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If an enzyme is a protein how might you change the specificity of such an enzyme?
Wiki User
∙ 15y ago
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.
Wiki User
∙ 15y ago
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How might an amino acid change at a site distant from the active site of the enzyme alter the enzyme's substrate specificity?
The alteration of an amino acid on a site other than the active site will: change the shape of the protein.
What might happen if pepsin doesn't work properly?
Pepsin is the proteolytic enzyme of the stomach which converts proteins to peptones and dipeptides.. if this enzyme is not present, protein digestion cannot be completed... hence our body will suffer from protein deficiency..
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..
How might amino acid change affect the enzyme?
The pKA of enzyme affects its ionization which could alter enzyme activity. For pH < pKa, the value of vmax is constant and that for pH > pKa, vmax decreases; ie. enzyme activity starts to decline.
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 does a blood serum enzyme test diagnose myopathy?
A blood serum enzyme test measures how much muscle protein is ciruclating in the blood. Antibodies might indicate an inflammatory myopathy; genetic testing may indicate if defects exist.
How does boiling an enzyme effects its activity?
As the enzyme gets boiled, the extra heat breaks the bonds that make up the enzyme. This changes it's shape. When an enzyme lose4s it's shape, shape of active site, it loses its specificity, not allowing it to bind to the substrate. This decreases the rate of the reaction until it's completely denatured.
What are several different situation in which an enzyme might lose its specific shape?
An enzyme can lose its shape (tertiary structure) through many ways. Some of these include: pH change, increased heat, or change in ionic strength of the solution (increasing or decreasing salt levels).
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.
What is client specificity?
"Client specificity" is simply a fancy way to say "something that is specific to or for this client". For example, in medication administration nurses practice "patient specificity" when the nurse conducts conducts med checks that it is the right patient, right medication, right time, etc. In another arena, documentation building you might have "client specificity" in tables and tasks. See the related links section for one website.
Altering the three-dimensional structure of an enzyme might?
prevent the substrate from binding the enzyme's active site
How a change in the sequence of nucleotides in a strand of DNA might cause a protein to malfunction?
The sequence of nucleotides is altered and therefore, the amino acid that is to be added to the peptide chain will be altered. hence the protein will be different. This protein can be functionless (will be degraded). If it turns out to be toxic, then there may be symptoms.
