ATP‐citrate lyase is another enzyme the histidine phosphorylation of which is inhibited by vanadate

FEBS Letters

Krivanek, Jiri¹  Novakova, Ludmila¹ 

[1] Institute of Physiology, Czechoslovak Academy of Sciences, Prague, Czechoslovakia

关键词: Vanadate;    ATP-citrate lyase;    Histidine phosphorylation;   

DOI  :  10.1016/0014-5793(91)80438-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have recently shown that phosphorylation of histidine residue of the α-subunit of the succinyl-CoA synthetase is inhibited by both vanadate and vanadyl. To assess the universality of this inhibition, we have estimated the effect of vanadate on the phosphorylation of another enzyme ATP-citrate lyase, prepared from rat liver. This enzyme contains histidine as the only amino acid with an acid-labile (P—N) phosphate bond. The 67% inhibition of endogenous phosphorylation by 1 mM vanadate disappeared after cleavage of the acidic P—N bond of histidine with acidic sample solution. The remaining 33 per cent radioactivity was due to labelling of the acid-stable phosphoamino acids (P-serine and P-threonine), the phosphorylation of which was not affected by vanadate. The dose—response curve for vanadate inhibition closely resembles that shown previously for inhibition of phosphorylation of histidine in the succinyl-CoA synthetase. The results suggest that the action of vanadate on histidinyl phosphorylation is a more general effect (like its influence on phosphorylation of the protein-bound tyrosine).

【 授权许可】

Unknown