When is km equivalent to kd

Since your Km is smaller than Ki, this implies the substrate binds more tightly to the enzyme active site than does the inhibitor. But the inhibitor will also occupy the active site significantly since their K values aren't that much different.

If the Km of the substrate is equal to the dissociation constant of the substrate Kd, and Ki is greater than Km, which binds more tightly, the inhibitor or the substrate? Mar 18, See below. Related questions How do I determine the molecular shape of a molecule? What is the lewis structure for co2? What is the lewis structure for hcn? How is vsepr used to classify molecules?

The key difference between Kd and Km is that Kd is a thermodynamic constant whereas Km is not a thermodynamic constant. Kd refers to dissociation constant while Km is the Michaelis constant. Both these constants are very important in the quantitative analysis of enzymatic reactions. Overview and Key Difference 2. What is Kd 3. What is Km 4. Kd is dissociation constant. It is also known as equilibrium dissociation constant due to its use in equilibrium systems. The dissociation constant is the equilibrium constant of reactions where a large compound is converted into small components reversibly.

The process of this conversion is also known as dissociation. An ionic molecule always dissociates into its ions. Then the dissociation constant or Kd is a quantity expressing the extent to which a particular substance in solution dissociates into ions. Thus, this is equal to the product of the concentrations of the respective ions divided by the concentration of the un-dissociated molecule.

Moreover, if there is a stoichiometric relationship, one should include the stoichiometric coefficients in the equation. Specifically, in biochemical applications, Kd helps to determine the amount of products given by a chemical reaction in the presence of an enzyme. The Kd of an enzymatic reaction expresses the ligand-receptor affinity. In other words, it states the capability of a substrate to leave the receptor of an enzyme. On the other hand, it describes how strongly a substrate binds to the enzyme.

Km is the Michaelis constant. Unlike Kd, Km is a kinetic constant.