Molecule X is expected to be a non-competitive inhibitor of an enzyme. If the inhibitor was tested at a saturating level of substrate the following would be observed: a. The inhibitor would decrease the Vmax b. The inhibitor would increase the Km c.
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.
Molecule X is expected to be a non-competitive inhibitor of an enzyme. If the inhibitor was tested at a saturating level of substrate the following would be observed:
The inhibitor would decrease the Vmax
The inhibitor would increase the Km
The inhibitor would decrease the Km
The inhibitor would increase the Vmax
The inhibitor would not change the Vmax
Vmax of a reaction is the maximum velocity of the enzyme that carries out the reaction that is when the enzyme is completely saturated with the substrate.
Km is that subsequently concentration at which half of the maximum velocity is achieved.
Inhibitors are the substances that may bind to some distinct site in the enzyme and after binding to the enzyme they inhibit the activity of the enzyme.
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