大肠杆菌K-12中L-丝氨酸脱氨酶的研究
Studies on L-serine deaminase in Escherichia coli K-12.
作者信息
Isenberg S, Newman E B
出版信息
J Bacteriol. 1974 Apr;118(1):53-8. doi: 10.1128/jb.118.1.53-58.1974.
Abstract
l-Serine deaminase has been studied in toluene-treated cells of Escherichia coli K-12 and shown to be a discrete entity distinct from l-threonine deaminase. Its level in the cell varies as a function of nitrogen nutrition, carbon source, and amino acids (glycine and leucine). The metabolic role of the enzyme remains unclear but may be related to serine toxicity. The enzyme is unstable within the cell in the presence of its inducers, glycine and leucine, but not in their absence.
摘要
已对甲苯处理过的大肠杆菌K-12细胞中的L-丝氨酸脱氨酶进行了研究，结果表明它是一种与L-苏氨酸脱氨酶不同的独立实体。其在细胞中的水平随氮营养、碳源和氨基酸（甘氨酸和亮氨酸）的变化而变化。该酶的代谢作用尚不清楚，但可能与丝氨酸毒性有关。在其诱导剂甘氨酸和亮氨酸存在的情况下，该酶在细胞内不稳定，但在它们不存在时则稳定。
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