One characteristic of enzyme competitive inhibition is that it results in an increase in the Km of the enzyme without a change in the Vmax. Why does competitive inhibition cause an increase in Km? OA. Because by binding to the active site the inhibitor increases the affinity of the enzyme for substrate. B. Because at low substrate concentration the inhibitor interferes with substrate binding to the enzyme. OC. Because the inhibitor binds to substrate molecules preventing them from accessing the enzyme active site. D. Because the inhibitor changes the shape of the active site preventing substate binding.
Enzyme kinetics
In biochemistry, enzymes are proteins that act as biological catalysts. Catalysis is the addition of a catalyst to a chemical reaction to speed up the pace of the reaction. Catalysis can be categorized as either homogeneous or heterogeneous, depending on whether the catalysts are distributed in the same phase as that of the reactants. Enzymes are an essential part of the cell because, without them, many organic processes would slow down and thus will affect the processes that are important for cell survival and sustenance.
Regulation of Enzymes
A substance that acts as a catalyst to regulate the reaction rate in the living organism's metabolic pathways without itself getting altered is an enzyme. Most of the biological reactions and metabolic pathways in the living systems are carried out by enzymes. They are specific for their works and work in particular conditions. It maintains the best possible rate of reaction in the most stable state. The enzymes have distinct properties as they can proceed with the reaction in any direction, their particular binding sites, pH specificity, temperature specificity required in very few amounts.
Trending now
This is a popular solution!
Step by step
Solved in 3 steps
