Purified recombinant human Pyruvate Dehydrogenase protein fragments expressed in E.coli.
Conjugation:
Unconjugated
Alternative Names:
PHE1A, Pyruvate dehydrogenase E1 component subunit alpha somatic form mitochondrial, PDHE1-A type I
The pyruvate dehydrogenase complex catalyzes the conversion of pyruvate and CoA into acetyl-CoA and CO2 in the presence of NAD+. Acetyl-CoA then goes into the citric acid cycle where it reacts with oxaloacetate to form citrate. Acetyl-CoA is also used for fatty acid and cholesterol biosynthesis. The reaction of oxidative decarboxylation of pyruvate therefore serves as a critical link between glycolysis and the citric acid cycle and lipid metabolism. In mammalian cells, the pyruvate dehydrogenase complex is located in the mitochondrial matrix . This complex is comprised of three enzymes: pyruvate dehydrogenase , dihydrolipoamide acetyltransferase, and dihydrolipoamide dehydrogenase . Pyruvate dehydrogenase consists of two subunits: alpha and beta. This enzyme catalyzes the removal of CO2 from pyruvate. Mutations in the alpha subunits of pyruvate dehydrogenase lead to congenital defects that are usually associated with lactic acidosis, neurodegeneration, and early death .~Pyruvate dehydrogenase kinase 1 phosphorylates pyruvate dehydrogenase alpha1 subunit at Ser293 to inactivate its activity . This phosphorylation contributes to the tumor metabolic reprogramming toward glycolysis in hypoxia by inhibiting the citric acid cycle .
