title: Altering the substrate specificity of glutamate dehydrogenase from Bacillus subtilis by site-directed mutagenesis.
abstract: The Lys80, Gly82 and Met101 residues of glutamate dehydrogenase from Bacillus subtilis were mutated into a series of single mutants. The wild-type enzyme was highly specific for 2-oxoglutarate, whereas G82K and M101S dramatically switched to increased specificity for oxaloacetate with kcat values 3.45 and 5.68 s-1, which were 265-fold and 473-fold higher respectively than those for 2-oxoglutarate.
authors.affiliation: Department of Life Science and Biotechnology, Faculty of Life and Environmental Science, Shimane University, Shimane 690-8504, Japan.
authors.forename: Iqbal Hassan
authors.initials: IH
authors.lastname: Khan
authors.forename: Hyeung
authors.initials: H
authors.lastname: Kim
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Ashida
authors.forename: Takahiro
authors.initials: T
authors.lastname: Ishikawa
authors.forename: Hitoshi
authors.initials: H
authors.lastname: Shibata
authors.forename: Yoshihiro
authors.initials: Y
authors.lastname: Sawa
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D001665:Binding Sites / Q000502:physiology; D005969:Glutamate Dehydrogenase / Q000737:chemistry* / Q000235:genetics* / Q000502:physiology; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D013379:Substrate Specificity / Q000235:genetics
chemical_list: D005969:Glutamate Dehydrogenase