Deleo A B, Magasanik B
J Bacteriol. 1975 Jan;121(1):313-9. doi: 10.1128/jb.121.1.313-319.1975.
Mutations at two sites of the Klebsiella aerogenes chromosome, unlinked by transduction with phages PW52 and P1, result in the lack of enzymatically active glutamine synthetase. A mutation in the glnB site leads to a marked decrease in the formation of an apparently normal enzyme. Some of the mutations in the glnA site lead to the production of enzymatically inactive material capable of reacting with anti-glutamine synthetase serum. The revertant of a glnA mutant was found to produce a glutamine synthetase with less activity and less stability to heat than the enzyme of the wild type. These results locate the structural gene to the production of enzymatically inactive glutamine synthetase antigen, not subject to repression by exogenously added ammonia. This observation suggests that glutamine synthetase is itself involved in the regulation of the synthesis of glutamine synthetase.
产气克雷伯菌染色体上两个位点发生突变，通过噬菌体PW52和P1转导不连锁，导致缺乏酶活性的谷氨酰胺合成酶。glnB位点的突变导致明显正常的酶形成显著减少。glnA位点的一些突变导致产生能够与抗谷氨酰胺合成酶血清反应的无酶活性物质。发现glnA突变体的回复体产生的谷氨酰胺合成酶比野生型酶的活性更低且热稳定性更差。这些结果将无酶活性的谷氨酰胺合成酶抗原产生的结构基因定位，该基因不受外源添加氨的抑制。这一观察结果表明谷氨酰胺合成酶本身参与谷氨酰胺合成酶合成的调节。
