Pyruvate Dehydrogenase Microplate Assay Kit

The enzyme EC 1.2.4.1, commonly known as pyruvate dehydrogenase, plays a crucial role in cellular metabolism. It is a part of the mitochondrial pyruvate dehydrogenase complex (MtPDC), which is responsible for converting pyruvate into acetyl-CoA. Another enzyme with a similar name, pyruvate decarboxylase, also participates in pyruvate metabolism but functions in a different pathway.
The pyruvate dehydrogenase enzyme catalyzes the decarboxylation of pyruvate, removing a carbon dioxide molecule and producing acetyl-CoA. It contains a lipoamide cofactor, which aids in the transfer of acetyl groups. The overall complex, known as the pyruvate dehydrogenase complex, consists of multiple subunits and coenzymes that work together to carry out this important biochemical reaction.
Specifically, the enzyme can be referred to as pyruvate:lipoamide 2-oxidoreductase, highlighting its role in both decarboxylation and accepting the acetyl group. It is also sometimes called pyruvic acid dehydrogenase or pyruvic dehydrogenase. Regardless of the specific name, this enzyme is essential for the proper functioning of cellular respiration and energy generation.
In summary, the pyruvate dehydrogenase enzyme, found within the mitochondrial pyruvate dehydrogenase complex, is responsible for converting pyruvate into acetyl-CoA. It uses a lipoamide cofactor and facilitates decarboxylation while accepting the acetyl group. This enzyme plays a vital role in cellular metabolism and is crucial for energy production.

The activity of pyruvate dehydrogenase can be detected and quantified through various methods. These methods involve measuring the production of products or the consumption of reactants during the reaction catalyzed by pyruvate dehydrogenase.
One approach is to measure the rate of CO2 production from the decarboxylation of pyruvate. This can be done using radiolabeled pyruvate, which produces radiolabeled CO2 that can be quantified. Alternatively, non-radiolabeled pyruvate can be enzymatically converted to acetyl-CoA, which can then react with oxaloacetate to form citrate, which can be measured spectrophotometrically.
Another method involves measuring the formation of NADH, which is produced during the oxidation of pyruvate to acetyl-CoA. This can be done through spectrophotometry or fluorometry by monitoring the absorbance or fluorescence intensity of NADH.
Finally, pyruvate dehydrogenase activity can also be measured through the consumption of substrates or the production of products downstream of the reaction. For example, the consumption of pyruvate can be measured using a colorimetric or spectrophotometric assay that detects the reduction of NAD+ to NADH, which occurs during the reaction catalyzed by pyruvate dehydrogenase.

4 umol/L - 400 umol/L

Shipped and store at 4°C for 6 months.