Glucokinase Recombinant Rabbit Monoclonal Antibody [JE33-40]

Function

Glucokinase (EC 2.7.1.2) is an enzyme that facilitates phosphorylation of glucose to glucose-6-phosphate. Glucokinase occurs in cells in the liver and pancreas of humans and most other vertebrates. In each of these organs it plays an important role in the regulation of carbohydrate metabolism by acting as a glucose sensor, triggering shifts in metabolism or cell function in response to rising or falling levels of glucose, such as occur after a meal or when fasting. Mutations of the gene for this enzyme can cause unusual forms of diabetes or hypoglycemia. Glucokinase (GK) is a hexokinase isozyme, related homologously to at least three other hexokinases.[4] All of the hexokinases can mediate phosphorylation of glucose to glucose-6-phosphate (G6P), which is the first step of both glycogen synthesis and glycolysis. However, glucokinase is coded by a separate gene and its distinctive kinetic properties allow it to serve a different set of functions. Glucokinase has a lower affinity for glucose than the other hexokinases do, and its activity is localized to a few cell types, leaving the other three hexokinases as more important preparers of glucose for glycolysis and glycogen synthesis for most tissues and organs. Because of this reduced affinity, the activity of glucokinase, under usual physiological conditions, varies substantially according to the concentration of glucose.

Background References

1. Ashcroft FM et al. Glucokinase activity in diabetes: too much of a good thing? Trends Endocrinol Metab. 2023 Feb

2. Ren Y et al. Glucokinase as an emerging anti-diabetes target and recent progress in the development of its agonists. J Enzyme Inhib Med Chem. 2022 Dec

Subcellular Location

Cytoplasm, Nucleus, Mitochondrion.

UNIPROT

SwissProt: P35557 Human

Synonyms