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 .

References

es:Piruvato deshidrogenasa fosfatasa