Evans sandbox 1: Difference between revisions
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{{STRUCTURE_1lvl | PDB=1lvl | SCENE= }} | {{STRUCTURE_1lvl | PDB=1lvl | SCENE= }} | ||
==General== | ==General== | ||
Dihydrolipoamide dehydrogenase(E3), a component of the Saccharomyces cerevisiae and mammalian [[Pyruvate dehydrogenase]] complexes (PDC), anchors an E3 homodimer inside each of the 12 pentagonal faces of the 60-mer dihydrolipoamide acetyltransferase (E2)[http://pubs.acs.org/doi/full/10.1021/bi9600254?prevSearch=%2528Dihydrolipoamide%2Bdehydrogenase%2B%2528E3%2529%2529%2BNOT%2B%255Batype%253A%2Bad%255D%2BNOT%2B%255Batype%253A%2Bacs-toc%255D&searchHistoryKey=] PDC is the enzyme in the citric acid cycle responsible for the reaction converting Pyruvate to Acetyl CoA, NAD+ to NADH and H+ and the release of carbon dioxide. | Dihydrolipoamide dehydrogenase(E3), a component of the Saccharomyces cerevisiae and mammalian [[Pyruvate dehydrogenase]] complexes (PDC), anchors an E3 homodimer inside each of the 12 pentagonal faces of the 60-mer dihydrolipoamide acetyltransferase (E2)[http://pubs.acs.org/doi/full/10.1021/bi9600254?prevSearch=%2528Dihydrolipoamide%2Bdehydrogenase%2B%2528E3%2529%2529%2BNOT%2B%255Batype%253A%2Bad%255D%2BNOT%2B%255Batype%253A%2Bacs-toc%255D&searchHistoryKey=] PDC is the enzyme in the citric acid cycle responsible for the reaction converting Pyruvate to Acetyl CoA, NAD+ to NADH and H+ and the release of carbon dioxide. Pyruvate dehydrogenase is regulated by the competition of binding to E3 by NADH and NAD+ | ||
E3 is common to all a-ketoacid dehydrogenase complexes. Errors in the gene coding human E3 cause combined deficiencies in a-ketoacid dehydrogenase complexes manifested by lactic acidemias and Maple Syrup Urine Disease[http://en.wikipedia.org/wiki/Maple_syrup_urine_disease]. A subset of the human E3 mutations has been suggested to occur at the homodimer interface or at the putative E3/E3BP interaction surface | E3 is common to all a-ketoacid dehydrogenase complexes. Errors in the gene coding human E3 cause combined deficiencies in a-ketoacid dehydrogenase complexes manifested by lactic acidemias and Maple Syrup Urine Disease[http://en.wikipedia.org/wiki/Maple_syrup_urine_disease]. A subset of the human E3 mutations has been suggested to occur at the homodimer interface or at the putative E3/E3BP interaction surface | ||