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Pyruvate dehydrogenase (PDH) deficiency is a congenital degenerative metabolic disease resulting from a mutation of the pyruvate dehydrogenase complex (PDC) located on the X chromosome. While defects have been identified in all 3 enzymes of the complex, the E1-α subunit is predominantly the culprit.
In eukaryotic cells the pyruvate decarboxylation occurs inside the mitochondrial matrix, after transport of the substrate, pyruvate, from the cytosol. The transport of pyruvate into the mitochondria is via the transport protein pyruvate translocase. Pyruvate translocase transports pyruvate in a symport fashion with a proton (across the inner ...
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial is an enzyme that in humans is encoded by the PDHA1 gene.The pyruvate dehydrogenase complex is a nuclear-encoded mitochondrial matrix multienzyme complex that provides the primary link between glycolysis and the tricarboxylic acid (TCA) cycle by catalyzing the irreversible conversion of pyruvate into acetyl-CoA.
The PDHB gene is responsible for the coding of the E1 beta subunit of the pyruvate dehydrogenase complex. The DLAT gene is responsible for the coding of the E2 subunit, and the PDP1 is responsible for producing the PDH phosphatase catalytic subunit that catalyzes PDH dephosphorylation. This dephosphorylation activates the complex.
The primary sequencing between the four isozymes are conserved with 70% identity. The greatest differences occur near the N-terminus. [2] PDK1 is the largest of the four with 436 residues while PDK2, PDK3 and PDK4 have 407, 406, and 411 residues respectively. The isozymes have different activity and phosphorylation rates at each site.
The PDH complex is composed of multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). The E1 enzyme is a heterotetramer of two alpha and two beta subunits. This gene encodes the E1 beta subunit.
Pyruvate dehydrogenase complex reaction. Pyruvate decarboxylation or pyruvate oxidation, also known as the link reaction (or oxidative decarboxylation of pyruvate [1]), is the conversion of pyruvate into acetyl-CoA by the enzyme complex pyruvate dehydrogenase complex.
The PDH complex serves as the link between glycolysis and the citric acid cycle and is required for oxidative metabolism. The activity of PDH involves three distinct enzymes, four activities, and five different cofactors. [5] [6] [7] Steps of the PDH complex: (1) decarboxylation (E1, formation of hydroxyethyl-TPP)