Question

How many types of Inhibition of enzyme
#100 pointsss​

Answer 1

Answer:

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$\green{\boxed{\tt Competitive\: Inhibition}}$

• Reversible.Occurs due to substrate or increase Enzyme analogue

$\green{\boxed{\tt Non-Compititive\: Inhibition}}$

• Inhibitor forms a complex with Enzyme at a site other than the active site.

$\green{\boxed{\tt Allosteric\: Inhibition}}$

• Inhibitor bind to Enzyme at specific site other than active site and change the structure of active site to affect substrate binding.

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Answer 2

Answer:

Explanation:

Competitive Inhibition

Probably the easiest type of enzyme inhibition to understand is competitive inhibition and it is the one most commonly exploited pharmaceutically. Molecules that are competitive inhibitors of enzymes resemble one of the normal substrates of an enzyme. An example is methotrexate, which resembles the folate substrate of the enzyme dihydrofolate reductase (DHFR).

Non-Competitive Inhibition

A second type of inhibition employs inhibitors that do not resemble the substrate and bind not to the active site, but rather to a separate site on the enzyme (rectangular site below). The effect of binding a non-competitive inhibitor is significantly different from binding a competitive inhibitor because there is no competition. In the case of competitive inhibition, the effect of the inhibitor could be reduced and eventually overwhelmed with increasing amounts of substrate.

Uncompetitive Inhibition

A third type of enzymatic inhibition is that of uncompetitive inhibition, which has the odd property of a reduced Vmax as well as a reduced KM. The explanation for these seemingly odd results is rooted in the fact that the uncompetitive inhibitor binds only to the enzyme-substrate (ES) complex. The inhibitor-bound complex forms mostly under concentrations of high substrate and the ES-I complex cannot release product while the inhibitor is bound, thus explaining the reduced Vmax.