Below is a Michaelis Menten plot for an allosteric enzyme. Which line represents the enzyme in it's T state? Vo B 0 A [S] mM Vmax
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In allosteric enzymes, the active site can exist in two different conformations: the tense (T) state and the relaxed (R) state. The T state has a lower affinity for the substrate and a lower catalytic activity, while the R state has a higher affinity for the Show more…
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6. The following is a Michaelis-Menten curve. Label on this graph the following: - As [S] increases, the initial rate or velocity (V₀) increases (Label as A) - As [S] increases, V increases less and less (Label as B) - V no longer increases and velocity reaches its maximum (Label as C) Figure 1. The Michaelis-Menten curve describes the relationship between an enzyme (at constant concentration) and the concentration of substrate [S]. V₀ is the initial rate. Where on the graph (A, B, or C) is the enzyme saturated with substrate?
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The rate of a simple enzyme reaction is given by the standard Michaelis-Menten equation:\[\text { rate }=V_{\max }[\mathrm{S}]/\left([\mathrm{S}]+K_{\mathrm{M}}\right)\].If the $V_{\max }$ of an enzyme is 100 \mumole/sec and the $K_{M}$ is $1 \mathrm{mM},$ at what substrate concentration is the rate 50 \mumole/sec? Plot a graph of rate versus substrate (S) concentration for $[\mathrm{S}]=0$ to $10 \mathrm{mM}$. Convert this to a plot of 1/rate versus 1/[S]. Why is the latter plot a straight line?
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