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How might a change of one amino acid at a site distant from the active site of an enzyme alter an enzyme's substrate specificity?
A change of one amino acid at a site distant from the active site of an enzyme can alter the enzyme's substrate specificity by affecting the overall conformation or stability of the enzyme. This alteration can influence how the enzyme binds to its substrate, either by modifying the shape of the active site or by impacting the enzyme's interactions with other molecules. Additionally, such a change might affect the dynamics of the enzyme, potentially enhancing or diminishing its ability to recognize particular substrates. Hence, even distant amino acid substitutions can have significant functional consequences on enzyme activity.
Suppose that enzyme X catalyzes a reaction that involves the breakdown of a molecule. The product of this reaction is an amino acid. What molecule is the enzyme breaking down?
it might be a protein.. since proteins are polymers of various amino acids..
Suppose that the amio acids that make up an enzyme's active site are changed how might this affect the enzyme?
Changing the amino acids in an enzyme's active site can alter the enzyme's shape, potentially disrupting the enzyme-substrate interactions crucial for catalysis. This alteration may result in reduced enzyme activity or even loss of function. The specificity and affinity of the enzyme for its substrate could also be affected, impacting the overall efficiency of the catalytic reaction.
How might this change affect the enzyme when they make up enzyme?
Changes in the environment, such as temperature or pH, can significantly affect enzyme activity. For instance, an increase in temperature may enhance reaction rates up to a certain point, but excessive heat can denature the enzyme, altering its structure and active site. Similarly, changes in pH can disrupt ionic and hydrogen bonds, leading to a loss of enzyme functionality. Overall, these changes can impact the enzyme's ability to bind substrates and catalyze reactions efficiently.
How might a point mutation in a gene affect the reasulting protein?
point mutations include substitutions insertions and deletions of a single nuceotide in DNA. CONSIDER: insertions and deletions have a greater effect on proteins that do substiutions because insertions and deletions affect every amino acid that is specified by the nucleotides that follow the point of mutation CONSIDER: a substitution affects a single amino acid a change in more than one amino acid is more likely to alter the ability of the protein to function narmally than is a change in a single amino acid CONSIDER: follow me on twitter @Rocco_Gone_Ham
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.
Suppose that enzyme X catalyzes a reaction that involves the breakdown of a molecule. The product of this reaction is an amino acid. What molecule is the enzyme breaking down?
it might be a protein.. since proteins are polymers of various amino acids..
If an enzyme is a protein how might you change the specificity of such an enzyme?
What an enzyme does is based on its shape, therefore you would have to change it on a molecular level in order to alter its job.
Suppose that the amio acids that make up an enzyme's active site are changed how might this affect the enzyme?
Changing the amino acids in an enzyme's active site can alter the enzyme's shape, potentially disrupting the enzyme-substrate interactions crucial for catalysis. This alteration may result in reduced enzyme activity or even loss of function. The specificity and affinity of the enzyme for its substrate could also be affected, impacting the overall efficiency of the catalytic reaction.
How might very low pH affect an enzyme's hydrogen bonds?
A very low pH can break the hydrogen bonds in an enzyme which causes the shape of the enzyme to change shape making the enzyme unable to do it's job. This is called "denaturation" However some enzymes such as pepsin only work in a low pH (pepsin works best in a pH of about 3) so it does depend on the enzyme.
How might a point mutation in a gene affect the reasulting protein?
point mutations include substitutions insertions and deletions of a single nuceotide in DNA. CONSIDER: insertions and deletions have a greater effect on proteins that do substiutions because insertions and deletions affect every amino acid that is specified by the nucleotides that follow the point of mutation CONSIDER: a substitution affects a single amino acid a change in more than one amino acid is more likely to alter the ability of the protein to function narmally than is a change in a single amino acid CONSIDER: follow me on twitter @Rocco_Gone_Ham
Altering the three-dimensional structure of an enzyme might?
prevent the substrate from binding the enzyme's active site
How do changes in pH and temperature affect the native confirmation of an enzyme?
Changes in pH and temperature can disrupt the bonds that hold the enzyme in its native conformation. This can lead to denaturation of the enzyme, resulting in loss of its catalytic activity. Each enzyme has an optimal pH and temperature at which it functions best, and deviations from these conditions can affect enzyme structure and function.
During protein synthesis l-amino acid binds to t-rna through which?
We might need more information to answer this question. An amino acid will bind to the carboxyl group on the 3'-OH of the tRNA with an ester bond. The tRNA then becomes "charged" and can now begin translation at the ribosome.
Changing one amino acid with a protein could change what about the protein?
It will depend on how different the amino acid is to the one it replaced. If the structure and/or charge is quite different, a change of one amino acid can change the entire 3D structure of the protein. This will affect the proteins function.
Can changing just one nucleotide in a gene change the shape of a protein?
If shape of a protein is changed its function is altered. This might change or stop a particular biochemical pathway in which that enzyme was critical. Specific 3D shape of each protein is very essential for its function. Change in shape of proteins is caused by a mutation in the DNA.
How might altering the pH affect the rate of the reaction?
Altering the pH might cause the enzymes involved in a reaction to be denatured. When enzymes are denatured, they do not function properly and the rate of the reaction either slows down or completely stops.
