Well, unlike competitive inhibitors the non-competitive inhibitors will not compete the active site of the enzyme with substrate . Instead, it will combine with the enzyme somewhere except the ative site and alter the whole shape of the enzymes therefore the active site of substrate and enzyme are not the same and therefore no enzyme-substrate complex can be formed and the enzymatic effect can't be restored becausr the enzymes are now denatured
A "non-competitive activator" doesn't exist; however, there is a non-competitive inhibitor. An inhibitor would inhibit a process, holding it back. A non-competitive inhibitor would decrease enzyme activity.
it unravels the enzyme causing it to denaturate
The shape of the active site is distorted.
Inhibited. Competitive, noncompetitive, allosterically and so on.
Denature enzyme activity
Prosthetic groups can be as simple as a single metal ion bound into the enzyme's structure, or may be a more complicated organic molecule (which might also contain a metal ion). it is permanently bonded to enzyme. Activator is only metal ion that is detachable. source:chemguide.co.uk Stuffidious.com
The optimum pH for activity of Peroxidase is 5-7 that is about neutral. The Hydrochloric acid reduces the pH and thus inactivates the enzyme with reducing pH.
Several factors affect the rate at which enzymatic reactions proceed - temperature, pH, enzyme concentration, substrate concentration, and the presence of any inhibitors or activator
The shape of the active site is distorted.
No change in enzyme activity would be observed.
A noncompetitive inhibitor has a structure that does not resemble the substrate structure. A compound that binds to the surface of an enzyme, and changes its shape so that a substrate cannot enter the active site is called a noncompetitive inhibitor.
No. Remember what "inhibit" means: to hold back; restrain. Both non-competitive and competitive inhibitors affect enzymes by preventing the substrate from binding, though they differ in their methods. The opposite of an inhibitor is called an activator. So when you see the word "inhibitor," you know the functionality of the enzyme will decrease, and when you see the word "activator," you know the functionality of the enzyme will increase. The adjective before "inhibitor" or "activator" will ultimately tell you how the enzyme is inhibited or activated.
A competitive inhibitor often binds to an enzyme's active site. Noncompetitive inhibitors usually bind to a different site on the enzyme.
the precise location on the enzyme to which they bind
Inhibited. Competitive, noncompetitive, allosterically and so on.
temperature
Shape of substrate, shape of the enzyme, Competitive, noncompetitive and allosteric inhibitors.
The enzyme becomes saturated by the substrate and enzyme activity plateaus.
When an enzyme is frozen, it only slows down activity. Unlike boiling an enzyme, it does not stop it from working.