Pyruvate dehydrogenase E1 component subunits alpha and beta, mitochondrial (EC 1.2.4.1; UniProt P08559 and P11177; also known as PDHE1-A type I and PDHE1-B, respectively) are encoded by the PDHA1 (also known as PDHA, PDHAD, PHE1A) and the PDHB (also known as PDHBD, PHE1B) genes (Gene ID 5160 and 5162, respectively) in human. The pyruvate dehydrogenase (PDH) complex catalyzes the overall, irreversible conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle. This complex contains multiple copies of three enzymatic components: PDH (E1 or PDHE1-A type I), dihydrolipoamide acetyltransferase (E2), and lipoamide dehydrogenase (E3). PDH (E1) performs the first two reactions within the PDH complex: a decarboxylation of pyruvate and a reductive acetylation of lipoic acid. Lipoic acid is covalently bound to dihydrolipoamide acetyltransferase (E2), which is the second catalytic component enzyme of PDC. The reaction catalyzed by PDH (E1) is considered to be the rate-limiting step for the PDH complex. PDH is regulated by both pyruvate dehydrogenase kinase (PDK)-mediated phosphorylation and feedback inhibition. 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, Ser-232, Ser-293, and Ser-300, is required for reactivation. PDH (E1) deficiency has been linked to primary lactic acidosis in children.
Synonyms: Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial, PDHE1-A type I, Pyruvate dehydrogenase E1 component subunit beta, mitochondrial, PDHE1-B
Application: Research CategorySignaling
Other Notes: Concentration: Please refer to lot specific datasheet.