Localization | Comment | Organism | GeneOntology No. | Textmining |
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Organism | UniProt | Comment | Textmining |
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Geobacillus stearothermophilus | - |
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Subunits | Comment | Organism |
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More | there may be two conformers of E1alpha in the pyruvate decarboxylase E1 heterotetramer, one being more susceptible to proteolysis than the other. A highly conserved region in E1a, part of a surface loop at the entrance to the active site, is the most susceptible to cleavage in E1 (a2b2). As a result, the oxidative decarboxylation of pyruvate catalysed by E1 in the presence of dichlorophenol indophenol as an artificial electron acceptor is markedly enhanced, but the reductive acetylation of a free lipoyl domain is unchanged. The parameters of the interaction between cleaved E1 and the peripheral subunit-binding domain of the dihydrolipoyl acetyltransferase E2 component are identical to those of the wild-type E1. However, a pyruvate dehydrogenase complex assembled in vitro with cleaved E1p exhibits a markedly lower overall catalytic activity than that assembled with untreated E1 | Geobacillus stearothermophilus |