Pyruvate dehydrogenase is one of the most important enzymes in the cell. It catalyzes the reaction that converts pyruvate to acetyl-CoA with the release of CO2.
Acetyl-CoA is the molecule that enters the citric acid cycle (Krebs Cycle) to be broken down to two additional molecules of CO2.
April 16, 2007
Monday's Molecule #22 (pruvate). The series began with an unknown molecule that turned out to be pyruvate.
April 17, 2007
Pyruvate. A more complete description of the properties of pyruvate.
(April 18, 2007)
Pyruvate Dehydrogenase Reaction. This posting described the reaction catalyzed by pyruvate dehydrogenase.
April 18, 2007
The Structure of the Pyruvate Dehydrogenase Complex was described in some detail, including the techniques used to elucidate it.
April 18, 2007
Nobel Laureate: Aaron Klug. Aaron Klug worked out the technique used to describe the structure of the pyruvate dehydrogenase complex.
April 20, 2007
Some Bacteria Don't Need Pyruvate Dehydrogenase. There are other ways to catalyze the formation of acetyl-CoA.
April 20, 2007
Pyruvate Dehydrogenase Evolution. The evolution of the genes encoding the pyruvate dehydrogenase subunits is explained.
April 20, 2007
Human Genes for the Pyruvate Dehydrogenase Complex. Identifying the genes for the subunits of the complex.
April 23, 2007
Regulating Pyruvate Dehydrogenase. How pyruvate dehydrogenase is regulated, including the effect of the inhibitor dichloroacetate (DCA).
August 31, 2007
Dichloroacetate (DCA) Website Shut Down by the FDA
August 3, 2012
On the Evolution of New Enzymes: Completely Different Enzymes Can Catalyze Similar Reactions
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