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Introduction to Enzymology Exam Study Guide Questions and Complete Solutions
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Introduction to Enzymology ExamStudy Guide Questions and Complete
Solutions
Hydrolases - ✔Catalyze hydrolysis or splitting of a bond by the addition of water
(hydrolytic reactions)
Hydrolases - ✔Esterases (ACP, ALP, LPS)
Peptidases (Trypsin, Pepsin, LAP)
Glycosidases (AMS, Galactosidase)
Lyases - ✔Catalyze removal of groups from substrates without hydrolysis.
Product contains double bonds
Lyases - ✔Glutamate decarboxylase
Pyruvate decarboxylase
Tryptophan decarboxylase
Aldolase
Ligases - ✔Catalyze the joining of two substrate molecules, coupled with breaking
of pyrophosphate bond in ATP or similar compoun
Ligases - ✔Synthase
First-Order Kinetics - ✔Reaction rate is directly proportional to the substrate concentration
, Substrate increases = reaction rate increases
Zero-Order Kinetics - ✔Only a fixed number of substrate (in excess) is converted to
product per second
Further increase in the concentration of the substrate will produce no more enhancement of
the reaction rate
Reaction rate switched its maximum
Enzyme is already saturated with the substrate
Michaelis-Menten Constant - ✔Describes how reaction velocity varies with
substrate concentration
Expression of the relationship between the velocity of an enzymatic reaction and substrate
concentration
Competitive Inhibitor - ✔Physically bind to the active site of an enzyme
Both the substrate and the inhibitor compete for the same active site of the enzyme
Inhibitor may bind the active site, blocking the access of the substrate
Non-Competitive Inhibitor - ✔Binds an enzyme at a place other than the active site
Do not compete with the substrate but look for areas other than the active site
Binds to the allosteric site causing a change in the shape of the enzyme that interferes with the
substrate binding
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