#Question id: 558
#Unit 1. Molecules and their Interaction Relevant to Biology
In a plot of l/V against 1/[S] for an enzyme-catalyzed reaction, the presence of a competitive inhibitor will alter the:
#Question id: 559
#Unit 1. Molecules and their Interaction Relevant to Biology
In competitive inhibition, an inhibitor:
#Question id: 560
#Unit 1. Molecules and their Interaction Relevant to Biology
Vmax for an enzyme-catalyzed reaction:
#Question id: 561
#Unit 1. Molecules and their Interaction Relevant to Biology
Enzyme X exhibits maximum activity at pH = 6.9. X shows a fairly sharp decrease in its activity when the pH goes much lower than 6.4. One likely interpretation of this pH activity is that:
#Question id: 562
#Unit 1. Molecules and their Interaction Relevant to Biology
Phenyl-methane-sulfonyl-fluoride (PMSF) inactivates serine proteases by binding covalently to the catalytic serine residue at the active site; this enzyme-inhibitor bond is not cleaved by the enzyme. This is an example of what kind of inhibition?
#Question id: 563
#Unit 1. Molecules and their Interaction Relevant to Biology
Both water and glucose share an —OH that can serve as a substrate for a reaction with the terminal phosphate of ATP catalyzed by hexokinase. Glucose, however, is about a million times more reactive as a substrate than water. The best explanation is that: