Question

Biochem Lab: Explain how an inhibitor could bind to an enzyme active site and reduce the V_max but not alter the K_m. Draw a reaction diagram like discussed in the pre-lab for lab 10 to illustrate. Also, name this type of inhibitor.

Answer 1

Reversible inhibitors tie non-covalently to chemicals, and a wide range of kinds of restraint can happen contingent upon what the inhibitors tie to. The non-covalent connections between the inhibitors and proteins incorporate hydrogen securities, hydrophobic communications, and ionic securities. A significant number of these feeble bonds join to deliver solid and explicit authoritative. As opposed to substrates and irreversible inhibitors, reversible inhibitors for the most part don't experience concoction responses when bound to the chemical and can be effectively evacuated by weakening or dialysis

Most reversible inhibitors pursue the great Michaelis-Menten plot, where a chemical (E) ties to its substrate(S) to shape a catalyst substrate complex (ES). km is the Michaelis consistent that compares to the convergence of the substrate when the speed is a large portion of the greatest. Vmax is the greatest speed of the catalyst.

Competitive inhibitors can only bind to E and not to ES. They increase Km by interfering with the binding of the substrate, but they do not affect Vmax because the inhibitor does not change the catalysis in ES because it cannot bind to ES.