Transaldolase (EC: 2.2.1.2) catalyzes the reversible transfer of a three-carbon ketol unit from sedoheptulose 7-phosphate to glyceraldehyde 3-phosphate to form erythrose 4-phosphate and fructose 6-phosphate. This enzyme, together with transketolase, provides a link between the glycolytic and pentose-phosphate pathways. Transaldolase is an enzyme of about 34 Kd whose sequence has been well conserved throughout evolution. A lysine has been implicated [PMID:8109173] in the catalytic mechanism of the enzyme; it acts as a nucleophilic group that attacks the carbonyl group of fructose-6-phosphate.

Transaldolase is evolutionary related [PMID:7773398] to a bacterial protein of about 20 Kd (known as talC in Escherichia coli, INTERPRO: IPR004731), whose exact function is not yet known.