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酵母液泡H⁺-ATP酶的组装和ATP水解在缺少亚基c''的情况下发生。

Assembly of the yeast vacuolar H+-ATPase and ATP hydrolysis occurs in the absence of subunit c''.

作者信息

Whyteside Graham, Gibson Lucien, Scott Moira, Finbow Malcolm E

机构信息

School of Biological and Biomedical Sciences, Glasgow Caledonian University, Cowcaddens Road, Glasgow G4 0BA, United Kingdom.

出版信息

FEBS Lett. 2005 Jun 6;579(14):2981-5. doi: 10.1016/j.febslet.2005.04.049.

Abstract

The V-ATPases are ubiquitous enzymes of eukaryotes. They are involved in many cellular processes via their ability to pump protons across biological membranes. They are two domain enzymes comprising an ATP hydrolysing sector and a proton translocating sector. Both sectors are functionally coupled. The proton tanslocating sector, V0, is comprised of five polypeptides in an as yet undetermined stoichiometry. In V0 three homologous proteins, subunit c, c' and c'' have previously been reported to be essential for assembly of the enzyme. However, we report that subunit c'' is not essential for assembly but is for functional coupling of the enzyme.

摘要

V-ATP酶是真核生物中普遍存在的酶。它们通过将质子泵过生物膜的能力参与许多细胞过程。它们是由一个ATP水解区和一个质子转运区组成的双结构域酶。两个区在功能上相互耦合。质子转运区V0由五种多肽组成,其化学计量尚未确定。在V0中,先前已报道三种同源蛋白亚基c、c'和c''对该酶的组装至关重要。然而,我们报告亚基c''对组装不是必需的,但对该酶的功能耦合是必需的。

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