FBP1 Human

Fructose-1,6-Bisphosphatase 1 (FBP1) is a crucial enzyme in the gluconeogenesis pathway, which is the metabolic process that generates glucose from non-carbohydrate substrates. This enzyme is encoded by the FBP1 gene in humans and plays a significant role in maintaining blood sugar levels during fasting.

FBP1 catalyzes the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate. This reaction is a key regulatory step in gluconeogenesis, making FBP1 a rate-limiting enzyme in this pathway . The enzyme requires divalent cations, such as magnesium ions, for its activity .

FBP1 can exist in two states: an active R-state and an inactive T-state. The transition between these states is regulated by various metabolic signals, ensuring that glucose production is tightly controlled according to the body’s needs .

FBP1 is primarily expressed in the liver, where it plays a pivotal role in glucose homeostasis. It is also involved in regulating glucose sensing and insulin secretion in pancreatic beta-cells . Additionally, FBP1 modulates glycerol gluconeogenesis in the liver, contributing to the overall regulation of glucose levels in the blood .

Deficiency in FBP1 activity can lead to a rare metabolic disorder known as Fructose-1,6-Bisphosphatase Deficiency. This condition is characterized by hypoglycemia and metabolic acidosis, particularly during periods of fasting or illness . Patients with this deficiency may experience symptoms such as lethargy, seizures, and developmental delays.

Recombinant FBP1 is produced using various expression systems, including yeast, E. coli, and mammalian cells . The recombinant protein is often used in research to study the enzyme’s structure, function, and regulatory mechanisms. It is also utilized in the development of therapeutic strategies for metabolic disorders involving gluconeogenesis .