Class II fructose-bisphosphate aldolase

Class II fructose-bisphosphate aldolase is an enzyme found predominantly in bacteria, fungi, and some protists, where it catalyzes a key glycolytic and gluconeogenic step—the reversible cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate[1][3][5][7]. Unlike class I aldolases (common in animals and plants), class II aldolases require a divalent metal ion, typically zinc, for catalysis, enabling polarization of the substrate carbonyl group[1][3][5]. The enzyme adopts a TIM barrel (α/β)_8 fold and features a bimetallic active site architecture[1]. Class II aldolase is of interest as a drug target in infectious diseases because it is absent in mammals; selective inhibitors (especially metal chelators) have been explored to block metabolic pathways in pathogens without affecting the host[6]. No widely used clinical inhibitors exist yet, but research focuses on such molecules for the treatment of bacterial, fungal, and protozoal infections[6].

Other names

Fructose-1,6-bisphosphate aldolase (Class II)FBP-aldolase (Class II)FBA (Class II)D-glyceraldehyde-3-phosphate lyase (Class II)EC 4.1.2.13 (Class II)

Inhibition by metal chelation (blocking divalent cation, usually zinc, required for enzymatic activity); Substrate analogs (competitive binding to active site)