title: Aspartate aminotransferase of E. coli: effects of site-directed mutagenesis on substrate recognition.
abstract: R292 is crucial for both the binding and the catalysis of the transamination reaction of dicarboxylic acid substrates. Substitution of R292 to uncharged residues greatly enhanced the catalytic efficiency of transamination of neutral amino acids without any effect on the binding. Residues at position 292 may not be involved in recognition of the neutral side chain. The indole ring of W140 not only regulates the rotational movement of the coenzyme ring during catalysis, but it also may be involved in binding the carboxyl side chain of dicarboxylic substrates. The phenol group of Y70 is essential for the stabilization of the transition states with all substrates. Benzene ring at position 70 is necessary to recognize the glutamate-2-oxoglutarate substrate pair.
authors.affiliation: Department of Medical Chemistry, Osaka Medical College, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Kagamiyama
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D001219:Aspartate Aminotransferases / Q000235:genetics* / Q000378:metabolism; D001665:Binding Sites / Q000502:physiology; D002384:Catalysis; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D013379:Substrate Specificity
chemical_list: D000596:Amino Acids; D001219:Aspartate Aminotransferases