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This enzyme contains histidine as the only amino acid with an acid\u2010labile (P\u2014N) phosphate bond. The 67% inhibition of endogenous phosphorylation by 1 mM vanadate disappeared after cleavage of the acidic P\u2014N bond of histidine with acidic sample solution. The remaining 33 per cent radioactivity was due to labelling of the acid\u2010stable phosphoamino acids (P\u2010serine and P\u2010threonine), the phosphorylation of which was not affected by vanadate. The dose\u2014response curve for vanadate inhibition closely resembles that shown previously for inhibition of phosphorylation of histidine in the succinyl\u2010CoA 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\u2010bound tyrosine).<\/jats:p>","DOI":"10.1016\/0014-5793(91)80438-9","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T07:43:20Z","timestamp":1027583000000},"page":"32-34","source":"Crossref","is-referenced-by-count":8,"title":["ATP\u2010citrate lyase is another enzyme the histidine phosphorylation of which is inhibited by vanadate"],"prefix":"10.1002","volume":"282","author":[{"given":"Jiri","family":"Krivanek","sequence":"first","affiliation":[]},{"given":"Ludmila","family":"Novakova","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2001,12,7]]},"reference":[{"key":"e_1_2_1_2_1","first-page":"123","volume":"45","author":"Nechay B.R.","year":"1986","journal-title":"Fed. 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