GCK Human

Glucokinase, also known as Hexokinase-4 (HK4), is a crucial enzyme in glucose metabolism. It plays a significant role in regulating blood glucose levels by catalyzing the phosphorylation of glucose to glucose-6-phosphate, the first step in glycolysis. This enzyme is predominantly found in the liver and pancreatic beta-cells, where it acts as a glucose sensor and regulates insulin secretion.

Glucokinase is distinct from other hexokinases due to its lower affinity for glucose and its lack of inhibition by glucose-6-phosphate. This allows it to remain active even when glucose levels are high, making it an essential regulator of glucose homeostasis. The enzyme’s activity is modulated by insulin and glucagon, with insulin promoting its activation and glucagon inhibiting it .

Mutations in the gene encoding glucokinase (GCK) can lead to various metabolic disorders. For instance, variants that decrease GCK activity can cause elevated fasting glucose levels, a condition known as Glucokinase-Maturity-Onset Diabetes of the Young (GCK-MODY). This form of diabetes is often misdiagnosed as type 1 or type 2 diabetes, leading to unnecessary treatments . Conversely, hyperactive variants of GCK can result in hyperinsulinemic hypoglycemia .

Recombinant human glucokinase is produced using E. coli expression systems and is often tagged with His-tags for purification purposes. This recombinant protein is used in various research applications, including studies on glucose metabolism, diabetes, and drug development .

Recombinant human glucokinase is a valuable tool in biochemical and medical research. It helps in understanding the enzyme’s role in glucose metabolism and its implications in metabolic disorders. Additionally, it is used in drug screening assays to identify potential therapeutic agents targeting glucokinase activity .