Binding of pyruvate dehydrogenase to the core of the human pyruvate dehydrogenase complex [PDF]
In human (h) pyruvate dehydrogenase complex (PDC) the pyruvate dehydrogenase (E1) is bound to the E1‐binding domain of dihydrolipoamide acetyltransferase (E2). The C‐terminal surface of the E1β subunit was scanned for the negatively charged residues involved in binding with E2.
Korotchkina, Lioubov G. +1 more
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The relationships between transketolase, yeast pyruvate decarboxylase and pyruvate dehydrogenase of the pyruvate dehydrogenase complex [PDF]
The amino acid sequences of four thiamine pyrophosphate‐requiring enzymes were aligned with the published amino acid sequence of the transketolase of Hansenula polymorpha. Sequences of the combined α and β subunits of the E1 enzyme of the pyruvate dehydrogenase complexes of Homo sapiens and Bacillus stearothermophilus aligned well with the ...
Robinson, Brian H., Chun, Kathy
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The Role of Pyruvate Dehydrogenase Kinase in Diabetes and Obesity [PDF]
The pyruvate dehydrogenase complex (PDC) is an emerging target for the treatment of metabolic syndrome. To maintain a steady-state concentration of adenosine triphosphate during the feed-fast cycle, cells require efficient utilization of fatty acid and ...
In-Kyu Lee
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Restoration of fitness lost due to dysregulation of the pyruvate dehydrogenase complex is triggered by ribosomal binding site modifications [PDF]
Summary: Pyruvate dehydrogenase complex (PDC) functions as the main determinant of the respiro-fermentative balance because it converts pyruvate to acetyl-coenzyme A (CoA), which then enters the TCA (tricarboxylic acid cycle).
Amitesh Anand +7 more
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GDAP1 loss of function inhibits the mitochondrial pyruvate dehydrogenase complex by altering the actin cytoskeleton [PDF]
GDAP1 mutations effect Charcot-Marie-Tooth disease 4A by inhibiting the pyruvate dehydrogenase complex and restricting mitochondrial localization of dynamin-related protein 1 through alterations of the actin cytoskeleton.
Christina Wolf +22 more
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Monitoring phosphorylation of the pyruvate dehydrogenase complex [PDF]
The pyruvate dehydrogenase multienzyme complex (PDC) is a key regulatory point in cellular metabolism linking glycolysis to the citric acid cycle and lipogenesis. Reversible phosphorylation of the pyruvate dehydrogenase enzyme is a critical regulatory mechanism and an important point for monitoring metabolic activity.
Matthew J Rardin +2 more
exaly +3 more sources
The mitochondrial pyruvate dehydrogenase complex is regulated by reversible seryl-phosphorylation of the E1α subunit by a dedicated, intrinsic kinase. The phospho-complex is reactivated when dephosphorylated by an intrinsic PP2C-type protein phosphatase.
Nagib eAhsan +5 more
doaj +2 more sources
Correction: The pyruvate dehydrogenase complex regulates mitophagic trafficking and protein phosphorylation [PDF]
Mutations in the PDC affect the phosphorylation and mitophagic trafficking of matrix proteins, through the novel regulation of associated kinases and a phosphatase.
Panagiota Kolitsida +6 more
doaj +2 more sources
The tricarboxylic acid (TCA) cycle is a central route for generating cellular energy and precursors for biosynthetic pathways. Emerging evidences have shown that the aberrations of metabolic enzymes which affect the integrity of TCA cycle are implicated ...
Tao Shen +4 more
doaj +1 more source
Pyruvate dehydrogenase complex deficiency is a rare genetic disorder that can lead to severe metabolic consequences. We present the case of a young adult with pyruvate dehydrogenase complex deficiency who presented with progressive shortness of breath ...
Madison B. Calder, Kristen D. Kelley
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