Fructose-bisphosphate aldolase (Aldolase (FBP-aldolase))

Fructose-bisphosphate aldolase (FBP-aldolase; EC 4.1.2.13) is a key glycolytic enzyme that catalyzes the reversible cleavage of fructose 1,6-bisphosphate to dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). It plays an essential role in both glycolysis and gluconeogenesis, and is present in most organisms, with three main isozymes in vertebrates: Aldolase A (muscle and red blood cells), Aldolase B (liver, kidney, and small intestine), and Aldolase C (brain). Aldolase is divided mechanistically into class I (predominant in animals and plants, utilizing a Schiff base mechanism with an active-site lysine) and class II (bacterial and fungal, requiring a divalent metal ion such as zinc). Human diseases associated with aldolase deficiencies include hereditary fructose intolerance (aldolase B defect) and hemolytic anemia (aldolase A defect). In cancer, aldolase is often upregulated in the context of increased glycolysis (the Warburg effect). While the enzyme itself is not yet a major direct drug target in human medicine, its homologs in pathogens are being investigated for antimicrobial development.

Other names

AldolaseFructose-1,6-bisphosphate aldolaseAldolase A (muscle isozyme)Aldolase B (liver isozyme)Aldolase C (brain isozyme)FBP-aldolase

Enzyme inhibition (blocking glycolytic or gluconeogenic activity) Inhibitors often act on the active site (lysine/schiff base, or metal ion binding for class II enzymes)