Shiraki H, Ogawa H, Matsuda Y, Nakagawa H
Biochim Biophys Acta. 1979 Feb 9;566(2):345-52. doi: 10.1016/0005-2744(79)90038-x.
The problems of whether the kinetic and regulatory properties of AMP deaminase were modified by formation of a deaminase-myosin complex were investigated with an enzyme preparation from rat skeletal muscle. Results showed that AMP deaminase was activated by binding to myosin. Myosin-bound AMP deaminase showed a sigmoidal activity curve with respect to AMP concentration in the absence of ATP and ADP, but a hyperbolic curve in their presence. Addition of ATP and ADP doubled the V value, but did not affect the Km value. Myosin-bound AMP deaminase also gave a sigmoidal curve in the presence of alkali metal ions, whereas free AMP deaminase gave a hyperbolic curve. GTP abolished the activating effects of both myosin and ATP.
利用大鼠骨骼肌的酶制剂，研究了AMP脱氨酶的动力学和调节特性是否因脱氨酶-肌球蛋白复合物的形成而改变。结果表明，AMP脱氨酶通过与肌球蛋白结合而被激活。在没有ATP和ADP的情况下，与肌球蛋白结合的AMP脱氨酶相对于AMP浓度呈现S形活性曲线，但在有ATP和ADP存在时呈现双曲线。添加ATP和ADP使V值加倍，但不影响Km值。在碱金属离子存在下，与肌球蛋白结合的AMP脱氨酶也呈现S形曲线，而游离的AMP脱氨酶呈现双曲线。GTP消除了肌球蛋白和ATP的激活作用。
