2. A 500ul reaction containing 0.5 pmol of an enzyme following Michaelis –-Menten kineties with saturating substrate concentration is studied. For this enzyme kl = 1 x 10° M-1 s', k-1 = 2 x 10's", and k2 = lx 10ʻ s". a. What is the Vmax for the enzyme considering that it has only one substrate binding site? b. What are the values of Km and Ks? Is this a rapid equilibrium enzyme or does it follow steady state kineties? Explain why. c. What is the substrate concentration needed to achieve half maximal velocity? Explain the basis for your answer. d. If the substrate concentration in part e is doubled, how many fold will the initial velocity increase?
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.
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