Long-term regulation and promoter analysis of mammalian pyruvate dehydrogenase complex

The mammalian pyruvate dehydrogenase complex (PDC) plays a key role in the irreversible decarboxylation of pyruvate derived from glucose and amino acids to form acetyl-CoA in the mitochondria. Acetyl-CoA is then utilized for either energy production by the tricarboxylic acid cycle or energy storage by the lipogenic pathway. This enzyme complex contains multiple copies of three catalytic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetytransferase (E2) and dihydrolipoamide dehydrogenase (E3), two regulatory components (E1-kinase, phospho-E1 phosphatase) and one non-catalytic protein X (also referred to as E3-binding protein) (for review see: Reed, 1974; Patel and Roche, 1990; Behal et al., 1993). These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.