Properties of Crystalline Glutamine Synthetase from Gluconobacter suboxydans Grown on Glutamate as a Nitrogen Source : Amino Acid Metabolism in Acetic Acid Bacteria (XI)

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概要

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• The optimum pH of the glutamine forming (synthesizing) reaction of glutamine synthetase from Gluconobacter suboxydans IFO 3172 was 8.0-8.5; that of the γ-glutamyl-hydroxamate-forming (transferring) reaction was 9.5. The activity ratio (transferringreaction/synthesizing reaction) was 2.8 at pH 8.5. The enzyme specifically required glutamate as an amino acid in the synthesizing reaction. dATP showed 67 and CTP 10% of the reactivity of ATP. Hydroxylamine could be substituted for ammonia with 33% reactivity. K_m values for glutamate, ATP and ammonia were 4.2,1.6 and 1.1 mM, respectively. Mg^<2+> was more effective as a cofactor in the synthesizing reaction than Mn^<2+> or Co^<2+>. However, their effects varied with their concentration and the pH of the reaction mixture : Mn^<2+> and Co^<2+> respectively showed 1 and 20% reactivity of Mg^<2+> at 30 mM concentration at pH 8.5 but 40 and 150% at 5 mM and pH 7.0. The metal saturation curves at fixed amounts of ATP were sigmoidal. Addition of a small amount of Co^<2+> stimulated the activity in the presence of suboptimal levels of Mg^<2+> or Mn^<2+>. The enzyme was inhibited by such metabolites as glycine, alanine, serine and adenine derivatives. Cumulative inhibition was observed with mixtures of inhibitors.

• 社団法人日本生物工学会の論文
• 1983-02-25

著者

• TACHIKI TAKASHI

  Department of Food Science and Technology, Kyoto University

• TOCHIKURA TATSUROKURO

  Department of Food Science and Technology, Kyoto University

• Tochikura Tatsurokuro

  Department Of Agricultural Chemistry Kyoto University

• TOKORO KAZUMI

  Department of Food Science and Technology, Kyoto University

• Tachiki Takashi

  Department Of Bioscience & Technology Faculty Of Science & Engineering Ritsumeikan Universit

• Tokoro Kazumi

  Department Of Food Science And Technology Kyoto University

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