title: Characterization of γ-glutamyl kinase mutants from Saccharomyces cerevisiae.
abstract: We characterized the yeast γ-glutamyl kinase important for proline biosynthesis. Asp154 and Ile150 were involved in the affinity with glutamate as well as proline. The Asp154Asn and Ile150Thr mutants had increased thermostability, in addition to desensitization to proline. Deletion of a C-terminal domain dramatically decreased the reaction rate and stability.
authors.affiliation: Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
authors.forename: Yuki
authors.initials: Y
authors.lastname: Tatehashi
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Takagi
mesh_terms: D000595:Amino Acid Sequence; D004795:Enzyme Stability / Q000235:genetics; D018698:Glutamic Acid / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D050505:Mutant Proteins / Q000235:genetics / Q000378:metabolism*; D017851:Phosphotransferases (Carboxyl Group Acceptor) / Q000235:genetics* / Q000378:metabolism*; D011392:Proline / Q000096:biosynthesis / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D017384:Sequence Deletion / Q000235:genetics
chemical_list: D050505:Mutant Proteins; D018698:Glutamic Acid; D011392:Proline; D017851:Phosphotransferases (Carboxyl Group Acceptor); C020650:glutamate 5-kinase
keywords: PUA domain; Proline synthesis; Saccharomyces cerevisiae; Yeast; γ-Glutamyl kinase