Allosterically modified
an allosteric enzyme
answer is D! lol i love Plato
Allosteric regulation involves a molecule binding to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and activity. Competitive inhibition involves a molecule binding to the active site of the enzyme, blocking substrate binding and enzyme activity.
The chemical reactions occur on the active site of an enzyme. The rest of the answers could include "substrate" for the molecule acted upon by the enzyme, "cofactor" for an additional substance required for enzyme activity, and "inhibitor" for a molecule that reduces enzyme activity.
These chemicals are called competitive inhibitors.
Competitive inhibition occurs when a molecule competes with the substrate for the active site of an enzyme, blocking its function. Allosteric inhibition, on the other hand, involves a molecule binding to a site other than the active site, causing a conformational change that inhibits enzyme activity.
Allosteric inhibition occurs when a molecule binds to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and reducing its activity. Noncompetitive inhibition, on the other hand, involves a molecule binding to the enzyme at a site other than the active site, but it does not change the enzyme's shape. This type of inhibition reduces the enzyme's activity by blocking the active site or altering the enzyme's ability to bind to the substrate.
Allosteric inhibition and competitive inhibition are two ways enzymes can be regulated. Allosteric inhibition occurs when a molecule binds to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and reducing its activity. Competitive inhibition, on the other hand, occurs when a molecule binds to the active site of the enzyme, blocking the substrate from binding and inhibiting the enzyme's activity. In summary, allosteric inhibition affects enzyme activity by binding to a site other than the active site, while competitive inhibition affects enzyme activity by binding to the active site directly.
ATP is an active molecule in cellular processes.
Allosteric inhibition occurs when a molecule binds to a site on an enzyme that is not the active site, causing a change in the enzyme's shape and reducing its activity. Noncompetitive inhibition, on the other hand, involves a molecule binding to the enzyme at a site other than the active site, which does not change the enzyme's shape but still reduces its activity.
Allosteric regulation involves a molecule binding to a site on the enzyme other than the active site, causing a conformational change that either activates or inhibits the enzyme. Noncompetitive inhibition involves a molecule binding to a site other than the active site, but it does not cause a conformational change. Instead, it blocks the active site, preventing substrate binding and enzyme activity.
Yes, both salinity and inhibitors can affect enzyme activity. There are two types of inhibitors, non-competitive and competitive inhibitors that will either bind to the allosteric or active site respectively.