Role of excess lipoyl dehydrogenase in reconstituted alpha-ketoglutarate dehydrogenase complex of Escherichia coli.
The alpha-ketoglutarate dehydrogenase complex of Escherichia coli can bind up to 12 dimers of dihydrolipoyl dehydrogenase (E3) besides those already present. Maximal activity does not increase, however, when surplus E3 is present. This observation was previously interpreted to mean that the excess enzyme is inactive. We have now determined that if the reactions catalyzed by E3 are made rate-limiting, the excess E3 functions equivalently to that in the native complex.
D008058:Dihydrolipoamide Dehydrogenase / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D007655:Ketoglutarate Dehydrogenase Complex / Q000378:metabolism*; D007658:Ketone Oxidoreductases / Q000378:metabolism*; D007700:Kinetics; D009243:NAD / Q000378:metabolism; D013329:Structure-Activity Relationship
D009243:NAD; D007658:Ketone Oxidoreductases; D007655:Ketoglutarate Dehydrogenase Complex; D008058:Dihydrolipoamide Dehydrogenase