PMID:2121725

Citation	Kamitori, S, Okamoto, A, Hirotsu, K, Higuchi, T, Kuramitsu, S, Kagamiyama, H, Matsuura, Y and Katsube, Y (1990) Three-dimensional structures of aspartate aminotransferase from Escherichia coli and its mutant enzyme at 2.5 A resolution. J. Biochem. 108:175-84
Abstract	The structure of Escherichia coli aspartate aminotransferase complex with the inhibitor 2-methylaspartate, and that of the mutant enzyme in which an arginine was substituted for a lysine residue thereby forming a Schiff base with the coenzyme pyridoxal 5'-phosphate, were determined at 2.5 A resolution, by the molecular replacement method using the known structure of pig cytosolic aspartate aminotransferase. The enzyme catalyzes the reversible transamination between L-aspartate and alpha-ketoglutarate, and forms a dimeric structure of two identical subunits. Each subunit comprises two domains, a small and a large one. Although, in general, the overall and secondary structure of E. coli enzyme are similar to those of higher animals, some differences of enzymatic action between the enzyme from E. coli and those from higher animals could be explained on the basis of the X-ray structures and molecular mechanics calculation based on them.
Links	PubMed
Keywords	Amino Acids/analysis; Animals; Arginine/analysis; Aspartate Aminotransferases/chemistry; Aspartate Aminotransferases/genetics; Chemistry, Physical; Crystallography; Escherichia coli/enzymology; Escherichia coli/genetics; Kinetics; Lysine/analysis; Mutation; Physicochemical Phenomena; Protein Conformation; Schiff Bases; Swine; X-Ray Diffraction
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