Selective modification by transglutaminase of a glutamine side chain in the hinge region of the histidine-388----glutamine mutant of yeast phosphoglycerate kinase.
Selective modification by transglutaminase of a glutamine side chain in the hinge region of the histidine-388----glutamine mutant of yeast phosphoglycerate kinase.
复制标题
通过转谷氨酰胺酶选择性修饰酵母磷酸甘油酸激酶组氨酸-388----谷氨酰胺突变体铰链区的谷氨酰胺侧链。
DOI：
10.1042/bj2730073
复制
发表时间：
1991
影响因子：
4.1
通讯作者：
L. Sawyer
中科院分区：
文献类型：
--
作者：
P. Coussons;S. Kelly;N. C. Price;C. Johnson;B. Smith;L. Sawyer
本文研究了腐胺和单丹酰尸胺在转氨酶催化下与酵母磷酸甘油酸激酶的结合。几乎没有掺入到野生型酶的胺，但近化学计量掺入到组氨酸-388-谷氨酰胺突变体酶。C.D.研究表明，突变酶的总体结构与野生型酶非常相似。将胺掺入突变酶中不会导致其活性发生显著变化。谷氨酰胺-388显示，通过分离和测序的修饰肽，将单丹酰尸胺纳入突变酶的网站。转氨酶反应的特异性进行了讨论，根据现有的数据。
The transglutaminase-catalysed incorporation of putrescine and monodansylcadaverine into yeast phosphoglycerate kinase has been studied. There is little incorporation of the amines into wild-type enzyme, but nearly stoichiometric incorporation into the histidine-388----glutamine mutant enzyme. C.d. studies show that the overall structure of the mutant enzyme is very similar to that of the wild-type enzyme. Incorporation of the amines into the mutant enzyme causes no significant change in its activity. Glutamine-388 was shown, by isolation and sequencing of the modified peptide, to be the site of incorporation of monodansylcadaverine into the mutant enzyme. The specificity of the transglutaminase reaction is discussed in the light of available data.