Introducing
Your new presentation assistant.
Refine, enhance, and tailor your content, source relevant images, and edit visuals quicker than ever before.
Trending searches
How Enzyme-mediated Reactions can be Controlled through Diff
32
Noncompetitive Inhibitors
Noncompetitive inhibitors do not directly compete with a substrate to bind to the enzyme at the active site. In contrast to competitive inhibitors, they interfere enzymatic reactions by binding to another part of the enzyme. The particular interaction causes the protein to change its shape which leaves the active site less effective at catalyzing the conversion of substrates into products. Due to the change in shape of the enzyme, the active site is less effective because the shape determines the function of the enzyme.
Competitive Inhibitors
A substrate can normally bind to the active site of the an enzyme. A competitive inhibitor mimics the substrate, and competes for the active site
Competitive Inhibitors
Competitive inhibitors reduce the productivity of enzymes by blocking the substrates from entering the active sites of the enzymes. This kind of inhibition can be overcome by increasing the concentration of the substrate so that as active sites become available, more substrate molecules than inhibitor molecules are present to gain access entry to the sites.