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If you have an enzymatic reaction proceeding at the optimum pH and optimum temperature You add a competitive inhibitor to the reaction and notice that the reaction slows down?
Wiki User
∙ 14y ago
Exactly. If a reaction is going as fast as it can go (optimum) and you add an inhibitor (something to impede it) it slows down. This could be done to prevent excessive heat or too much gas at one time.
Wiki User
∙ 14y ago
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Is copper sulfate a competitive or noncompetitive inhibitor?
Non-Competitive Inhibitor
How does a non-competitive activator affect enzyme activity?
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
What inhibitor binds into the active site of an enzyme not allowing the subrtate to bind?
This would be a competitive inhibitor. It can be a structural analog of the substrate. This type of inhibition can be out competed by adding more substrate. A competitive inhibitor increases the Km of the enzyme.
What is the purpose of using malonic acid in this experiment?
it is a competitive inhibitor
What is an inhibitor that forms a covalent bond with an amino acid side group within the active site?
Competitive inhibitor source - AP Bio Text Book
What statement best describes the function of a competitive inhibitor in an enzyme-catalyzed reaction?
Competitive inhibitor is a substance that competes directly with a normal substrate for an enzymatic-binding site of an enzyme. Such an inhibitor usually resembles the substrate to the extent that it specifically binds to the active site of the enzyme but differs from it so as to be unreactive and therefore there will be no catalytic reaction. Some examples are: methotrexate that is competitive inhibitor of dihydrofolate reductase, and malonate which structurally resembles succinate (that is converted to fumarate by succinate dehydrogenase during the citric acid cycle) but cannot be dehydrogenated.
Is copper sulfate a competitive or noncompetitive inhibitor?
Non-Competitive Inhibitor
What happens the reaction time with a competitive inhibitor?
with a competitive inhibitor the reaction time proceeds slowly.
Is PTU a competitive inhibitor?
non-competitive
Is penicillin an competitive inhibitor?
yes it is
Is penicillin a non-competitive inhibitor?
no
How does a non-competitive activator affect enzyme activity?
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
What inhibitor binds into the active site of an enzyme not allowing the subrtate to bind?
This would be a competitive inhibitor. It can be a structural analog of the substrate. This type of inhibition can be out competed by adding more substrate. A competitive inhibitor increases the Km of the enzyme.
What inhibitor has a structure that is so similar to the substrate that it can bond to the enzyme just like the substrate?
Competitive inhibitor. It is termed to be an analogue. It is also known to sometimes act as a "catalytic poison".
What does a repressor do in the enzymes active site?
Repressors bind to the silencers in the DNA to block the RNA polymerase from binding to the promoter of the gene to reduce gene expression, not really binding to enzymes active sites I think what you meant was "what does an inhibitor do to the enzymes active site"? In which case, it depends on the type of inhibitor. A competitive inhibitor has a structure similar to the substrate, hence would bind to the active site as well, competing with the substrate for the enzyme active sites, decreasing enzymatic activity. A non-competitive inhibitor binds to the allosteric site of the enzyme, causing a structural change in the enzyme active site shape. Hence the enzyme would not be able to bind to the original substrate, so enzymatic activity comes to a halt for the enzymes that are bound by the non-competitive inhibitors
What happens to the vmax when a competitive reversible inhibitor is added to an enzyme?
The vmax stays the same as the competitive reversible inhibitor does not affect catalysis in the enzyme-substrate.
Inhibitors that decrease an enzymes activity by binding to the active site?
I would just call it an inhibitor. An inhibitor may be a small molecule,such as a metal or it may be a protein.
