Fructose Bisphosphate Aldolase

From Proteopedia

Fructose biphosphate aldolase Fructose biphosphate aldolase is an enzyme in glycolysis. It catalyzes the breakdown of fructose-1,6-biophosphate into dihydroxyacetone phosphate (DHAP) and glyceraldehyde-2-phosphate (GAP). The reaction is an aldol cleavage, or otherwise termed, retro aldo condensation. Catalysis occurs by the formation of a Schiff base (an imine resulting from a ketone and amine) from the amine of the aldolase's Lys229 and the open-ring form of FBP accompanied by stabilization from Asp33. <refname="jmol">Jmol: an open-source Java viewer for chemical structures in 3D. http://www.jmol.org/Cite error: Invalid <ref> tag; refs with no content must have a name Aldol cleavage produces GAP and an enamine precursor to DHAP. Tautomerization, protonation and the hydrolysis of the Schiff base produce the final product of DHAP and the active enzyme.^[1]