鼠伤寒沙门氏菌中蛋氨酸控制的高丝氨酸脱氢酶的证据。
Evidence for a methionine-controlled homoserine dehydrogenase in Salmonella typhimurium.
作者信息
Cafferata R L, Freundlich M
出版信息
J Bacteriol. 1969 Jan;97(1):193-8. doi: 10.1128/jb.97.1.193-198.1969.
Abstract
Evidence is presented for the existence of a second homoserine dehydrogenase in Salmonella typhimurium. The formation, but not the activity, of this enzyme is controlled by methionine. Two distinct homoserine dehydrogenases were separated from wild-type cells by diethylaminoethyl (cellulose) column chromatography. Sucrose gradient ultracentrifugation gave molecular weight estimates for the threonine-regulated enzyme (HSD I) of 220,000 to 240,000 and for the methionine controlled enzyme (HSD II) of 130,000 to 140,000. Approximately 12% of the total HSD activity in wild-type cells was accounted for by HSD II. A threonine-requiring strain of S. typhimurium was found to lack HSD I but not HSD II. Under certain conditions, this mutant grew rapidly in minimal medium. Rapid growth in minimal medium was correlated with the appearance of an enzyme with similar characteristics to HSD I. The possible origins of this HSD I-like enzyme are presented.
摘要
有证据表明鼠伤寒沙门氏菌中存在第二种高丝氨酸脱氢酶。该酶的形成而非活性受甲硫氨酸控制。通过二乙氨基乙基（纤维素）柱色谱法从野生型细胞中分离出两种不同的高丝氨酸脱氢酶。蔗糖梯度超速离心法得出，苏氨酸调节的酶（HSD I）分子量估计为220,000至240,000，甲硫氨酸控制的酶（HSD II）分子量估计为130,000至140,000。野生型细胞中约12%的总HSD活性由HSD II负责。发现一株需要苏氨酸的鼠伤寒沙门氏菌菌株缺乏HSD I但不缺乏HSD II。在某些条件下，该突变体在基本培养基中生长迅速。在基本培养基中的快速生长与一种具有与HSD I相似特征的酶的出现相关。文中介绍了这种类似HSD I的酶的可能来源。
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