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16.4 Enzymes -- Part 1
A patient has elevated blood levels.
There are five isoenzymes for lactase de Hydro Genase.
The activity is affected by a number of factors.
Enzymes are sensitive to temperature.
There is not a sufficient amount of energy for the catalyzed reaction to take place at low temperatures.
The activity of the enzyme increases at higher temperatures.
The optimum temperature for the reaction maximum rate activity is 37 degC.
There is enough energy to disrupt the interactions between the R groups at high temperatures.
The shape of most proteins is destroyed when too many interactions are disrupted.
The high temperatures of the autoclaves denature the enzymes in harmfulbacteria, which is why equipment in hospitals and laboratories is sterile.
The range of temperatures in which thermophiles live is from 50 to 120 degrees.
In order to survive, thermophiles use a hot spring.
The tertiary structures of the enzymes must not be destroyed by high temperatures.
Some research shows that their enzymes are very similar to ordinary ones except they have more hydrogen bonds and salt bridges and resist unfolding and the loss of activity.
As a result, theidase no longer binding the substance.
Most cells have optimal pH values around 7.4.
pepsin has an optimum pH of 1.5 to 2.0.
Most of the time, the Enzymes show little or no activity in the GI tract.
When food enters the stomach, the acid in it is active.
When the pH is lowered to about 2, the optimum pH values are higher or lower.
The rate of the reaction catalyzed by urease would be affected by the temperature being lowered.
There is a decrease in the rate of reaction when the temperature is 10 degC.
Denaturation of the tertiary structure will decrease the activity of urease.
What happens to the rate of the material?
A competitive inhibitor competes with the other to bind with the active site on the enzyme.
There is a loss of activity if the concentration is large.
The competitive inhibitor is displaced by adding more substrate.
The activity of theidases is regained as more of them bind to theES.
A noncompetitive inhibitor can bind to a site that isn't the active site.
The shape of the enzyme is distorted when the noncompetitive inhibitor is bonding to it.
It is possible for the substrate to not fit in the active site.
Adding more substrate won't reverse this type of inhibition because a noncompetitive inhibitor isn't competing for the active site.
When chemical reagents are removed, catalytic activity is restored.
In irreversible inhibition, a molecule causes an enzyme to stop working.
There are toxic substances that destroy the enzymes.
A covalent bond is formed between the active site and the side group of the irreversible inhibitor, which prevents it from binding to the active site.
Eliminating insects and nerve gases is an effective way to kill them.
Try Practice Problems 16.47 impulses are blocked and paralysis occurs.
Antibiotics produced bybacteria, mold, or yeast are used to stop growth.
penicillin does not affect the formation of cell walls in humans, but it does affect the formation of cell walls inbacteria.
An incomplete cell wall will cause the infection to be stopped.
Somebacteria are resistant to penicillin because Amoxicillin is a derivatives of penicillinase, an enzyme that breaks down penicillin.
The antibiotics penicillin and derivatives have been used over the years.
The structure of the inhibitor is similar to that of the substrate.
The shape of the inhibitor can be changed in such a way that it cannot bind to the substrate.
When the structure of the inhibitor is similar to that of the substrate, it competes with the other for the active site.
This type of inhibition can be reversed by increasing the concentration of the substrate.
The shape of the enzyme and the active site can be changed by an inhibitor.
This type of inhibition is not competitive because it does not compete with the active site and has a different shape.
The inhibition by sarin is irreversible because it forms a bond with an R group in the active site.
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