A competitive inhibitor often binds to an enzyme's active site. Noncompetitive inhibitors usually bind to a different site on the enzyme.
A non-competitive inhibitor
Copper sulfate is a noncompetitive inhibitor. It binds to the enzyme at a site other than the active site, which results in a change in the enzyme's shape and prevents the substrate from binding effectively.
A noncompetitive inhibitor binds to a site on the enzyme that is not the active site.
A competitive inhibitor competes with the substrate to bind to the active site while a noncompetitive inhibitor binds to an allosteric site of the enzyme (one other than the active site). Thus no amount of substrate can overcome or in a sense interfere with the inhibitors binding to an allosteric site.
No, lactose is not a noncompetitive inhibitor. Lactose is a sugar found in milk that can act as an inducer for the lactose operon in bacteria, but it does not act as an inhibitor in enzyme kinetics.
Because you will still have the same number of enzymes inhibited. For example, you have 20 enzymes and 10 non-competitive inhibitors. Regardless of substrate concentration, at any one time, there will only be 10 enzymes available to accept a substrate. Increasing the substrate concentration does not affect this.
Competitive inhibitors compete with the substrate for the enzyme's active site, while noncompetitive inhibitors bind to a different site on the enzyme. Competitive inhibitors can be overcome by increasing substrate concentration, while noncompetitive inhibitors cannot. Both types of inhibitors reduce enzyme activity, but competitive inhibitors specifically affect the binding of the substrate, while noncompetitive inhibitors can alter the enzyme's shape or function.
A noncompetitive inhibitor binds to an enzyme at a site other than the active site, while an allosteric inhibitor binds to a different site on the enzyme, causing a change in the enzyme's shape and reducing its activity.
Allosteric inhibition is a type of noncompetitive inhibition.
Competitive inhibitors bind to the active site of the enzyme, competing with the substrate, while noncompetitive inhibitors bind to a site other than the active site, changing the enzyme's shape and preventing substrate binding. Competitive inhibitors can be overcome by increasing substrate concentration, while noncompetitive inhibitors cannot.
Cyanide is a non-competitive inhibitor that binds to the active site of the enzyme, inhibiting its activity by preventing the binding of the substrate. It disrupts the normal functioning of enzymes involved in cellular respiration, leading to a decrease in ATP production and ultimately cell death.