a protein phosphoserine phosphatase associated with the mitochondrial matrix that activates phosphorylated pyruvate dehydrogenase complex by dephosphorylation. The PDPs play crucial roles in switching metabolic flux from glycolysis towards oxidative phosphorylation. Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex . PDP1 is composed of a catalytic subunit and a regulatory subunit (PDPR). Heterodimer of a catalytic subunit and a FAD protein of unknown function . Defects in PDP1 are the cause of pyruvate dehydrogenase phosphatase deficiency (PDP deficiency). PDP deficiency results in lactic acidosis leading to neurological dysfunction. Belongs to the PP2C family. Note: This description may include information from UniProtKB.
Protein type: Protein phosphatase, Ser/Thr (non-receptor); Mitochondrial; Motility/polarity/chemotaxis; EC 126.96.36.199
Molecular Function: [pyruvate dehydrogenase (lipoamide)] phosphatase activity; calcium ion binding; magnesium-dependent protein serine/threonine phosphatase activity; protein binding; protein complex binding; protein serine/threonine phosphatase activity
Biological Process: cellular metabolic process; pyruvate metabolic process; regulation of acetyl-CoA biosynthetic process from pyruvate
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.