What is the substrate used in the enzyme kinetics lab?

What is the substrate used in the enzyme kinetics lab?

In all enzymes are extremely important to the reactions that take place within our bodies and cells. Specific to this lab, catalase was the enzyme used and hydrogen peroxide was the substrate used.

What is Michaelis Menten enzyme kinetics?

Michaelis-Menten kinetics, a general explanation of the velocity and gross mechanism of enzyme-catalyzed reactions. First stated in 1913, it assumes the rapid reversible formation of a complex between an enzyme and its substrate (the substance upon which it acts to form a product).

How does substrate concentration affect the kinetics of an enzyme?

As the number of substrate molecules increases, the enzyme attains the saturation level, since there is no more reaction sites remaining for binding. So the enzyme can work with full capacity and its reaction rate is independent of substrate concentration. (Phase II).

How is the kinetic value of an enzyme determined?

A competitive inhibitor reduces the concentration of free enzyme available for substrate binding (1). The value of Ki for a competitive inhibitor can be determined from the plot of K appKM = (1+ [I]/K i) K M versus inhibitor concentration, [I]; its intercept on the [I] axis, – K I.

How does competitive inhibition of an enzyme work?

In competitive inhibition, the inhibitor competes directly with a normal substrate for an enzyme’s substrate-binding site (1). An inhibitor such as this resembles the substrate structure but does not perform the same reactions as the normal substrate; instead it inhibits the active site of the enzyme.

Where does the enzyme bind to the substrate?

In the enzyme- substrate complex, the substrate molecule binds to a very specific region of the enzyme molecule called the active site. These active sites are highly selective for a specific substrate molecule with which the enzyme binds.