91影视

Write the rate equations for a first-order and a second-order reaction.

Consider the nonenzymatic elementary reaction A 鈫� B. When the
concentration of A is 20 mM, the reaction velocity is measured as 5 碌M
B produced per minute. (a) Calculate the rate constant for this reaction.
(6) What is the molecularity of the reaction?

Identify the enzymes in Table 12-1 whose catalytic efficiencies are near the diffusion-controlled limit.

What distinguishes an inhibitor from an inactivator?

Calculate ${\mathbf{K}}_{\mathbf{M}}$and ${\mathbf{V}}_{\mathbf{max}}$ from the following data:

Why might an enzyme鈥檚 substrate, transition state, and product all serve as starting points for the design of a competitive inhibitor?

Describe the effects of competitive, uncompetitive, and mixed inhibitors on K_M and V_max.

Explain why each of the following data sets from a Lineweaver Burk plot are not individually ideal for determining KM for an enzyme catalysed reaction that follows Michaelis-Menten kinetics.

The K_M for the reaction chymotrypsin with N-acetylvaline ethyl ester is $\mathbf{8}\mathbf{.}\mathbf{8}\mathbf{脳}{\mathbf{10}}^{\mathbf{鈥�}\mathbf{2}}\mathbf{M}$, and the ${\mathbf{K}}_{\mathbf{M}}$ for the reaction of chymotrypsin with N-acetyltyrosine ethyl ester is $\mathbf{6}\mathbf{.}\mathbf{6}\mathbf{脳}{\mathbf{10}}^{\mathbf{鈥�}\mathbf{4}}\mathbf{M}$. (a) Which substrate has the higher apparent affinity for the enzyme? (b) Which substrate is likely to give a higher value for ${\mathbf{V}}_{\mathbf{max}}$?

How can inhibitor binding to an enzyme be quantified?