大肠杆菌K-12中L-丝氨酸脱氨酶的体外和体内激活
In vitro and in vivo activation of L-serine deaminase in Escherichia coli K-12.
作者信息
Newman E B, Dumont D, Walker C
出版信息
J Bacteriol. 1985 Jun;162(3):1270-5. doi: 10.1128/jb.162.3.1270-1275.1985.
Abstract
Escherichia coli L-serine deaminase (L-SD) in crude extracts made in glycylglycine could be activated by incubation with iron sulfate and dithiothreitol. This activation could also be demonstrated in vitro in two mutants which were physiologically deficient in L-SD activity in vivo. This suggests that these mutants were deficient not in L-SD but in an enzyme(s) activating L-SD. The suggestion is made that production of a functional L-SD in vivo requires activation of the structural gene product by an enzyme or enzymes that reduce the protein to an active form.
摘要
在甘氨酰甘氨酸中制备的粗提物中的大肠杆菌L-丝氨酸脱氨酶（L-SD），可通过与硫酸铁和二硫苏糖醇一起温育来激活。这种激活在两个体内生理上缺乏L-SD活性的突变体中也能在体外得到证实。这表明这些突变体缺乏的不是L-SD，而是激活L-SD的一种或多种酶。有人提出，在体内产生功能性L-SD需要一种或多种酶将结构基因产物还原为活性形式来激活。
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