Pyruvate dehydrogenase phosphatase catalytic subunit 2 (PDP2)

Pyruvate dehydrogenase phosphatase catalytic subunit 2 (PDP2) is a mitochondrial enzyme and member of the protein phosphatase 2C (PP2C) family that catalyzes the dephosphorylation and reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex (PDC)[2][3]. Through this action, PDP2 plays a critical role in regulating the conversion of pyruvate to acetyl-CoA, thereby linking glycolysis with the tricarboxylic acid (TCA) cycle and fatty acid synthesis pathways. Basal activity of PDP2 is required to restore PDC activity after it has been inhibited by phosphorylation, supporting cellular energy production, especially during high metabolic demand. Mutations or deficiencies in this enzyme have been associated with metabolic disorders and are implicated in regulation of immune cell function and, potentially, in the pathology of cancer[3].

Other names

Pyruvate dehydrogenase [acetyl-transferring]-phosphatase 2, mitochondrialKIAA1348PDP 2PDPC 2PPM2C2PPM2BProtein phosphatase 2C, magnesium-dependent, catalytic subunit 2Protein phosphatase, Mg2+/Mn2+ dependent 2BPyruvate dehydrogenase phosphatase isoenzyme 2

Activation via dephosphorylation of the pyruvate dehydrogenase complex (PDC) E1 alpha subunit, counteracting the inactivating phosphorylation by pyruvate dehydrogenase kinases (PDKs)[2][3] Drugs targeting this class, if they existed, would likely act as phosphatase modulators