Bartlett R T, Spivey H O
Enzyme. 1978;23(4):257-61. doi: 10.1159/000458587.
NADH substrate inhibition of bovine liver glutamate dehydrogenase appears to be eliminated at enzyme concentrations above 0.5mg/ml. Since the inhibition cannot be restored by preincubation of the enzyme with any substrate or product combination, the release of inhibition had previously been considered the result of enzyme polymerization. Benzene-saturated solutions, however, increase the extent of enzyme polymerization without affecting the NADH inhibition. These and related control measurements demonstrate that the release of substrate inhibition is the result of a hysteretic transition of an enzyme central and transitory complex.
牛肝谷氨酸脱氢酶的NADH底物抑制作用在酶浓度高于0.5mg/ml时似乎会消除。由于用任何底物或产物组合对酶进行预孵育都无法恢复这种抑制作用，因此之前认为抑制作用的解除是酶聚合的结果。然而，苯饱和溶液会增加酶的聚合程度，而不影响NADH抑制作用。这些及相关的对照测量结果表明，底物抑制作用的解除是酶中心瞬时复合物滞后转变的结果。
