Understanding Active Sites - Biology

Proteins can be inhibited in numerous ways by different types of inhibitors. Competitive inhibitors will compete with substrate for the active site to block the protein from performing its function. If there is enough substrate and very little competitive inhibitor, proteins will perform their functions almost as if there were no competitive inhibitors.

In contrast, allosteric inhibitors bind to regions of the protein away from the active site, but change the shape of the active site such that substrate cannot bind. Since there is no direct competition, increasing substrate concentration cannot overcome allosteric inhibition. Non-competitive inhibition is a type of allosteric inhibition. Uncompetitive inhibition occurs when the inhibitor will only bind to the enzyme-substrate complex, locking the substrate in place and preventing other substrates from binding.

The active site on a protein is the area where a substrate can attach. This relationship is most often described using a metaphor of a lock and a key because each protein has an active site specific to one substrate much like a lock can only be opened by one key.

The key here is to know that if something binds the enzyme at a location other than the active site, the type of modification is defined as allosteric. The other words more generally describe things that can bind to receptors, enzymes, etc., but the best and most specific answer is "allosteric."

It is important to know that when exposed to high temperatures, all proteins become denatured, and lose their native shape/conformation.

This has nothing to do with the activation energy of the reaction (eliminating that answer). While some substrates may be degraded at high temperatures, the word "all" renders this answer incorrect, nor does this describe what happens to the enzyme. Covalent modificatinos can change enzymatic function, but do not have anything to do with higher temperature.

The correct answer is that the enzyme itself is denatured, thus changing the shape and the way the active site is shaped, resulting in an inability to efficiently bind its substrate. The structure of the enzyme is dictated by intermolecular forces, which are susceptible to interference from temperature changes (unlike covalent bonds).

Competitive inhibition is the only type of inhibition in which the inhibitor molecule directly binds the active site of the enzyme, thereby 'competing' with the actual substrate for location on the enzyme. The other choices involve binding elsewhere on the enzyme (non-competitive) or binding the enzyme-substrate complex but not an isolated enzyme (mixed), but none of them describe binding the active site except for competitive.

Proteins can be inhibited in numerous ways by different types of inhibitors. Competitive inhibitors will compete with substrate for the active site to block the protein from performing its function. If there is enough substrate and very little competitive inhibitor, proteins will perform their functions almost as if there were no competitive inhibitors.

In contrast, allosteric inhibitors bind to regions of the protein away from the active site, but change the shape of the active site such that substrate cannot bind. Since there is no direct competition, increasing substrate concentration cannot overcome allosteric inhibition. Non-competitive inhibition is a type of allosteric inhibition. Uncompetitive inhibition occurs when the inhibitor will only bind to the enzyme-substrate complex, locking the substrate in place and preventing other substrates from binding.

The active site on a protein is the area where a substrate can attach. This relationship is most often described using a metaphor of a lock and a key because each protein has an active site specific to one substrate much like a lock can only be opened by one key.

The key here is to know that if something binds the enzyme at a location other than the active site, the type of modification is defined as allosteric. The other words more generally describe things that can bind to receptors, enzymes, etc., but the best and most specific answer is "allosteric."

It is important to know that when exposed to high temperatures, all proteins become denatured, and lose their native shape/conformation.

This has nothing to do with the activation energy of the reaction (eliminating that answer). While some substrates may be degraded at high temperatures, the word "all" renders this answer incorrect, nor does this describe what happens to the enzyme. Covalent modificatinos can change enzymatic function, but do not have anything to do with higher temperature.

The correct answer is that the enzyme itself is denatured, thus changing the shape and the way the active site is shaped, resulting in an inability to efficiently bind its substrate. The structure of the enzyme is dictated by intermolecular forces, which are susceptible to interference from temperature changes (unlike covalent bonds).

Competitive inhibition is the only type of inhibition in which the inhibitor molecule directly binds the active site of the enzyme, thereby 'competing' with the actual substrate for location on the enzyme. The other choices involve binding elsewhere on the enzyme (non-competitive) or binding the enzyme-substrate complex but not an isolated enzyme (mixed), but none of them describe binding the active site except for competitive.

Proteins can be inhibited in numerous ways by different types of inhibitors. Competitive inhibitors will compete with substrate for the active site to block the protein from performing its function. If there is enough substrate and very little competitive inhibitor, proteins will perform their functions almost as if there were no competitive inhibitors.

In contrast, allosteric inhibitors bind to regions of the protein away from the active site, but change the shape of the active site such that substrate cannot bind. Since there is no direct competition, increasing substrate concentration cannot overcome allosteric inhibition. Non-competitive inhibition is a type of allosteric inhibition. Uncompetitive inhibition occurs when the inhibitor will only bind to the enzyme-substrate complex, locking the substrate in place and preventing other substrates from binding.

The active site on a protein is the area where a substrate can attach. This relationship is most often described using a metaphor of a lock and a key because each protein has an active site specific to one substrate much like a lock can only be opened by one key.

The key here is to know that if something binds the enzyme at a location other than the active site, the type of modification is defined as allosteric. The other words more generally describe things that can bind to receptors, enzymes, etc., but the best and most specific answer is "allosteric."

It is important to know that when exposed to high temperatures, all proteins become denatured, and lose their native shape/conformation.

This has nothing to do with the activation energy of the reaction (eliminating that answer). While some substrates may be degraded at high temperatures, the word "all" renders this answer incorrect, nor does this describe what happens to the enzyme. Covalent modificatinos can change enzymatic function, but do not have anything to do with higher temperature.

The correct answer is that the enzyme itself is denatured, thus changing the shape and the way the active site is shaped, resulting in an inability to efficiently bind its substrate. The structure of the enzyme is dictated by intermolecular forces, which are susceptible to interference from temperature changes (unlike covalent bonds).

Competitive inhibition is the only type of inhibition in which the inhibitor molecule directly binds the active site of the enzyme, thereby 'competing' with the actual substrate for location on the enzyme. The other choices involve binding elsewhere on the enzyme (non-competitive) or binding the enzyme-substrate complex but not an isolated enzyme (mixed), but none of them describe binding the active site except for competitive.

Proteins can be inhibited in numerous ways by different types of inhibitors. Competitive inhibitors will compete with substrate for the active site to block the protein from performing its function. If there is enough substrate and very little competitive inhibitor, proteins will perform their functions almost as if there were no competitive inhibitors.

In contrast, allosteric inhibitors bind to regions of the protein away from the active site, but change the shape of the active site such that substrate cannot bind. Since there is no direct competition, increasing substrate concentration cannot overcome allosteric inhibition. Non-competitive inhibition is a type of allosteric inhibition. Uncompetitive inhibition occurs when the inhibitor will only bind to the enzyme-substrate complex, locking the substrate in place and preventing other substrates from binding.

The active site on a protein is the area where a substrate can attach. This relationship is most often described using a metaphor of a lock and a key because each protein has an active site specific to one substrate much like a lock can only be opened by one key.

The key here is to know that if something binds the enzyme at a location other than the active site, the type of modification is defined as allosteric. The other words more generally describe things that can bind to receptors, enzymes, etc., but the best and most specific answer is "allosteric."

It is important to know that when exposed to high temperatures, all proteins become denatured, and lose their native shape/conformation.

This has nothing to do with the activation energy of the reaction (eliminating that answer). While some substrates may be degraded at high temperatures, the word "all" renders this answer incorrect, nor does this describe what happens to the enzyme. Covalent modificatinos can change enzymatic function, but do not have anything to do with higher temperature.

The correct answer is that the enzyme itself is denatured, thus changing the shape and the way the active site is shaped, resulting in an inability to efficiently bind its substrate. The structure of the enzyme is dictated by intermolecular forces, which are susceptible to interference from temperature changes (unlike covalent bonds).

Competitive inhibition is the only type of inhibition in which the inhibitor molecule directly binds the active site of the enzyme, thereby 'competing' with the actual substrate for location on the enzyme. The other choices involve binding elsewhere on the enzyme (non-competitive) or binding the enzyme-substrate complex but not an isolated enzyme (mixed), but none of them describe binding the active site except for competitive.