human pancreatic glucokinase is determined. The molecular dynamic simulations indicate that the binding triggers molecular motion of the flexible surface /active site loop and partial closure of the interdomain active site cleft. The modelled structure of the hGK-ATP binary complex shows the residue contacts involved in ATP binding at the active site |
722237 |
2.7.1.1 | ATP + D-hexose = ADP + D-hexose 6-phosphate |
- |
- |
2.7.1.1 | ATP + D-hexose = ADP + D-hexose 6-phosphate |
catalytic residues in the D-glucose binding site are Glu269, Glu302, and Asp211 |
662581 |
2.7.1.1 | ATP + D-hexose = ADP + D-hexose 6-phosphate |
equilibrium random Bi Bi mechanism with formation of the abortive enzyme-ADP-glucose complex |
-, 287006 |
2.7.1.1 | ATP + D-hexose = ADP + D-hexose 6-phosphate |
non-cooperative conditions shows an ordered kinetic mechanism with MgADP as the last product to be released |
660949 |
2.7.1.1 | ATP + D-hexose = ADP + D-hexose 6-phosphate |
random kinetic mechanism |
640209 |
2.7.1.1 | ATP + D-hexose = ADP + D-hexose 6-phosphate |
random process |
640249 |
2.7.1.1 | ATP + D-hexose = ADP + D-hexose 6-phosphate |
random sequential mechanism |
640251 |