elow are plots of enzyme activity vs and substrate concentrations respectively.
ID: 526720 • Letter: E
Question
elow are plots of enzyme activity vs and substrate concentrations respectively. 17. The fact that rate increases and then levels off with increasing substrate reaction concentration can be explained by which of the following A. There is afixed number of active binding sites on the enzyme and eventually those B. sites get filled up. competitive binding limits access to is a particular concentration, sites on the enzyme C. Reverse inhibition plays a role at higher substrate concentrations D. At higher substrate concentration, irreversible binding occurs E. None of the above. Maximum activity 18. The plot at right shows that the rate of enzyme catalysis peaks out at a very specific pH. This is quite different from effects due to enzyme of substrate concentration. In the space below provide a rational that includes discussion of weak (non covalent) interactions an amino acid side chainsExplanation / Answer
17. Reaction rate increases and then levels of with increasing substrate concentration because
A. There is a fixed number of active binding sites on the enzyme and eventually those sites get filled up.
18. Every enzyme has an optimum pH of activity when the substrate binds to the active site of the enzyme using different ionic bonds. The enzyme is nothing but a protein comprising of different amino acids, with both acidic and basic side chains. On changing the pH from optimum due protonation or deprotonation of one or more of such basic or acidic side chain of amino acids, the interaction or binding with the substrate can get affected. That's why activity is maximum at a certain pH.
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