Phosphoenzyme formation by purified, reconstituted copper ATPase of Enterococcus hirae

被引：18

作者：

WylerDuda, P ^{[1
]}

Solioz, M ^{[1
]}

机构：

[1] UNIV BERN, INST CLIN PHARMACOL, CH-3010 BERN, SWITZERLAND

来源：

FEBS LETTERS | 1996年 / 399卷 / 1-2期

关键词：

copper; P-type ATPase; purification; phosphorylation; vanadate; (Enterococcus hirae);

D O I：

10.1016/S0014-5793(96)01306-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The Enterococcus hirae CopB ATPase serves in the secretion of excess copper from cells and belongs to the recently discovered, new class of heavy metal transport ATPases. We here report the affinity purification of CopB to near homogeneity and its reconstitution into phospholipid vesicles. In these proteoliposomes, the ATPase formed an acylphosphate reaction intermediate with the gamma-phosphate of ATP. ATPase activity and phosphoenzyme formation were inhibited by vanadate with an Iso of 0.1 mM. Our results suggest that heavy metal and non-heavy metal ATPases operate by the same underlying mechanism.

引用

页码：143 / 146

页数：4

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