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V max for an enzyme catalyzed reaction a generally

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28.Vmaxfor an enzyme-catalyzed reaction:A)generally increases when pH increases.B)increases in the presence of a competitive inhibitor.C)is limited only by the amount of substrate supplied.D)is twice the rate observed when the concentration of substrate is equal to theKmE)is unchanged in the presence of a uncompetitive inhibitor..
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29.Enzyme X exhibits maximum activity at pH = 6.9.X shows a fairly sharp decrease inits activity when the pH goes much lower than 6.4.One likely interpretation of this pHactivity is that:
30.Phenyl-methane-sulfonyl-fluoride (PMSF) inactivates serine proteases by bindingcovalently to the catalytic serine residue at the active site; this enzyme-inhibitor bond isnot cleaved by the enzyme.This is an example of what kind of inhibition?
31.Both water and glucose share an —OH that can serve as a substrate for a reaction withthe terminal phosphate of ATP catalyzed by hexokinase.Glucose, however, is about amillion times more reactive as a substrate than water.The BEST explanation is that:
32.A good transition-state analog:A)binds covalently to the enzyme.B)binds to the enzyme more tightly than the substrate.C)binds very weakly to the enzyme.D)is too unstable to isolate.
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E)must be almost identical to the substrate.33.A transition-state analog:

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