(a)
Interpretation:
V0 versus pH curve when the substrate concentration is much greater than the enzyme KM should be drawn.
Concept introduction:
KM is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower KM needs a higher concentration of substrate to achieve Vmax.
(b)
Interpretation:
V0 versus pH curve when the substrate concentration is much less than the enzyme KM should be drawn.
Concept introduction:
KM is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower KM needs a higher concentration of substrate to achieve Vmax.
(c)
Interpretation:
The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.
Concept introduction:
KM is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower KM needs a higher concentration of substrate to achieve Vmax.
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Chapter 8 Solutions
BIOCHEMISTRY (LOOSELEAF)-W/ACCESS
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