Explain the role of allosteric site in enzyme inhibition?
Answers
Answered by
4
hiiii
Enzymes work at different speeds depending on their environment. The rate at which the enzyme does its job is called enzyme activity. How hot or cold the environment is, the pH, the location in the body, and what other substances are around all influence enzyme activity.
Some substances bind the enzyme at a site other than the active site. This other site is called the allosteric site. The allosteric siteallows molecules to either activate or inhibit, or turn off, enzyme activity. These molecules bind the allosteric site and change the confirmation, or shape, of the enzyme.
Molecules that turn off enzymes are called allosteric inhibitors. Allosteric inhibitors change how the active site is shaped and prevents it from binding, or attaching, to the substrate. If the enzyme can't attach to the substrate, it can't do its job! These molecules and the allosteric site to which they bind are like the 'off switch' for the enzyme.
Allosteric activators on the other hand, make the enzyme more efficient. They change the shape of the enzyme, like allosteric inhibitors, but they make the enzyme better able to bind the substrate, instead of worse. This makes the enzyme do its job better. These molecules and their allosteric sites are like the 'on switch' for the enzyme.
hope it helps u
plz mark me brainlist
#RUDEBOY
Enzymes work at different speeds depending on their environment. The rate at which the enzyme does its job is called enzyme activity. How hot or cold the environment is, the pH, the location in the body, and what other substances are around all influence enzyme activity.
Some substances bind the enzyme at a site other than the active site. This other site is called the allosteric site. The allosteric siteallows molecules to either activate or inhibit, or turn off, enzyme activity. These molecules bind the allosteric site and change the confirmation, or shape, of the enzyme.
Molecules that turn off enzymes are called allosteric inhibitors. Allosteric inhibitors change how the active site is shaped and prevents it from binding, or attaching, to the substrate. If the enzyme can't attach to the substrate, it can't do its job! These molecules and the allosteric site to which they bind are like the 'off switch' for the enzyme.
Allosteric activators on the other hand, make the enzyme more efficient. They change the shape of the enzyme, like allosteric inhibitors, but they make the enzyme better able to bind the substrate, instead of worse. This makes the enzyme do its job better. These molecules and their allosteric sites are like the 'on switch' for the enzyme.
hope it helps u
plz mark me brainlist
#RUDEBOY
Similar questions