What mode (property) of enzyme catalysis increases effective molarity within the active site of enzymes?
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Mode of inhibition. The kinetics of an enzyme are measured as a function of substrate concentration in the presence and in the absence of $2 \mathrm{mM}$ inhibitor $(\mathrm{I})$. (a) What are the values of $V_{\max }$ and $K_{\mathrm{M}}$ in the absence of inhibitor? In its presence? (b) What type of inhibition is it? (c) What is the binding constant of this inhibitor? (d) If $[\mathrm{S}]=10 \mu \mathrm{M}$ and $[\mathrm{I}]=2 \mathrm{mM},$ what fraction of the en zyme molecules have a bound substrate? A bound inhibitor? (e) If $[\mathrm{S}]=30 \mu \mathrm{M},$ what fraction of the enzyme molecules have a bound substrate in the presence and in the absence of $2 \mathrm{mM}$ inhibitor? Compare this ratio with the ratio of the reaction velocities under the same conditions.
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10.) Under current enzyme models, describe the active site of an enzyme (i.e. what makes enzymes so effective)?
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