产气克雷伯菌的谷氨酰胺合成酶：缺乏尿苷酰转移酶的glnD突变体的特性
Glutamine synthetase of Klebsiella aerogenes: properties of glnD mutants lacking uridylyltransferase.
作者信息
Foor F, Cedergren R J, Streicher S L, Rhee S G, Magasanik B
出版信息
J Bacteriol. 1978 May;134(2):562-8. doi: 10.1128/jb.134.2.562-568.1978.
Abstract
The glnD mutation of Klebsiella aerogenes is cotransducible by phage P1 with pan (requirement for pantothenate) and leads to a loss of uridylytransferase and uridylyl-removing enzyme, components of the glutamine synthetase adenylylation system. This defect results in an inability to deadenylylate glutamine synthetase rapidly and in a requirement for glutamine for normal growth. Suppression of the glnD mutation are located at the glutamine synthetase structural gene glnA.
摘要
产气克雷伯菌的glnD突变可被噬菌体P1与泛酸（泛酸需求）共转导，并导致尿苷酰转移酶和尿苷酰去除酶的缺失，这两种酶是谷氨酰胺合成酶腺苷酸化系统的组成部分。这种缺陷导致无法迅速使谷氨酰胺合成酶去腺苷酸化，并导致正常生长需要谷氨酰胺。glnD突变的抑制位于谷氨酰胺合成酶结构基因glnA处。
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本文引用的文献
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