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(a)
Interpretation:
The peptide that can be digested most rapidly and most slowly should be determined.
Concept introduction:
KM is the Michaelis constant which is the substrate concentration at the half of the Vmax. k2 is also referred as kcat which is known as turn over number. The turnover number is defined as the number of substrate molecules converted into product per unit time at a single catalytic site. The ratio between kcat/KM is a measure of enzyme efficiency and specificity for a common substrate.
(b)
Interpretation:
The features of the amino acid sequence describing the specificity of the enzyme should be suggested.
Concept introduction:
KM is the Michaelis constant which is the substrate concentration at the half of the Vmax. k2 is also referred as kcat which is known as turn over number. Turn over number is defined as the number of substrate molecules converted into product per unit time at a single catalytic site. The ratio between kcat/KM is a measure of enzyme efficiency and specificity for a common substrate.
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Chapter 8 Solutions
Biochemistry
- Show a mechanism that leads to the opening of the ring below under acid-catalyzed conditions. Give the correct Fischer projection for this sugar.arrow_forwardWhat is the stereochemical relationship between B & C?arrow_forwardDon't use ai or any chat gpt will dislike okk just use accurate information okkk okkk just solve full accurate. don't use guidelines okk just did it accurate 100% sure experts solve it correct complete solutions okkk follow all instructions requirements okkkarrow_forward
- Problem 15 of 15 Submit Using the following reaction data points, construct Lineweaver-Burk plots for an enzyme with and without an inhibitor by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. Using the information from this plot, determine the type of inhibitor present. 1 mM-1 1 s mM -1 [S]' V' with 10 μg per 20 54 10 36 20 5 27 2.5 23 1.25 20 Answer: |||arrow_forward12:33 CO Problem 4 of 15 4G 54% Done On the following Lineweaver-Burk -1 plot, identify the by dragging the Km point to the appropriate value. 1/V 40 35- 30- 25 20 15 10- T Км -15 10 -5 0 5 ||| 10 15 №20 25 25 30 1/[S] Г powered by desmosarrow_forward1:30 5G 47% Problem 10 of 15 Submit Using the following reaction data points, construct a Lineweaver-Burk plot for an enzyme with and without a competitive inhibitor by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. 1 -1 1 mM [S]' s mM¹ with 10 mg pe 20 V' 54 10 36 > ст 5 27 2.5 23 1.25 20 Answer: |||arrow_forward
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