You have a new enzyme at your hand and you have completed some kinetic studies with this enzyme in the presence and absence of two inhibitors. One inhibitor is a substrate analog and the other is an alkylating agent. The results of your experiment are given below. The concentration of inhibitor A is 5mM and that of B is 3.2 uM. Determine a)Km and vmax values for the uninhibited reaction. What is the inhibition constant Ki for A and B. given [S] mM {5.0, 2.5, 1.7, 1.2, 1.0}; v(umole/min) No inhibitor {1.25, 0.87, 0.67, 0.54, 0.45}: v(umole/min) Inhibitor A {0.74, 0.45, 0.32, 0.25, 0.21}:v(umole/min) inhibitor B {0.48, 0.33,0.25, 0.20, 0.17} draw the Lineweaver burk plots and identify which inhibitor is substrate analog and which is the alkylating agent.
You have a new enzyme at your hand and you have completed some kinetic studies with this enzyme in the presence and absence of two inhibitors. One inhibitor is a substrate analog and the other is an alkylating agent. The results of your experiment are given below. The concentration of inhibitor A is 5mM and that of B is 3.2 uM. Determine a)Km and vmax values for the uninhibited reaction. What is the inhibition constant Ki for A and B. given [S] mM {5.0, 2.5, 1.7, 1.2, 1.0}; v(umole/min) No inhibitor {1.25, 0.87, 0.67, 0.54, 0.45}: v(umole/min) Inhibitor A {0.74, 0.45, 0.32, 0.25, 0.21}:v(umole/min) inhibitor B {0.48, 0.33,0.25, 0.20, 0.17} draw the Lineweaver burk plots and identify which inhibitor is substrate analog and which is the alkylating agent.
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