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Archives of Biochemistry and Biophysics, 1985
The specificities of pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase were probed using synthetic peptides corresponding to the sequence around phosphorylation sites 1 and 2 on pyruvate dehydrogenase [Tyr-His-Gly-His-Ser(P1)-Met-Ser-Asp-Pro-Gly-Val-Ser(P2)-Tyr-Arg].
T R, Mullinax +3 more
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The specificities of pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase were probed using synthetic peptides corresponding to the sequence around phosphorylation sites 1 and 2 on pyruvate dehydrogenase [Tyr-His-Gly-His-Ser(P1)-Met-Ser-Asp-Pro-Gly-Val-Ser(P2)-Tyr-Arg].
T R, Mullinax +3 more
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Insulin mediator stimulation of pyruvate dehydrogenase phosphatases
Archives of Biochemistry and Biophysics, 1992A two stage assay for detecting insulin mediator based upon its stimulation of soluble pyruvate dehydrogenase (PDH) phosphatase to activate soluble pyruvate dehydrogenase complex (PDC) has been developed. This coupled assay determines the activation of PDC by monitoring production of [14C]CO2 from [1-14C]pyruvic acid.
K, Lilley +4 more
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Inhibition of pyruvate dehydrogenase and pyruvate dehydrogenase phosphate phosphatase by glyoxylate
Bioorganic Chemistry, 1985Abstract The overall reaction catalyzed by the pyruvate dehydrogenase complex from rat epididymal fat tissue is inhibited by glyoxylate at concentrations greater than 10 μ m . The inhibition is competitive with respect to pyruvate; Ki was found to be 80 μ m .
Susan M. Beatty, Gordon A. Hamilton
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Biochemical and Biophysical Research Communications, 1977
Abstract Evidence is presented that phosphopeptides produced by tryptic digestion of phosphorylated pyruvate dehydrogenase are effective substrates for pyruvate dehydrogenase phosphatase and that the dephosphopeptides can serve as substrates for pyruvate dehydrogenase kinase.
P F, Davis, F H, Pettit, L J, Reed
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Abstract Evidence is presented that phosphopeptides produced by tryptic digestion of phosphorylated pyruvate dehydrogenase are effective substrates for pyruvate dehydrogenase phosphatase and that the dephosphopeptides can serve as substrates for pyruvate dehydrogenase kinase.
P F, Davis, F H, Pettit, L J, Reed
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Stimulation of pyruvate dehydrogenase phosphatase activity by polyamines
Biochemical and Biophysical Research Communications, 1984Pyruvate dehydrogenase phosphatase requires Mg2+ or Mn2+, and its activity in the presence of Mg2+ is markedly stimulated by Ca2+. At saturating Mg2+ and Ca2+ concentrations, the polyamines spermine, spermidine and putrescine stimulated the activity of pyruvate dehydrogenase phosphatase 1.5- to 3-fold. Spermine was the most active of the polyamines. At
Z, Damuni, J S, Humphreys, L J, Reed
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Pyruvate dehydrogenase phosphatase
1996Four classes of protein serine/threonine phosphatases have been identified in eukaryotic cells on the basis of substrate specificities and sensitivity to activators and inhibitors (Cohen, 1989; Shenolikar and Nairn, 1991). Protein phosphatase 1 is sensitive to the thermostable proteins inhibitor 1 and inhibitor 2, and protein phosphatases 1 and 2A are ...
L. J. Reed +3 more
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Function of calcium ions in pyruvate dehydrogenase phosphatase activity
Biochemical and Biophysical Research Communications, 1972Abstract Phosphorylation and dephosphorylation of the pyruvate dehydrogenase (PDH) component of the mammalian pyruvate dehydrogenase complex are catalyzed, respectively, by a MgATP2-requiring kinase and a Mg2+-requiring phosphatase. The kinase and the PDH, but not the phosphatase, are tightly bound to the dihydrolipoyl transacetylase core of the ...
F H, Pettit, T E, Roche, L J, Reed
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Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003
The activity of mammalian pyruvate dehydrogenase complex (PDC) is regulated by a phosphorylation/dephosphorylation cycle. Dephosphorylation accompanied by activation is carried out by two genetically different isozymes of pyruvate dehydrogenase phosphatase, PDP1c and PDP2c.
Tatiana, Karpova +3 more
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The activity of mammalian pyruvate dehydrogenase complex (PDC) is regulated by a phosphorylation/dephosphorylation cycle. Dephosphorylation accompanied by activation is carried out by two genetically different isozymes of pyruvate dehydrogenase phosphatase, PDP1c and PDP2c.
Tatiana, Karpova +3 more
openaire +2 more sources

