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What blocks enzyme activity by binding to allosteric site of an enzyme causing the enzyme's active site to change shape?
Allosteric inhibitors bind to a specific site on an enzyme (allosteric site) other than the active site, inducing a conformational change that decreases enzyme activity. This alteration prevents the substrate from binding to the active site, thus blocking the enzyme's ability to catalyze reactions.
Where do non-competitive inhibitors bind in relation to the enzyme's active site?
Non-competitive inhibitors bind to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and preventing the substrate from binding effectively.
What is the place where the substrate attaches to the enzyme?
The active site is where the substrate binds to the enzyme. It is a region on the enzyme where the chemical reaction takes place. The active site is specific to the substrate molecule, allowing for precise catalysis to occur.
How does allosteric inhibition differ from noncompetitive inhibition in terms of their mechanisms of action on 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.
Explain the difference between substrate and active site?
The substrate is the molecule that binds to the active site of an enzyme. The active site is a region on the enzyme where the substrate binds and undergoes a chemical reaction. The specificity of the active site allows only certain substrates to bind and react with the enzyme.
What blocks enzyme activity by binding to allosteric site of an enzyme causing the enzyme's active site to change shape?
Allosteric inhibitors bind to a specific site on an enzyme (allosteric site) other than the active site, inducing a conformational change that decreases enzyme activity. This alteration prevents the substrate from binding to the active site, thus blocking the enzyme's ability to catalyze reactions.
What is an active site and where is it located?
A region on an enzyme that binds to a protein or other substance during a reaction
Where do non-competitive inhibitors bind in relation to the enzyme's active site?
Non-competitive inhibitors bind to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and preventing the substrate from binding effectively.
What is the place where the substrate attaches to the enzyme?
The active site is where the substrate binds to the enzyme. It is a region on the enzyme where the chemical reaction takes place. The active site is specific to the substrate molecule, allowing for precise catalysis to occur.
How does allosteric inhibition differ from noncompetitive inhibition in terms of their mechanisms of action on 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.
Explain the difference between substrate and active site?
The substrate is the molecule that binds to the active site of an enzyme. The active site is a region on the enzyme where the substrate binds and undergoes a chemical reaction. The specificity of the active site allows only certain substrates to bind and react with the enzyme.
What will happen to the enzyme active site after NADH binds there?
After NADH binds to the enzyme's active site, it will undergo a redox reaction where it donates electrons to the enzyme. This interaction may induce a conformational change in the enzyme, allowing it to carry out its catalytic function in the metabolic pathway.
How can the allosteric site affect the active site?
The binding of a molecule at the allosteric site can induce a conformational change in the enzyme, affecting the active site's shape and activity. This can either increase or decrease the enzyme's affinity for its substrate, leading to changes in the enzyme's catalytic efficiency.
What is an enzyme's active site?
An enzyme's active site is a groove or dip in the enzyme that is shaped for a particular substrate to attach to.
What is the site on the surface of an enzyme where a reactant binds to the enzyme is called?
The site on the surface of an enzyme where a reactant binds is called the active site. This is where the chemical reaction takes place between the enzyme and its substrate. The active site has a specific shape that allows it to bind with the substrate molecule.
How might an amino acid change at a site distant from the active site of the enzyme alter the enzyme's substrate specificity?
An amino acid change distant from the active site can impact the enzyme's conformation and flexibility, leading to changes in the active site shape and size. This can alter how substrates bind to the active site, affecting substrate specificity. Additionally, changes in distant amino acids can cause conformational changes that transmit through the protein, ultimately affecting enzyme-substrate interactions.
What is the part of the enzyme that binds with the substrate?
The active site is the part of the enzyme that binds with the substrate. It is where the catalytic activity of the enzyme takes place. The active site is specific to the substrate, allowing for selective binding and catalysis.
