Imagine an enzymecatalyzed reaction proceeding under typical

Imagine an enzyme-catalyzed reaction proceeding under typical conditions (for that enzyme). Identify at least two factors that would affect the rate of this reaction

Solution

Answer:

The two factors that would affect the rate of this reaction are pH and temperature for a typical enzyme-catalyzed reaction

As the temperature is increasing, the rate of covalent modification of active sites responsible for \"reaction mechanism involving various substrates\" are going to change result in inadequate active enzymes

Enzymes lower activation energy of reactant by forming an enzyme –substrate complex” with optimum temperature result in \"higher rate of reaction\". This mechanism is involves a enzyme-substrate transition state so that the active site of enzyme reacts with the substrate finally causes conformation changes & reduction in free energy of enthalphy of reactants at specific pH. So that the enzymes often reduce activation energy of a reactant to further proceed a spontaneous reaction from left to right

The existence of enzyme-substrate complexes was well accepted long before it became possible to directly observe them experimentally. Enzyme specificity with active sites for specific substrate binding feature of enzyme kinetics provided strong evidence for this complex before one could explicitly detect them as described below (lock & key hypothesis)

Explaination:

Michaelis and Menton assumption:                                                    

E + S ----> ES ----> P (The reverse reaction of enzyme with product does not occur)

Formation of product depends only on the rate of enzyme -substrate complex formation

The reverse reaction of enzyme with product does not occur

The reaction occurs under steady state conditions for the enzyme substrate complex

The catalytic rate of enzymes under steady-state conditions is constant but reaction proceeds in which ES (enzyme –substrate) level is unchanged & however, the product concentration and substrate concentration is going to change. Therefore, at steady state conditions, reaction proceeds for the ES complex because “the rate of enzyme-substrate production is equal to the rate of enzyme –substrate breakdown”

The formation of enzyme-substrate complex at a fixed concentration of enzyme, the reaction velocity (V₀) is exhibiting a linear relationship with concentration of substrate [S]. Therefore, enzyme binding specificity with substrate to form specific ES complex is considered as a meticulous \"reaction intermediate\" during catalysis