Question

describe the process involved in the catalysis of a substrate by an enzyme and state how competitive inhibition and allosteric inhibition affect this catalysis

Answer 1

substrates bind to the active site of the enzyme, the conformation of the enzyme is such that the substrates can bind to the active site then the enzyme-substrate complex forms, the enzyme reduces the activation energy of the reaction so that the reaction can occur fast, once the substrate is converted to product and product is released and the enzyme becomes free to catalyze the conversion of next molecules

the competitive inhibitor binds to the active site of the enzyme, so the substrate cannot bind so the enzyme is inhibited, but the binding of competitive inhibitor is reversible at high concentrations of the substrate the inhibitor is removed from the active site.

Allosteric inhibitors bind to the site other than active site and change the conformation of the protein so that the enzyme cannot bind to the substrate, allosteric regulation is reversible as the concentration of the regulator decreases the regulator is removed from the enzyme.