Describe the chemical compositions and configuration of enzymes and discuss the factors that modify enzymes structure and function?

Answer 1

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.

Answer 2

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