Biochemistry (Looseleaf)
Biochemistry (Looseleaf)
9th Edition
ISBN: 9781319114800
Author: BERG
Publisher: MAC HIGHER
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Chapter 8, Problem 40P
Interpretation Introduction

(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.

Interpretation Introduction

(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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Suppose the data below are obtained for an enzyme catalyzed reaction with and without the inhibitor I. (s)( mM) 0.2 0.4 0.8 1.0 2.0 4.0 V without i (mM/min) 5.0 7.5 10.0 10.7 12.5 13.6 V with I (mM/min) 3.0 5.0 7.5 8.3 10.7 12.5   Make a Lineweaver Burke plot for this data using graph paper or a spreadsheet  Calculate KM and Vmax without inhibitor.  What type of inhibition is observed? show graph and work 2. Give the Lineweaver Burk equation and define all the parameters. 3. When substrate concentration is much greater than Km, the rate of catalysis is almost equal to   a. kcat b. none of these c. all of these d. Kd e. Vmax
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