The text discusses three forms of enzyme inhibition: uncompetitive inhibition, competitive inhibition, and irreversible inhibition.(a) Describe how an enzyme inhibitor of each type works.(b) What kinds of bonds are formed between an enzymeand each of these three kinds of inhibitors?

Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
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The text discusses three forms of enzyme inhibition: uncompetitive inhibition, competitive inhibition, and irreversible inhibition.
(a) Describe how an enzyme inhibitor of each type works.
(b) What kinds of bonds are formed between an enzyme
and each of these three kinds of inhibitors?

Expert Solution
Step 1Introduction

Enzyme 

  • Coined by Kuhne in 1878. 
  • Popularly known as biological catalysts. 
  • Metabolic and cellular reactions are largely enzymatically catalyzed which otherwise will complete in many years if they are not catalyzed by enzymes.
  • For example, The digestion of a single food meal in the stomach will occur in years if not enzymatically catalyzed.
  • The rate of enzyme-catalyzed reaction or the rate at which product is formed is studied under enzyme kinetics

Inhibition 

  • It is the process in which enzyme activity is adversely affected, either partially or completely in the presence of a molecule known as an inhibitor.
  • The rate of the formation of products is affected by the combination of an inhibitor to the enzyme.
  • The inhibitor may or may not bind to the enzyme's active site.
  • The inhibitor may or may not resemble the substrate structurally.
  • Inhibition is of two types: Reversible and irreversible inhibition. 
Step 2 Answer a Mechanism of three types of inhibitors

Competitive Inhibition

  • It is a type of reversible inhibition 
  • Here, the inhibitor resembles the substrate.
  • The inhibitor competes with the substrate for binding at the active site of an enzyme. 
  • The strength of inhibition depends upon the concentrations of substrate and inhibitors.
  • By increasing the concentration of substrate, inhibition can be reversed. In this case, Vmax remains the same but Km will increase as compared to a normal enzyme-substrate association.

Uncompetitive Inhibition 

  • It is also a reversible inhibition.
  • Here, the inhibitor binds to an allosteric site of an enzyme.
  • In this case, binding occurs with the Enzyme-substrate complex only not the free enzyme. 
  • In this case, Vmax and Km decrease in the presence of inhibitors.

Irreversible Inhibition 

  • It is a type of inhibition that can't be reversed or there is a slow dissociation of the inhibitor from the enzyme.
  • There is a tight association of inhibitors at the enzyme's active site.
  • An enzyme is almost inactive in the presence of inhibitors. 
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