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Effects of lipids and long-chain alkyl derivatives on the activity of (Ca2+-Mg2+)-ATPase.

Abstract：

:The ATPase activity of the (Ca2+-Mg2+)-ATPase reconstituted into bilayers of phosphatidylcholines depends on the fatty acyl chain length of the phospholipids. It is shown that the fluorescence response to Ca2+ of the ATPase modified with fluorescein isothiocyanate is also dependent on phospholipid structure and is interpreted in terms of a change in the equilibrium between two forms of the ATPase, E1 and E2. A kinetic scheme for the ATPase is presented in which ATPase activity is markedly dependent on the rate of the transition between two phosphorylated forms of the ATPase, E1'PCa2 and E2'PCa2, and it is postulated that changing the phospholipid structure changes this rate. The rate of dephosphorylation of the ATPase and the ATP dependence of the E1'PCa2-E2'PCa2 transition are also lipid dependent. Binding of oleyl alcohol causes large, lipid-dependent changes in ATPase activity, and these are interpreted in terms of changes in the rates of these same steps. Oleylamine, which has been shown to bind more strongly at annular sites than at nonannular sites, inhibits ATPase activity irrespective of lipid structure, whereas fatty acids, which bind less strongly at annular sites, only inhibit at high concentrations. Methyl oleate, which binds more strongly at nonannular sites than at annular sites, causes marked stimulation for the ATPase reconstituted with short-chain lipids.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Froud RJ,East JM,Jones OT,Lee AG

doi

10.1021/bi00371a043

subject

Has Abstract

pub_date

1986-11-18 00:00:00

pages

7544-52

issue

23

eissn

0006-2960

issn

1520-4995

journal_volume

25

pub_type

杂志文章

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