Question

explain the inhibition of enzymatic activity

Answer 1

1) competitive inhibitor:
competition molecule resemble the similar structure of substrate so competition molecule only bind with active site of enzyme
competition inhibitor is reversible inhibitor we can prevent the inhibition by removing of the competition molecule from active site of enzyme
because competition inhibitor there is no change in active site of enzyme by attracting with competition molecule


2) non-competition inhibitor:
competition molecule does not resemble the structure of substrate even and Induce changes in active site that's why it is irreversible inhibition
eg: cynaide attaches with cytochrome oxidase in place of copper
( even though it dosent have similar structure ac copper )

3) allosteric inhibition:
when completion molecule bind with active site it produce intermediate substance so it is also called as retro inhibition

eg: glucose 6 phosphate allsoteric inhibition of heterokinase

4) isoenzymes:
these are having different molecular structure but similar active site
eg: laclic dehydrogenase-5 similar active site
alcoholic dehydrogenase- 4 similar active site





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Answer 2

Hey mate ^_^

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Answer:
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Competitive inhibition:

Here, the inhibitor closely resembles the substrate, and binds with the active sites of enzymes. Hence, inhibiting the enzyme activity.
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Example:
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Malonate resembles succinate structurally, and hence, blocks the activity of the enzyme succinic dehydrogenase.
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Application:
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The principle of competitive inhibition is used to control the bacterial pathogens.

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