A kinetic study of an intestinal peptidase using glycylglycine as the substrate produced the experimental data shown in the table. glycylglycine + H₂O → 2 glycine [S] (mm) 1.5 2.0 3.0 4.0 8.0 16.0 Product formed (µmol min¹¹) 0.21 0.24 0.28 0.33 0.40 0.45 Calculate the standard error of regression (SER) for the Lineweaver-Burk slope and the Eadie-Hofstee slope to compare the precision of each.
Catalysis and Enzymatic Reactions
Catalysis is the kind of chemical reaction in which the rate (speed) of a reaction is enhanced by the catalyst which is not consumed during the process of reaction and afterward it is removed when the catalyst is not used to make up the impurity in the product. The enzymatic reaction is the reaction that is catalyzed via enzymes.
Lock And Key Model
The lock-and-key model is used to describe the catalytic enzyme activity, based on the interaction between enzyme and substrate. This model considers the lock as an enzyme and the key as a substrate to explain this model. The concept of how a unique distinct key only can have the access to open a particular lock resembles how the specific substrate can only fit into the particular active site of the enzyme. This is significant in understanding the intermolecular interaction between proteins and plays a vital role in drug interaction.
Please just answer this question, I answered the others already
Calculate the standard error of regression (SER) for the Lineweaver–Burk slope and the Eadie–Hofstee slope to compare the precision of each.
Eadie–Hofstee SER: it is not 0.128, 0.028, 0.136, or 0.1362 or 0.013.
![There are several ways to transform the Michaelis-Menten
equation so as to plot data and derive kinetic parameters, each
with different advantages depending on the data set being
analyzed. One transformation of the Michaelis-Menten
equation is the Lineweaver-Burk, or double-reciprocal,
equation. Multiplying both sides of the Lineweaver-Burk
equation by Vmax and rearranging gives the
Eadie Hofstee equation.
Vo = -(Km)
[S]
+ Vmax
Vo
Consider the plot of Vo versus for an enzyme-catalyzed
[S]
reaction. The control reactions (blue curve) did not contain
any inhibitor.
curve B
curve C
curve A
V₁
V mas
A
B
Slope =-K
V₁
[S]
Which of the other curves (A, B, or C) depicts this enzyme's activity in the presence of a competitive inhibitor?
C
J
mak
K
m](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F51044012-1e7d-4f53-9311-c2b96c730020%2Ff671a3ae-ab5b-4e46-8e94-9c12baa1eab4%2Fvuyihk_processed.jpeg&w=3840&q=75)
![A kinetic study of an intestinal peptidase using glycylglycine as the substrate produced the experimental data shown in the table.
glycylglycine + H₂O → 2 glycine
[S] (MM)
1.5
2.0
3.0
4.0
8.0
16.0
Calculate the standard error of regression (SER) for the Lineweaver-Burk slope and the Eadie-Hofstee slope to compare the
precision of each.
Product formed (µmol min-¹)
0.21
0.24
0.28
0.33
0.40
0.45
Lineweaver-Burk SER: 0.182
Eadie Hofstee SER:
0.128
Incorrect
μmol min
μmol min
-1](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F51044012-1e7d-4f53-9311-c2b96c730020%2Ff671a3ae-ab5b-4e46-8e94-9c12baa1eab4%2Fgf58lr_processed.jpeg&w=3840&q=75)
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