PDP1
PDP1 (pyruvate dehydrogenase phosphatase catalytic subunit 1, also known as PDP, PDH, PPM2A and PPM2C) is a mitochondrial PP2C-family enzyme. It dephosphorylates and reactivates the E1 alpha subunit of the pyruvate dehydrogenase complex, stimulating the conversion of pyruvate into acetyl-CoA. Browse Assay Genie's current range of PDP1 research reagents below, or read on for the biology behind the target.
PDP1 is a mitochondrial enzyme that catalyses the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex (PDC). In doing so it stimulates the conversion of pyruvate into acetyl-CoA. Pyruvate dehydrogenase (E1) is one of three components of the large complex, alongside E2 and E3. Pyruvate dehydrogenase kinases phosphorylate serine residues of E1, which inactivates E1 and inhibits the complex. Pyruvate dehydrogenase phosphatases reverse this, so PDP1 acts as the counterpart to the kinases in controlling PDC activity.
Pyruvate dehydrogenase phosphatase is a heterodimer of catalytic and regulatory subunits. Two catalytic subunits have been reported: one is predominantly expressed in skeletal muscle and the other is much more abundant in the liver. The catalytic subunit encoded by the PDP1 gene is the skeletal muscle form. It belongs to the protein phosphatase 2C (PP2C) superfamily, and HGNC places it in the Mg2+/Mn2+-dependent protein phosphatases group. Together with the pyruvate dehydrogenase complex and the kinases, it is located in the mitochondrial matrix. Multiple alternatively spliced transcript variants encoding different isoforms have been identified. Mouse and rat both have a Pdp1 ortholog.
The enzyme has carried several names, including protein phosphatase 2C, magnesium-dependent, catalytic subunit, and the earlier symbols PPM2A and PPM2C. Mutation in the PDP1 gene causes pyruvate dehydrogenase phosphatase deficiency, which makes the protein relevant to studies of pyruvate metabolism and PDC regulation.
PDP1 reverses kinase-mediated phosphorylation of the E1 alpha subunit, making it central to studies of how PDC activity is switched on.
By promoting conversion of pyruvate into acetyl-CoA, PDP1 is relevant to research on mitochondrial matrix enzymes and metabolic flux.
The PDP1 catalytic subunit is the form predominantly expressed in skeletal muscle, distinguishing it from the liver-abundant subunit.
Mutation in the PDP1 gene causes pyruvate dehydrogenase phosphatase deficiency, supporting research into inherited disorders of pyruvate metabolism.
PDP1 is a mitochondrial phosphatase that dephosphorylates the alpha subunit of the E1 component of the pyruvate dehydrogenase complex. This reactivates the complex and stimulates the conversion of pyruvate into acetyl-CoA, opposing the inhibitory phosphorylation applied by pyruvate dehydrogenase kinases.
PDP1 is also known as PDP, PDH, PPM2A and PPM2C, and formerly as protein phosphatase 2C, magnesium-dependent, catalytic subunit. The gene produces multiple alternatively spliced transcript variants encoding different isoforms. It belongs to the PP2C family of phosphatases.
Mutation in the PDP1 gene causes pyruvate dehydrogenase phosphatase deficiency. Mouse and rat each have an ortholog named Pdp1. Check the datasheet of any product for its validated reactivity.
Other proteins with similar gene symbols, listed for navigation alongside PDP1 targets at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9P0J1; product specifications from Assay Genie datasheets.