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Glucokinase changes conformation and/or function in parallel with rising glucose concentrations in the physiologically important range of 4–10 M (72–180 mg/dL). It is half-saturated at a glucose concentration of about 8 mM (144 mg/dL). [10] [11] Glucokinase is not inhibited by physiological concentrations of its product, glucose-6-phosphate ...
Glucokinase (GK) is an enzyme that helps in the glycolytic pathway by phosphorylating glucose into glucose-6-phosphate (G6P). It is an isozyme of hexokinase and is found mainly in pancreatic β cells, but also liver, gut, and brain cells where glycolysis cause glucose-induced insulin secretion. [2]
In enzymology, an ADP-specific glucokinase (EC 2.7.1.147) also known as ADP-dependent glucokinase is an enzyme that catalyzes the chemical reaction. ADP + D-glucose AMP + D-glucose 6-phosphate. Thus, the two substrates of this enzyme are ADP and D-glucose, whereas its two products are AMP and D-glucose 6-phosphate.
The glucokinase regulatory protein (GKRP) also known as glucokinase (hexokinase 4) regulator (GCKR) is a protein produced in hepatocytes (liver cells). GKRP binds and moves glucokinase (GK), thereby controlling both activity and intracellular location [1] [2] of this key enzyme of glucose metabolism. [3] GKRP is a 68 kD protein of 626 amino acids.
These loss-of-function mutations result in a glucokinase molecule that is less sensitive or less responsive to rising levels of glucose. The beta cells in MODY 2 have a normal ability to make and secrete insulin, but do so only above an abnormally high threshold (e.g., 126–144 mg/dl, or 7-8 mM).
Glucose Hexokinase ATP ADP Glucose 6-phosphate Glucose-6-phosphate isomerase Fructose 6-phosphate Phosphofructokinase-1 ATP ADP Fructose 1,6-bisphosphate Fructose-bisphosphate aldolase Dihydroxyacetone phosphate + + Glyceraldehyde 3-phosphate Triosephosphate isomerase 2 × Glyceraldehyde 3-phosphate 2 × Glyceraldehyde-3-phosphate dehydrogenase NAD + + P i NADH + H + NAD + + P i NADH + H + 2 ...
Hexokinase/glucokinase, phosphofructokinase, and pyruvate kinase enzymes of glycolysis are replaced with glucose-6-phosphatase, fructose-1,6-bisphosphatase, and PEP carboxykinase/pyruvate carboxylase. These enzymes are typically regulated by similar molecules, but with opposite results.
The gene product is a regulatory protein that inhibits glucokinase in liver and pancreatic islet cells by binding non-covalently to form an inactive complex with the enzyme. This gene is considered a susceptibility gene candidate for a form of maturity onset diabetes of the young (MODY). [provided by RefSeq, Jul 2008].