In an enzymatic reaction of maltase, the disaccharide maltose is hydrolyzed to glucose. In an experiment, an inhibitor X was added to the reaction. The addition of the inhibitor brought about a change in the activity of the enzyme. When the substrate concentration was 0.125 mM, the initial velocity was 0.10 mM per minute. However, Vo / Initial velocity changed to 0.25 mM per minute when the substrate concentration was 0.50 mM. Hence, calculate the Km of the reaction.

Biochemistry
6th Edition
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter23: Fatty Acid Catabolism
Section: Chapter Questions
Problem 21P: Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved...
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In an enzymatic reaction of
maltase, the disaccharide
maltose is hydrolyzed to
glucose. In an experiment, an
inhibitor X was added to the
reaction. The addition of the
inhibitor brought about a
change in the activity of the
enzyme. When the substrate
concentration was 0.125 mM,
the initial velocity was 0.10
mM per minute. However,
Vo / Initial velocity
changed to 0.25 mM per
minute when the substrate
concentration was 0.50 mM.
Hence, calculate the
of the reaction.
Transcribed Image Text:In an enzymatic reaction of maltase, the disaccharide maltose is hydrolyzed to glucose. In an experiment, an inhibitor X was added to the reaction. The addition of the inhibitor brought about a change in the activity of the enzyme. When the substrate concentration was 0.125 mM, the initial velocity was 0.10 mM per minute. However, Vo / Initial velocity changed to 0.25 mM per minute when the substrate concentration was 0.50 mM. Hence, calculate the of the reaction.
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