Open AccessPig Heart [ 35 S]Thiophosphoryl Pyruvate Dehydrogenase Complexes
Author(s) -
TONKS Nicholas K.,
KEARNS Anne,
RANDLE Pshilip J.
Publication year - 1982
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1982.tb06472.x
Subject(s) - dephosphorylation , pyruvate dehydrogenase complex , chemistry , phosphorylation , biochemistry , adenosine triphosphate , pyruvate dehydrogenase phosphatase , pyruvate dehydrogenase kinase , adenosine , phosphatase , enzyme
Thiophosphorylation of pig heart pyruvate dehydrogenase complex with atp [ 35 S] (adenosine 5′[γ‐thio]‐ triphosphate) was analogous to phosphorylation with [γ‐ 32 p]ATP except that thiophosphorylation of sites 2 and 3 was more rapid. With pyruvate dehydrogenase phosphatase the rate of dethiophosphorylation was 0.5% of that of dephosphorylation. Thiophospghorylation of sites 2 and 3 in complex phosphorylated i n site educed the rate of dephosphorylation of site 1.