Enzymes Concerned in the Conversion of _L-Glutamic Acid Fermentation to _L-Glutamine and N-Acetyl-_L-Glutamine Fermentation by Corynebacterium glutamicum
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The mechanism of the conversion of _L-glutamic acid fermentation to _L-glutamine and N-acetyl-_L-glutamine (N-AGM) fermentation by Corymebacterium glutamicum was studied by investigating the enzymes concerned in the synthesis and decomposition of _L-glutamine and N-AGM. Activities of _L-glutamine and N-AGM synthetases were each separated into two protein fractions by column chromatography on DEAE-cellulose, while, the _L-glutaminase activity was similarly separated into three protein fractions and N-AGM deacetylase activity was separated into two protein fractions of which one was active and the other was slightly active. Either Mn^<2+> or Mg^<2+> was confirmed to serve as an activator for all the _L-glutamine and N-AGM synthetases. With Mn^<2+>, Zn^<2+> remarkably stimulated the activities of both _L-glutamine synthetases I and II whereas with Mg^<2+>, the activity of _L-glutamine synthetase II was stimulated by Zn<2+> but that of the synthetase I was little increased by any concentration of Zn^<2+>. With Mn^<2+>, activities of N-AGM synthetases I and II were slightly stimulated by Zn^<2+>, and with Mg^<2+>, the activity of N-AGM synthetase I was not increased by any level of Zn^<2+> though that of N-AGM synthetase II was slightly stimulated by the ion. On the other hand, Zn^<2+> significantly inhibited the activities of all the three _L-glutaminases and strongly inhibited the activity of N-AGM deacetylase.The role of Zn^<2+> in the produciton of _L-glutamine and N-AGM is discussed in the light of the observation that Zn^<2+> promotes the enzymatic synthesis of _L-glutamine more effectively than that of N-AGM, and in addition, the ion significantly suppresses the decomposition of both _L-glutamine and N-AGM.
- 公益社団法人日本生物工学会の論文
- 1978-12-25
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