Lipid-protein interactions: enhancement of enzyme activity of L-glutamic acid dehydrogenase by nonionic detergents.
Five nonionic detergents enhanced the activity of L-glutamic acid dehydrogenase [L-glutamate:nicotinamide adenine dinucleotide phosphate oxidoreductase (deaminating) (EC 1.4.1.3)]. These detergents activated the enzyme toward alpha-ketoglutaric acid reduction, causing a decrease in the sensitivity of the enzyme to allosteric regulation by guanosine 5-triphosphate. There was also a diminution of the enhancing effect of the modifier adenosine 5-diphosphate on the enzyme's L-glutamic acid dehydrogenase activity. These detergents may cause a conformational change in the enzyme, and this change could lead to an increase in the binding of the substrates for the alpha-ketoglutaric acid reduction. Accompanied with this conformational change would be a decrease in the binding of the modifier guanosine 5'-triphosphate, with no concomitant change in the binding of the adenosine 5'-diphosphate modifier.
D000244:Adenosine Diphosphate / Q000494:pharmacology; D003902:Detergents / Q000494:pharmacology*; D004347:Drug Interactions; D005969:Glutamate Dehydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000494:pharmacology; D007700:Kinetics; D011768:Pyruvate Dehydrogenase Complex / Q000378:metabolism
D003902:Detergents; D011768:Pyruvate Dehydrogenase Complex; D000244:Adenosine Diphosphate; D006160:Guanosine Triphosphate; D005969:Glutamate Dehydrogenase