Description
Protocol
Available protocols: ELISA+
Specificity / Sensitivity
The PathScan
Species Reactivity: Human, Mouse, Rat, Monkey
Background
The pyruvate dehydrogenase complex catalyzes the conversion of pyruvate and CoA into acetyl-CoA and CO in the presence of NAD . Acetyl-CoA then goes into the citric acid cycle where it reacts with oxaloacetate to form citrate. The reaction of oxidative decarboxylation of pyruvate serves as a critical link between glycolysis and the citric acid cycle. In mammalian cells, the pyruvate dehydrogenase complex is located in the mitochondrial matrix (1). This complex is composed of three enzymes: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). Pyruvate dehydrogenase (E1) consists of two subunits: α and β. This enzyme catalyzes the removal of CO from pyruvate. Mutations in the α subunits of pyruvate dehydrogenase (E1) lead to congenital defects that are usually associated with lactic acidosis, neurodegeneration, and early death (2). Pyruvate dehydrogenase kinase 1 phosphorylates pyruvate dehydrogenase (E1) α1 subunit at Ser293 to inactivate its activity (3,4). This phosphorylation contributes to the tumor metabolic reprogramming toward glycolysis in hypoxia by inhibiting the citric acid cycle (4).
Alternate Names
ODPA; PDHA; PDHA1; PDHAD; PDHCE1A; PDHE1-A type I; PHE1A; pyruvate dehydrogenase (lipoamide) alpha 1; pyruvate dehydrogenase alpha 1; pyruvate dehydrogenase complex, E1-alpha polypeptide 1; pyruvate dehydrogenase E1 alpha 1; pyruvate dehydrogenase E1 alpha 1 subunit; Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial; pyruvate dehydrogenase E1 subunit alpha 1
