(pyruvate dehydrogenase (acetyl-transferring))-phosphatase

In enzymology, a [pyruvate dehydrogenase (acetyl-transferring)]-phosphatase is an enzyme that catalyzes the chemical reaction


 * [pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O $$\rightleftharpoons$$ [pyruvate dehydrogenase (acetyl-transferring)] + phosphate

Thus, the two substrates of this enzyme are [pyruvate dehydrogenase (acetyl-transferring)] phosphate and H2O, whereas its two products are [pyruvate dehydrogenase (acetyl-transferring)] and phosphate.

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is [pyruvate dehydrogenase (acetyl-transferring)]-phosphate phosphohydrolase. Other names in common use include pyruvate dehydrogenase phosphatase, phosphopyruvate dehydrogenase phosphatase, [pyruvate dehydrogenase (lipoamide)]-phosphatase, and [pyruvate dehydrogenase (lipoamide)]-phosphate phosphohydrolase.

Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code.