Glucokinase acts as a glucose sensor in beta cells by regulating the rate of glucose entrance into the glycolytic pathway (glucose phosphorylation) and subsequent metabolism.
Despite the fact that it is a monomeric enzyme, glucokinase has a considerably lower affinity for glucose and exhibits positive cooperativity for this substrate. Glucokinase is a critical enzyme in the liver's capacity to store glucose as glycogen, particularly in the postprandial stage.
The affinity for glucose of glucokinase is lower than that of the other hexokinases. In the physiologically significant range of 4-10 mmol/L (72-180 mg/dL), glucokinase alters shape and/or function in tandem with increasing glucose concentrations. At a glucose content of roughly 8 mmol/L (144 mg/dL), it is half-saturated. It is theorized that glucokinase (GCK) serves as a glucose sensor not only for the regulation of insulin release by pancreatic -cells, but also for the rest of the cells in mammals that contribute to glucose homeostasis.
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