#Question id: 558
#Biochemistry
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
#Biochemistry
In competitive inhibition, an inhibitor:
#Question id: 560
#Biochemistry
Vmax for an enzyme-catalyzed reaction:
#Question id: 561
#Biochemistry
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
#Biochemistry
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: 564
#Biochemistry
A good transition-state analog:
