A) Determine Vmax and Km of the reaction in the absence of inhibitor. B) Determine the inhibition type? C) Determine the equilibrium constant (K:) associated with the enzyme-inhibitor complex.

Biochemistry
6th Edition
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter13: Enzymes—kinetics And Specificity
Section: Chapter Questions
Problem 16P
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Problem 1. Greco et al. have developed a regression curve fitting package in 1982 and tested it on Vp vs. [S]
profiles of Hexosaminidase enzyme (see the figure below). The reactions rates were experimentally measured at
various substrate concentrations in the presence or absence of an inhibitor. P-nitrophenyl-N-acetyl-ß-D-
glucosaminide (NAG) is the substrate. 2-acetamido-2,4-dideoxy-4-fluoro-D-galactono-1,5-lactone (ADFGL) is
the inhibitor.
1
0.9
0.8
-- No Inhibitor
0.7
- 0.2 mM Inhibitor
0.6
0.5
0.4
0.3
0.2
0.1
2
[S] (mM)
Using the data given in the Figure, answer the following questions.
A) Determine Vmax and Km of the reaction in the absence of inhibitor.
B) Determine the inhibition type?
C) Determine the equilibrium constant (K;) associated with the enzyme-inhibitor complex.
V, (mM/s)
Transcribed Image Text:Problem 1. Greco et al. have developed a regression curve fitting package in 1982 and tested it on Vp vs. [S] profiles of Hexosaminidase enzyme (see the figure below). The reactions rates were experimentally measured at various substrate concentrations in the presence or absence of an inhibitor. P-nitrophenyl-N-acetyl-ß-D- glucosaminide (NAG) is the substrate. 2-acetamido-2,4-dideoxy-4-fluoro-D-galactono-1,5-lactone (ADFGL) is the inhibitor. 1 0.9 0.8 -- No Inhibitor 0.7 - 0.2 mM Inhibitor 0.6 0.5 0.4 0.3 0.2 0.1 2 [S] (mM) Using the data given in the Figure, answer the following questions. A) Determine Vmax and Km of the reaction in the absence of inhibitor. B) Determine the inhibition type? C) Determine the equilibrium constant (K;) associated with the enzyme-inhibitor complex. V, (mM/s)
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