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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 ...
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.
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]
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].
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.
d -Glucose + 2 [NAD] + + 2 [ADP] + 2 [P] i 2 × Pyruvate 2 × + 2 [NADH] + 2 H + + 2 [ATP] + 2 H 2 O Glycolysis pathway overview The use of symbols in this equation makes it appear unbalanced with respect to oxygen atoms, hydrogen atoms, and charges. Atom balance is maintained by the two phosphate (P i) groups: Each exists in the form of a hydrogen phosphate anion, dissociating to contribute ...
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).
Enzyme denaturation is normally linked to temperatures above a species' normal level; as a result, enzymes from bacteria living in volcanic environments such as hot springs are prized by industrial users for their ability to function at high temperatures, allowing enzyme-catalysed reactions to be operated at a very high rate.