#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:
#Question id: 565
#XL - Q Biochemistry
A transition-state analog:
#Question id: 566
#XL - Q Biochemistry
The role of the metal ion (Mg2+) in catalysis by enolase is to
#Question id: 567
#XL - Q Biochemistry
Penicillin and related drugs inhibit the enzyme; this enzyme is produced by