The steady-state kinetics of an enzyme has been studied in the absence and presence of an inhibitor (Inhibitor A). The initial rate given as a function of substrate concentration in the following table: Substrate Concentration, [S] Initial rate, v, (mmol/L-min) Initial rate, v, (mmol/L-min) (mmol/L) No Inhibitor With Inhibitor A 1.25 1.72 0.98 1.67 2.04 1.17 2.50 2.63 1.47 5.00 3.33 1.96 10.00 4.17 2.38

Biochemistry
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Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
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Chapter1: Biochemistry: An Evolving Science
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1. As seen in the picture:

- What kind of inhibition (competitive, uncompetitive, mixed) is involved? 
- Calculate Vmax and Kmax in the absence and presence of inhibitor A

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The steady-state kinetics of an enzyme has been studied in the absence and presence of an inhibitor (Inhibitor A). The initial rate
given as a function of substrate concentration in the following table:
Substrate Concentration, [S]
Initial rate, v, (mmol/L-min)
No Inhibitor
1.72
Initial rate, v, (mmol/L-min)
With Inhibitor A
(mmol/L)
1.25
0.98
1.67
2.04
1.17
2.50
2.63
1.47
5.00
3.33
1.96
10.00
4.17
2.38
Transcribed Image Text:The steady-state kinetics of an enzyme has been studied in the absence and presence of an inhibitor (Inhibitor A). The initial rate given as a function of substrate concentration in the following table: Substrate Concentration, [S] Initial rate, v, (mmol/L-min) No Inhibitor 1.72 Initial rate, v, (mmol/L-min) With Inhibitor A (mmol/L) 1.25 0.98 1.67 2.04 1.17 2.50 2.63 1.47 5.00 3.33 1.96 10.00 4.17 2.38
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