For the following calculations, please provide your answers in whole numbers (no decimals). A research group has discovered a new enzyme they denote XC-95, which catalyzes the conversion of its substrate, propanol, to propionic acid, the product. The researchers begin to characterize the enzyme. In the first experiment, with [E]=4x10-5 mM, they find that Vmax=4 µM s-1. Based on this experiment, the Kcat for XC-95 in units of s-1 is A/ . In their second experiment, with [propanol]=0.01 mM, the researchers find that v₁-2000 nM s-1. The measured KM of XC-95 for propanol in units of µM is A/ Further researc showed that the purified XC-95 used in the first two experiments was actually contaminated with reversible inhibitor of the enzyme, butanol. When butanol is removed from the purified enzyme a the first two experiments are repeated, Vmax is found to be 4 μM s-1, and the measured KM becomes 10 μM. Based on this new data, the mechanism of inhibition by butanol is BEST described by which of the following: Competitive Uncompetitive Mixed Non-competitive A/ and the value of a is A .
For the following calculations, please provide your answers in whole numbers (no decimals). A research group has discovered a new enzyme they denote XC-95, which catalyzes the conversion of its substrate, propanol, to propionic acid, the product. The researchers begin to characterize the enzyme. In the first experiment, with [E]=4x10-5 mM, they find that Vmax=4 µM s-1. Based on this experiment, the Kcat for XC-95 in units of s-1 is A/ . In their second experiment, with [propanol]=0.01 mM, the researchers find that v₁-2000 nM s-1. The measured KM of XC-95 for propanol in units of µM is A/ Further researc showed that the purified XC-95 used in the first two experiments was actually contaminated with reversible inhibitor of the enzyme, butanol. When butanol is removed from the purified enzyme a the first two experiments are repeated, Vmax is found to be 4 μM s-1, and the measured KM becomes 10 μM. Based on this new data, the mechanism of inhibition by butanol is BEST described by which of the following: Competitive Uncompetitive Mixed Non-competitive A/ and the value of a is A .
Biomedical Instrumentation Systems
1st Edition
ISBN:9781133478294
Author:Chatterjee
Publisher:Chatterjee
Chapter5: Biomedical Electronics: Digital
Section: Chapter Questions
Problem 4P
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i subimtted this question on other websites and they were wrong, please dont copy paste
![For the following calculations, please provide your answers in whole numbers (no
decimals).
A research group has discovered a new enzyme they denote XC-95, which catalyzes the
conversion of its substrate, propanol, to propionic acid, the product. The researchers begin to
characterize the enzyme.
In the first experiment, with [E]=4x10-5 mM, they find that Vmax=4 µM s-¹1. Based on this
experiment, the Kcat for XC-95 in units of s-1 is
A/ . In their second experiment, with
[propanol]=0.01 mM, the researchers find that v₁-2000 nM s-¹. The measured KM of XC-95 for
propanol in units of µM is
. Further research
showed that the purified XC-95 used in the first two experiments was actually contaminated with a
reversible inhibitor of the enzyme, butanol. When butanol is removed from the purified enzyme and
the first two experiments are repeated, Vmax is found to be 4 µM s-1, and the measured KM
becomes 10 μM. Based on this new data, the mechanism of inhibition by butanol is BEST
described by which of the following:
Competitive
Uncompetitive
Mixed
Non-competitive
A/
and the value of a is](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F68c72f36-2bf0-4086-8182-5543f65133c5%2Fa75aca39-70be-47b6-a81a-1c64ac96be2b%2Ffb6878p_processed.png&w=3840&q=75)
Transcribed Image Text:For the following calculations, please provide your answers in whole numbers (no
decimals).
A research group has discovered a new enzyme they denote XC-95, which catalyzes the
conversion of its substrate, propanol, to propionic acid, the product. The researchers begin to
characterize the enzyme.
In the first experiment, with [E]=4x10-5 mM, they find that Vmax=4 µM s-¹1. Based on this
experiment, the Kcat for XC-95 in units of s-1 is
A/ . In their second experiment, with
[propanol]=0.01 mM, the researchers find that v₁-2000 nM s-¹. The measured KM of XC-95 for
propanol in units of µM is
. Further research
showed that the purified XC-95 used in the first two experiments was actually contaminated with a
reversible inhibitor of the enzyme, butanol. When butanol is removed from the purified enzyme and
the first two experiments are repeated, Vmax is found to be 4 µM s-1, and the measured KM
becomes 10 μM. Based on this new data, the mechanism of inhibition by butanol is BEST
described by which of the following:
Competitive
Uncompetitive
Mixed
Non-competitive
A/
and the value of a is
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