Glycolysis Enzymes: Difference between revisions

[[Austin_Drake_Sandbox|Aldolase]] catalyzes the retro-aldol cleavage of <scene name='39/392339/Cv1/2'>fructose 1,6-bisphosphate</scene> into two three-carbon phosphosugars, <scene name='39/392339/Cv1/3'>dihydroxyacetone phosphate</scene> and <scene name='39/392339/Cv/10'>glyceraldehyde-3-phosphate</scene>.

The reaction is an aldol cleavage, or otherwise termed, retro aldo condensation.  Catalysis occurs first when the nucleophilic ε-amine group of Lys229 attacks the carbonyl carbon of the substrate (FBP) in its open-ring state, pushing an electron pair to the oxygen of the carbonyl. The oxygen is protonated and leaves as water as a protonated <scene name='Austin_Drake_Sandbox/Schiff_base/2'>Schiff base</scene> is produced (an imine resulting from a ketone and amine) with the open-ring form of FBP  

First, [[Nathan_Line_sandbox_3|glyceraldehyde-3-phosphate dehydrogenase]] oxidizes <scene name='39/392339/Cv/11'>glyceraldehyde-3-phosphate</scene>, transferring a hydride to NAD+, generating NADH and H+. A phosphate ion is used instead of a water molecule, leading to the formation of <scene name='39/392339/Cv/12'>1,3-bisphosphoglycerate</scene>, a high energy compound.