FBP2 Human

FBP2 catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations like magnesium (Mg²⁺). This reaction is a key step in gluconeogenesis and glycogen synthesis from carbohydrate precursors such as lactate . The enzyme is subject to complex allosteric regulation, with AMP acting as an allosteric inhibitor and fructose 2,6-bisphosphate acting as a competitive inhibitor .

FBP2 is a moonlighting protein, meaning it performs multiple functions beyond its primary enzymatic activity. It binds to three Mg²⁺ ions per subunit and can exist in different conformational states, including an active R-state and an inactive T-state . The enzyme’s activity is regulated by various factors, including the NAD/NADH ratio, which influences the dimer/tetramer ratio of FBP2 .

Recent studies have shown that FBP2 plays a crucial role in the induction and maintenance of long-term potentiation (LTP), a molecular basis for memory formation. FBP2 interacts with neuronal mitochondria and CaMK2, and its activity is essential for the early and late phases of LTP .

Recombinant human FBP2 is produced using recombinant DNA technology, which involves inserting the human FBP2 gene into a suitable expression system, such as E. coli, to produce the enzyme in large quantities. This recombinant enzyme is used in various research applications to study its biochemical properties, regulatory mechanisms, and role in metabolic pathways .