Evolution of Enzymatic Activities in the Enolase Superfamily: Identification of the General Acid Catalyst in the Acitive Site of D-Glucarate Dehydratase from Escherichia coli

摘要

D-Glucarate dehydratase from Escherichia coli (GlucD), a member of the enolase superfamily, catalyzes the dehydration of both D-glucarate and L-idarate to form 5-keto-4-deoxy-D-glucarate (KDG).