multiple choice, choose the correct answer You stumble upon a potential inhibitor (I) for HIV protease, so you now have to perform a few experiments to characterize its behaviour. You find that if you add an excess of substrate to the reaction in the presence of inhibitor, enzyme activity increases but to only 0.5 Vmax to that observed in the absence of inhibitor. The affinity of the substrate for the enzyme is unaffected by the inhibitor. If you treated the enzyme with inhibitor, then dialyse the protein into a buffer solution without inhibitor, the activity is restored. What type of inhibitor is I? 1. Uncompetitive 2. Competitive 3. Non-competitive 4. Irreversible
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.
multiple choice, choose the correct answer
You stumble upon a potential inhibitor (I) for HIV protease, so you now have to perform a few experiments to characterize its behaviour. You find that if you add an excess of substrate to the reaction in the presence of inhibitor, enzyme activity increases but to only 0.5 Vmax to that observed in the absence of inhibitor. The affinity of the substrate for the enzyme is unaffected by the inhibitor. If you treated the enzyme with inhibitor, then dialyse the protein into a buffer solution without inhibitor, the activity is restored. What type of inhibitor is I?
1. Uncompetitive
2. Competitive
3. Non-competitive
4. Irreversible
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