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Fructose-1,6-bisphosphate is the glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate. This is a key step in the glycolytic cycle. The conversion from fructose -1,6-bisphosphate is dependent on the formation of a schiff base intermediate (see mechanism). Lysine 229 is responsible for the schiff base formation in human aldolase. In the natural state, aldolase forms a tetramer. Each subunit of the enzyme contains one alpha/beta barrel which contains the active site. The alpha/beta barrel is a series of alpha helices and beta sheets that alternate to form a beta barrel with parallel beta sheets. The C-terminal amino acids are also very involved in the reaction. In all forms of aldolase the terminal tyrosine has been conserved.

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