fructose-bisphosphate aldolase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate. [EC:4.1.2.13]

Fructose-bisphosphate aldolase activity is a critical enzyme in glycolysis and gluconeogenesis, responsible for catalyzing the reversible cleavage of fructose-1,6-bisphosphate (FBP) into glyceraldehyde-3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP). This reaction is a crucial step in carbohydrate metabolism as it provides the necessary intermediates for the production of ATP, NADH, and pyruvate.

The mechanism involves the formation of a Schiff base intermediate between the enzyme's active site lysine residue and the substrate FBP. This Schiff base formation stabilizes the transition state, facilitating the cleavage of the carbon-carbon bond in FBP. The enzyme exhibits a high degree of substrate specificity, selectively binding and cleaving FBP.

Fructose-bisphosphate aldolase activity is essential for maintaining cellular energy homeostasis, regulating glucose metabolism, and supporting various biological processes like muscle contraction, cell growth, and biosynthesis. Its deficiency or dysfunction can lead to metabolic disorders, such as fructose intolerance.'
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Proteins (1)

Compounds (1)