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Describe the relationship between substrate concentration and the initial reaction rate of an enzyme-catalyzed reaction Is this a linear relationship What happens to the initial reaction rate as sub?
Wiki User
∙ 13y ago
As the substrate concentration increases so does the reaction rate because there is more substrate for the enzyme react with.
Wiki User
∙ 13y ago
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Substrate-level phosphorylation can best be describe as?
Substrate-level phosphorylation can best be describe as the direct transfer of phosphate from one substrate to another. Oxidative phosphorylation is different from substrate level phosphorylation is that it generates ATP by using a proton motive force.
The initial rate of an enzyme catalysed reaction depend on?
Based on Michaelis-Menten enzyme kinetics, the initial rate of reaction, vi, is dependent on maximum rate Vmax, substrate concentration [S], and the enzyme's Michaelis constant Km, which represents the the tendency of the substrate/enzyme complex to dissociate. The dependence on enzyme concentration is factored into the maximum rate. The equation to describe this is: vi = Vmax([S]/(Km+[S])) Follow the link below for details.
If Pectinase only breaks down pectin and It has no effect in cellulose What term is used to describe this characteristic of enzymes?
Enzymes are substrate specific; meaning that their active site only allows for a certain substrate to bind - in this case, pectin, and the enzyme has no effect on any other biological molecules
Describe the concentration gradient shown in the transparency?
The description of the concentration of a gradient shown in the transparency is a gradual change of solutes that are in a solution. This is a function of distance through the solution in biology.
Describe the chemical compositions and configuration of enzymes and discuss the factors that modify enzymes structure and function?
Enzymes are composed of amino acids, and have different bonds such as a hydrogen bond which maintains the enzyme's shape. Factors such as temperature and pH have an effect upon the enzymes structure. Enzymes have slower rates of reaction when the temperature is below the enzymes optimum temperature. This is due to the fact that hydrogen bonds are stronger at lower temperatures meaning that the enzyme is less flexible and so, using the induced fit theory, this means that the substrate is less able to fit into the enzymes active site meaning less substrate is broken down therefore the rate of reaction is much less than it would be at the enzymes optimum temperature. When the temperature also exceeds the enzymes optimum temperature the rate of reaction is again slower that it would be at the optimum temperature, this is due to the high temperature causing the hydrogen bonds to be broken, meaning the enzyme can be denatured, and there is a point where the enzymes are unable to "renature" (when temp is returned to optimum) because too many hydrogen bonds would have been broken. pH is a factor which also affects the enzymes structure, by changing the pH from the enzymes optimum pH you are then causing there to be a change in the enzymes structure and molecular shape. pH can in turn strengthen or weaken the intermolecular forces like the hydrogen bonds. Competitive inhibitors can also alter the enzymes function. Competitive inhibitors have a molecular shape which is similar to the shape of the substrate; This means that they can occupy the enzymes active site meaning that they compete with the substrate for an available active site. The difference between the concentration of the competitive inhibitor and the substrate determines the effect upon the enzyme activity, if the competitive inhibitors concentration is highest the effect of the substrate is lessened. The inhibitor is not permenantly bound to the enzymes active site, so when it leaves another molecule may take its place, either another inhibitor or substrate. Sooner or later all of the substrate will occupy active sites of enzymes, but if the inhibitor concentration is higher this may take some time. Non-competitive inhibitors can also effect the enzyme activity by attaching themselves to the enzyme, but not at the active site. This attachment means the enzyme's active site may under-go a shape change meaning that the substrate may not fit into it, causing the effect of the enzyme to be lowered as less substrate can be broken down. Non-competitive inhibitors may be permanent. Hope this helps you, even if it is very slightly.
Can anyone help with this question Describe the relationship between substrate concentration and the initial reaction rate of an enzyme-catalyzed reaction Is this a linear relationship What happens t?
The more substrate the faster the rate of reaction up to a point where it levels out. Basically the enzymes and substrates bounce around until they meet the substrate that the enzyme can catalyse so obviously with more substrate there's more chance of he enzyme bumping into the right substrate
Substrate-level phosphorylation can best be describe as?
Substrate-level phosphorylation can best be describe as the direct transfer of phosphate from one substrate to another. Oxidative phosphorylation is different from substrate level phosphorylation is that it generates ATP by using a proton motive force.
The initial rate of an enzyme catalysed reaction depend on?
Based on Michaelis-Menten enzyme kinetics, the initial rate of reaction, vi, is dependent on maximum rate Vmax, substrate concentration [S], and the enzyme's Michaelis constant Km, which represents the the tendency of the substrate/enzyme complex to dissociate. The dependence on enzyme concentration is factored into the maximum rate. The equation to describe this is: vi = Vmax([S]/(Km+[S])) Follow the link below for details.
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Describe the change in the rate of reaction when the enzyme concentration is increased?
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