title: Novel properties of γ-glutamyltransferase from Pseudomonas syringae with β-aspartyltransferase activity.
abstract: OBJECTIVE
  Gene cloning, purification, and characterization of γ-glutamyltransferase from Pseudomonas syringae (PsGGT) were performed in Escherichia coli.
  
  
  RESULTS
  PsGGT was partially purified to 13-fold, with a specific activity of 0.92 U/mg. The molecule is presumed to be a heterodimeric consisting of large (37 kDa) and small (21 kDa) subunits. The optimal pH and temperature for hydrolytic activity were 8 and 37 °C, and those for transfer activity were 9 and 50 °C, respectively. PsGGT could transfer β-aspartyl moiety from asparagine to hydroxylamine and the γ-glutamyl moiety from glutamine to hydroxylamine.
  
  
  CONCLUSIONS
  PsGGT demonstrated novel functionality on both γ-glutamyltransferase and β-aspartyltransferase.
authors.affiliation: Department of Biotechnology, Graduate School of Life Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga, 525-8577, Japan.
authors.forename: Asep A
authors.initials: AA
authors.lastname: Prihanto
authors.affiliation: Household Division, Kobayashi Pharmaceutical Co., Ltd., Osaka, Japan.
authors.forename: Yuki
authors.initials: Y
authors.lastname: Nonomura
authors.affiliation: Department of Applied Chemistry Graduate School of Life Sciences, Ritsumeikan University, Kusatsu, Japan.
authors.forename: Kazuyoshi
authors.initials: K
authors.lastname: Takagi
authors.affiliation: Department of Biotechnology, Graduate School of Life Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga, 525-8577, Japan.
authors.forename: Ryosuke
authors.initials: R
authors.lastname: Naohara
authors.affiliation: Department of Biotechnology, Graduate School of Life Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga, 525-8577, Japan.
authors.forename: Midori
authors.initials: M
authors.lastname: Umekawa
authors.affiliation: Department of Biotechnology, Graduate School of Life Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga, 525-8577, Japan. wakayama@sk.ritsumei.ac.jp.
authors.forename: Mamoru
authors.initials: M
authors.lastname: Wakayama
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D044224:Pseudomonas syringae / Q000201:enzymology*; D016415:Sequence Alignment; D013696:Temperature; D014166:Transferases / Q000378:metabolism*; D005723:gamma-Glutamyltransferase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D014166:Transferases; D005723:gamma-Glutamyltransferase
keywords: Pseudomonas syringae; β-Aspartyl hydroxamate; β-Aspartyltransferase; γ-Glutamyltransferase