Effect of polyamines on mitochondrial F1-ATPase catalyzed reactions.

Abstract:

:The effect of polyamines on F1-ATPase catalyzed reactions has been studied through the use of submitochondrial particles and F1-ATPase. ATP degradation catalyzed by submitochondrial particles and F1-ATPase was inhibited by spermine and spermidine. Spermine's inhibition was much greater than spermidine's effect. In contrast, P1-ATP exchange and succinate dependent ATP synthesis catalyzed by submitochondrial particles were both stimulated by spermine. The inhibition of ATPase activity by polyamines probably occurs through polyamine's replacement of Mg2+ on ATP, for the following reasons. (a) The ATPase activity inhibited by spermine was partially recovered when Mg2+ was added. (b) Spermine bound to ATP and phospholipids but not to F1-ATPase; yet spermine inhibited the ATPase reaction catalyzed by F1-ATPase, a protein free of phospholipid. (c) The binding of spermine to ATP was inhibited by Mg2+. The ATP content in polyamine-deficient cells definitely was lower than that in normal cells. On the basis of these results, the possible role of spermine in keeping the ATP concentration at a high level is discussed.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Igarashi K,Kashiwagi K,Kobayashi H,Ohnishi R,Kakegawa T,Nagasu A,Hirose S

doi

10.1093/oxfordjournals.jbchem.a122847

subject

Has Abstract

pub_date

1989-08-01 00:00:00

pages

294-8

issue

2

eissn

0021-924X

issn

1756-2651

journal_volume

106

pub_type

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