Escherichia coli Aspartate Aminotransferase: Effects of Site-Specific Mutations on Substrate Binding and Catalysis

Crystal Structure of the Closed Form of Chicken Cystosolic Aspartate Aminotransferase at 1.9 Å Resolution

“…N. Jansonius et al, unpublished results). In addition to a long history of classical solution studies (for a review, see Christen & Metzler, 1985), more recent site-directed mutagenesis analyses, capitalizing on the X-ray crystallographic successes, have delineated the mechanistic roles of most active site residues (Malcolm & Kirsch, 1985;Cronin & Kirsch, 1988;Toney & Kirsch, 1987, 1991Goldberg et al, 1991;Kuramitsu et al, 1991;Hayashi et al, 1991;Inoue et al, 1991;Ziak et al, 1993). cAATase from chicken heart is an a 2 dimer with 411 amino acid residues per subunit (M r 2 × 46,500).…”