Inhibition of spinach glyceraldehyde-3-phosphate dehydrogenases by pentalenolactone
Inhibition of spinach glyceraldehyde-3-phosphate dehydrogenases by pentalenolactone
复制标题
五烯酸内酯对菠菜甘油醛-3-磷酸脱氢酶的抑制
作者：
K. Mann;D. Mecke
从各种链霉菌1 -3的发酵液中分离的抗生素并环戊烯内酯根据培养条件和纯化方法有三种不同的形式：E（环氧化物;图1）、D（二醇）和C（氯乙醇）。后两种衍生自E，通过环氧环的裂解，分别插入水和HCl元素。正如体外研究所示6，戊烯内酯通过特异性抑制甘油醛-3-磷酸脱氢酶（EC 1.2.1.12）来抑制糖酵解，但已知没有其他酶受到影响。这种抑制作用是不可逆的，无论酶来自大肠杆菌、酵母还是兔子肌肉，这种抑制作用都是相似的。我们在这里报告，抗生素有不同的影响，发生在菠菜叶的三个类的甘油醛-3-磷酸脱氢酶，我们证明了它的高特异性的糖酵解酶。
The antibiotic pentalenolactone, isolated from the fermentation broth of various species of Streptomyces1–3, has three different forms depending on culture conditions and purification procedure: E (epoxide; Fig. 1), D (diol) and C (chlorhydrine). The latter two derive from E by cleavage of the epoxide ring with insertion of the elements of water and HCl, respectively. As in vitro studies have shown6, pentalenolactone inhibits glycolysis by inhibiting specifically glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12), but no other enzyme was known to be affected. The inhibition is irreversible and is similar whether the enzyme comes from Escherichia coli, yeast or rabbit muscle. We report here that the antibiotic has different effects on the three classes of glyceraldehyde-3-phosphate dehydrogenases that occur in spinach leaves, and we demonstrate its high specificity for the glycolytic enzyme.