• 미생물학회지
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• 제26권2호
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• pp.93-100
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• 1988

In order to understand the regulation of glutamate dehydrogenase(GDH) synthesis in Brevibacterium flavum, we have isolated a mutant lacking NADP-linked GDH activity by ethlmethane sulfonate treatment. The $gdh^-$ mutant was grown on the minimal plate with 1mM ammonium chloride and not that with 300mM ammonium chloride. The cell-free extracts from $gdh^-$ mutant and prototroph were also examined with glutamine synthetase(GS) and glutamate synthase (GOGAT) production by niteogen sources. The growth of $gdh^-$ mutant in presence of 20mM ammonium chloride means that GOGAT synthesis is sufficient to allow growth in this condition. GS production of $gdh^-$ mutant as well as parental strain was induced by 1mM urea and ammonium tartrate, but it was repressed by higher concentration of ammonia, and also induced by 20mM to 50mM glutamate as a substrate. It was special attention that GOGAT synthesis from $gdh^-$ strain was more repressed by higher concentration of ammonia than prototroph as described in E. coli system.

• 미생물학회지
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• 제27권3호
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• pp.304-309
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• 1989

광합성 세균인 Rhodopseudomonus sphaeroiders의 질소고정 효소 합성 및 암모니아 동화 경로에 중요한 glutamine synthetase(GS), glutamate synthase(GOGAT) 및 glutamatc dehydrogenase(GDH) 활성에 미치는 TriazinerP 제초제인 simazine의 영향을 조사하였다. 배양중에 simazine을 처리할 경우 성장 및 in vivo 질소고정효소의 합성 및 GS의 합성이 크게 저해되었다. 그리고 정상 배지에서 배양한 Rp. sphaeroides의 GOGAT 및 GDH의 활성이 GS의 활성보다 simazinc에 의해 더 큰 저해를 받았다. 이상의 결과는 simazine이 Rp. sphacroides의 광합성 과정을 억제하여, 질소고정효소의 합성을 저해하며 이로인해 GS의 합성이 저해될 가능성이 있음을 시사한다고 하겠다.