PDHA2 Antibody – Rabbit Polyclonal

Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle. Ref.5

Catalytic activity: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. Ref.5

Cofactor: Thiamine pyrophosphate.

Enzyme regulation: Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA2; it is reactivated by dephosphorylation.

Subunit structure: Heterotetramer of two PDHA2 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules. Ref.4

Subcellular location: Mitochondrion matrix.

Tissue specificity: Testis. Expressed in postmeiotic spermatogenic cells. Ref.7

Post-translational modification: Phosphorylation at Ser-205, Ser-266 and Ser-273 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Phosphorylation at Ser-266 interferes with access to active site, and thereby inactivates the enzyme. Dephosphorylation at all three sites, i.e. at Ser-205, Ser-266 and Ser-273, is required for reactivation.

Sequence caution: The sequence AAH94760.1 differs from that shown. Reason: Erroneous initiation.