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PDHX  -  pyruvate dehydrogenase complex, component X

Bos taurus

 
 
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High impact information on MGC143185

  • Similarities between the N-terminal region of E1 and the dihydrolipoamide acetyltransferase (E2) and E3-binding components (E3BP) of the pyruvate dehydrogenase complex are highlighted by the specific cross-reactivities of subunit-specific antisera [1].
  • These results suggest that during the transition to anaerobic metabolism, E3 remains unchanged, but it appears that a novel E3BP, p45, is expressed which may help to maintain the activity of the PDC in the face of the elevated intramitochondrial NADH/NAD+ ratios associated with anaerobiosis [2].
  • The evidence presented in this study indicates that the strong association of E3BP with E2 facilitates the binding of E3, the lipoamide dehydrogenase component, and therefore may have an important role in the assembly and ultimately the catalytic activity of the pyruvate dehydrogenase multienzyme complex [3].
  • The catalytic activity and the state of aggregation of the dihydrolipoyl transacetylase-lipoamide dehydrogenase binding protein (E2-E3BP) subcomplex of the bovine heart pyruvate dehydrogenase multienzyme complex were investigated [3].

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