Pyruvate Dehydrogenase E1-alpha subunit est un gène codé par le symbole PDHA1. Communément appelé aussi: Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial; PDHE1-A type I; PDHA1; PHE1A. Pyruvate Dehydrogenase E1-alpha subunit a une masse de 43.3kDa, une longueur d'acide aminé de 390, et est impliqué dans Pyruvate dehydrogenase E1-alpha deficiency.
Nous proposons 14 des anticorps contre Pyruvate Dehydrogenase E1-alpha subunit, élevé dans Lapin, qui sont appropriés pour le WB, IHC, ELISA, ICC/IF et IP avec des échantillons dérivés de Humain, Souris et Rat.
Informations sur les Gènes et les Protéines
Résumé UniProt
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Résumé Entrez
The pyruvate dehydrogenase (PDH) complex is a nuclear-encoded mitochondrial multienzyme complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and provides the primary link between glycolysis and the tricarboxylic acid (TCA) cycle. 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 alpha 1 subunit containing the E1 active site, and plays a key role in the function of the PDH complex. Mutations in this gene are associated with pyruvate dehydrogenase E1-alpha deficiency and X-linked Leigh syndrome. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Spécificité tissulaire
Ubiquitous.
Implication dans la maladie
Pyruvate dehydrogenase E1-alpha deficiency: An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.
Modification post-traductionnelle
Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, is required for reactivation.
Localisation cellulaire
Mitochondrion matrix.
