4. A team of R&D scientists were trying to make a “better" enzyme. A molecular biologist mutated amino acid residues of an existing enzyme. An enzymologist on the team evaluated the engineered enzymes by measuring the dissociation constants between a substrate-analog and the different engineered enzymes. The engineer also measured Vmax of each enzyme, using a natural substrate of the enzyme. Which engineered enzyme is a failure and why? Provide a thermodynamic explanation. Include a reaction-progress energy diagram in your answer. Engineered Enzyme ID Ka (uM) Vmax (uM, min-!) А 10 150 B 0.4 2
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.
Enzyme catalysis is a process, in which an enzyme is reacted with the substrate in order to produce a product. Since the team of R & D scientist has discovered the two enzyme parameters by measuring their dissociation (Kd) constant and maximum velocity (Vmax).
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