修饰赖氨酸-126对牛肝谷氨酸脱氢酶物理、催化及调节特性的影响
The effect of modifying lysine-126 on the physical, catalytic and regulatory properties of bovine liver glutamate dehydrogenase.
作者信息
Wallis R B, Holbrook J J
出版信息
Biochem J. 1973 May;133(1):173-82. doi: 10.1042/bj1330173.
Abstract
- The reaction of 4-iodoacetamidosalicylate with bovine liver glutamate dehydrogenase is dependent on pH. The pH-activity curve is bell-shaped and can be described by apparent pK values of 7.8+/-0.2 and 9.1+/-0.2. 2. Enzyme in which lysine-126 has been modified by 4-iodoacetamidosalicylate has unaltered sedimentation characteristics except when measured in the presence of GTP and NADH. 3. GTP binding to the inhibited enzyme is unaltered. However, GTP can no longer promote the binding of a second molecule of NADH, since this is already bound to the inhibited enzyme without GTP. 4. The equilibrium binding of ADP, GTP, NAD-sulphite and NADH (when measured at low concentrations) was largely unchanged by modification. 5. The number of binding sites for 2-oxoglutarate to the enzyme-NADH complex were decreased by 60% in an enzyme that has been inhibited by 70%.
摘要
- 4-碘乙酰氨基水杨酸与牛肝谷氨酸脱氢酶的反应取决于pH值。pH-活性曲线呈钟形，可用表观pK值7.8±0.2和9.1±0.2来描述。2. 赖氨酸-126已被4-碘乙酰氨基水杨酸修饰的酶，其沉降特性未改变，除非在GTP和NADH存在下进行测量。3. GTP与受抑制酶的结合未改变。然而，GTP不再能促进第二个NADH分子的结合，因为在没有GTP的情况下，NADH已经与受抑制酶结合。4. 修饰后，ADP、GTP、NAD-亚硫酸盐和NADH（在低浓度下测量时）的平衡结合基本未变。5. 在被70%抑制的酶中，2-氧代戊二酸与酶-NADH复合物的结合位点数量减少了60%。
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