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The 34 kDa mitochondrial protein, phosphorylation of which is inhibited by vanadate, is the α‐subunit of succinyl‐CoA synthetase
Author(s) -
Křivánek Jiří,
Nováková Ludmila
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81021-x
Subject(s) - autophosphorylation , vanadate , phosphorylation , protein subunit , mitochondrion , biochemistry , chemistry , inhibitory postsynaptic potential , protein phosphorylation , microbiology and biotechnology , biology , protein kinase a , endocrinology , gene
Our previous characterization of the 34 500 Da protein, which occurs exclusively in mitochondria and the phosphorylation of which is inhibited rather than stimulated by vanadate, suggested that it might be the α‐subunit of succinyl‐CoA synthetase (SCS). In the present communication we show that in a commercial preparation of SCS there is only one band (34 500 Da) which is phosphorylated under endogenous phosphorylation conditions in vitro. The relative molecular weight of this band, sensitivity of its phosphorylation to the inhibitory action of both vanadate and vanadyl as well as dose response curves are identical to those described for the mitochondrial ‘34 kDa’ protein. This is the first demonstration of an inhibitory effect of vanadium ions on the autophosphorylation of the α‐subunit of SCS.