KINETIC CONSTANT No Na2HPO4 25mM Na2HPO4 50mM Na2HPO4 Vmax nmol p-NP. Min- 20.3252 14.30615 17.30104 Km mM -0.819106 -0.46495 -0.352941 1. What does this suggest about the structure of the active side of the enzyme?
Active site is the site where a substrate molecule binds with an enzyme. The binding between a substrate molecule and active site of an enzyme is highly specific. Vmax is the maximum velocity at which an enzyme can convert substrate molecules into product. And Km (Michaelis-Menten constant) is the substrate concentration that is required to attain half of the maximum velocity. Km value indicates the affinity of the enzyme for substrates. A high Km value indicates low affinity between enzyme and substrate, while a low Km value indicates high affinity between enzyme and substrate. Inhibitors are substances that inhibit the enzyme activity reversibly or irreversibly by binding to the active site or allosteric site or an enzyme-substrate complex. The binding of specific inhibitors causes changes in the Vmax and Km values of the enzymes.
Step by step
Solved in 3 steps
