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In enzymatic reactions, competitive inhibitors are proteins or molecules that block the active site of an enzyme, preventing substrate binding. An example of such a protein is the competitive inhibitor of the enzyme dihydrofolate reductase, which can be used in cancer treatment. These inhibitors mimic the substrate's shape, allowing them to fit into the active site and inhibit the enzyme's activity.

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2w ago

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An enzyme attaches to substrates at a region known as?

The Active Site. If the protein is denatured however, the active site loses shape and the substrates don't fit in the active site (subtrates are "put together" by the enzyme at the active site).


What is the most active site of protein synthesis?

The "ribosomes".


Which two levels of protein structure principally determine the active site of an enzyme?

The primary and secondary levels of protein structure determine the active site of an enzyme. The specific arrangement of amino acids in the active site, influenced by both the primary sequence and secondary structures such as alpha helices and beta sheets, is critical for enzyme-substrate interactions.


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


Can the active site of an enzyme be damaged at very high pH levels?

The active site of an enzyme can very much be influenced and damaged by a very high pH level. An enzyme is a protein, and because of that it is very sensitive to pH levels. High pH can denature a protein, and thus "damage" the active site.


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.


The region of a protein that binds a ligand?

The region on a protein that binds a ligand is known as the binding site. This site is typically composed of specific amino acids that interact with the ligand through various chemical bonds and molecular interactions. The binding of the ligand to the protein's binding site is crucial for the protein's function and activity.


How are amino acids held close together to form the active site?

The active site exists as a natural consequence of the shape of the rest of the protein. Essentially, the peptide residues in the active site are held in position by the intramolecular forces that give the protein as a whole its conformation.


Where on protease does a protein bond itself to?

It depends on the protease, but as with all enzymes, the substrate binds to the active site.


Does the shape of an enzyme protein determine specificity?

Shape of an enzyme specifically shape of its active site determines enzyme specificity .


How will you establish that a given protein having hydrolase activity involves active serine residue at its active site?

a diagnostic test for the presence of the active ser is it's reaction with diisopropylphosphofluoridate(DIPF) which irreversibly inactivates the enzyme.Other ser residues including those on the same protein, do not interact with DIPF.


An enzyme is a protein with a pocket on its surface called an?

An enzyme is a protein with a pocket on its surface called an active site. This is where the binding of substrate molecules take place and where chemical reaction happens.