Kempner D H, Johnson B J
J Pharm Sci. 1976 Dec;65(12):1799-801. doi: 10.1002/jps.2600651226.
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.
五种非离子去污剂增强了L-谷氨酸脱氢酶[L-谷氨酸：烟酰胺腺嘌呤二核苷酸磷酸氧化还原酶（脱氨基）（EC 1.4.1.3）]的活性。这些去污剂激活了该酶对α-酮戊二酸还原的作用，导致该酶对鸟苷5-三磷酸变构调节的敏感性降低。修饰剂腺苷5-二磷酸对该酶L-谷氨酸脱氢酶活性的增强作用也减弱了。这些去污剂可能会使酶发生构象变化，这种变化可能导致α-酮戊二酸还原的底物结合增加。伴随这种构象变化的将是修饰剂鸟苷5'-三磷酸结合的减少，而腺苷5'-二磷酸修饰剂的结合没有相应变化。
