Question

describe the effects of

mixed inhibition

Substrate inhibition

Product inhibition

Mechanism based/suicide inhibitors

Covalent intermediates

Ping Pong Mechanisms

Burst Kinetics

Allosteric Inhibitors

Answer 1

Mixed Inhibition: When the inhibitor attacks any other site of the enzyme than the active site i.e the allosteric site is called as Mixed inhibition. Due to mixed inhibition the affinity of the enzyme for the substrate decreases thus lowering the rate of the reaction.

Substrate Inhibition: The simplest explanation of substrate inhibitors is the binding of substrate to the enzyme at two different sites. One is the active site called as catalytic site and the other is the allosteric site called as the non-catalytic site. Due to high concentration of substrate, it may bind to both the sites. However, the velocity of the reaction increases to a certain level and then decreases due to substrate inhibition.

Product inhibition: Sometimes the product that is formed has the same amino acids that binds to the enzyme at the active site as the substrate binds. Due to this the product might bind to the enzyme at the active site and thus will decrease the velocity of the reaction.

Suicide Inhibition: Mechanism based inhibition or suicide inhibition is an irreversible form of inhibition that takes place when an enzyme binds to a substrate and forms an irreversible form of complex with it through a covalent bond during the normal catalysis reaction. Here the concentration of enzyme is reduced as it catalyses its own suicide and hence the rate of reaction is drastically decreased.