Crystallography and mutagenesis of transketolase: mechanistic implications for enzymatic thiamin catalysis

Abstract

The ThDP dependent enzyme transketolase is a convenient model system to study enzymatic thiamin catalysis. Crystallographic studies of the enzyme have identified the ThDP binding fold, the V-conformation of ThDP as the relevant conformation in enzymatic catalysis and details of enzyme–substrate interactions. Based on this structural information, the function of various active site residues in substrate binding and catalysis has been probed by site-directed mutagenesis.