Pyruvate dehydrogenase (PDH) is a mitochondrial enzyme that catalyzes the conversion of pyruvate to acetyl-CoA and CO₂, and also links the tricarboxylic acid (TCA) and glycolysis pathways. The enzyme is inhibited by phosphorylation and activated by dephosphorylation. Mutations in PDH have been linked to pyruvate dehydrogenase deficiency (causing lactic acidosis and neurologic dysfunctions) and Leigh syndrome. PDH has also been implicated in oncogene-induced senescence. PDH measurements can provide insights into metabolic functions and oncogenesis.

PDH Activity Assay Kit has been used to determine the activity of pyruvate dehydrogenase.

Suitable for the detection of PDH activity in a variety of biological samples such as cell and tissue culture supernatants and purified mitochondria.

Pyruvate dehydrogenase activity is determined using a coupled enzyme reaction, which results in a colorimetric (450 nm) product proportional to the enzymatic activity present. One unit of pyruvate dehydrogenase is the amount of enzyme that will generate 1.0 mmole of NADH per minute at 37 °C.