#Question id: 559
#XL - Q Biochemistry
In competitive inhibition, an inhibitor:
#Question id: 560
#XL - Q Biochemistry
Vmax for an enzyme-catalyzed reaction:
#Question id: 561
#XL - Q 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
#XL - Q 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: 563
#XL - Q Biochemistry
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:
#Question id: 564
#XL - Q Biochemistry
A good transition-state analog: