Pyruvate dehydrogenase kinases catalyze phosphorylation of serine residues of E1 to inactivate the E1 component and inhibit the complex.

Two catalytic subunits have been reported; one is predominantly expressed in skeletal muscle, and another one is much more abundant in the liver.

The catalytic subunit, encoded by this gene, is the former, and belongs to the protein phosphatase 2C (PP2C) superfamily.

[5] Pyruvate dehydrogenase phosphatase is stimulated by insulin, PEP, and AMP, but competitively inhibited by ATP, NADH, and Acetyl-CoA.

[5][clarification needed] This article incorporates text from the United States National Library of Medicine, which is in the public domain.