Vmax [S] Vo = Km + [S] Eadie-Hofstee plot Lineweaver-Burk (L-B) plot v=Vm-Km si [S] Km 1 Vm Vm [S] The equations above apply for Michaelis-Menten enzyme kinetics but are presented in three different formats. For uncompetitive inhibition The Michaelis-Menten equation becomes Vo-Vmax(S/(Km+a°[S) Put the Minchaelis-Menten equation for uncompetitive inhibition in the Eadie-Hofstee format. The Y-intercept of this plot will be

Vmax [S] Vo = Km + [S] Eadie-Hofstee plot Lineweaver-Burk (L-B) plot v=Vm-Km si [S] Km 1 Vm Vm [S] The equations above apply for Michaelis-Menten enzyme kinetics but are presented in three different formats. For uncompetitive inhibition The Michaelis-Menten equation becomes Vo-Vmax(S/(Km+a°[S) Put the Minchaelis-Menten equation for uncompetitive inhibition in the Eadie-Hofstee format. The Y-intercept of this plot will be

Principles of Instrumental Analysis

7th Edition

ISBN:9781305577213

Author:Douglas A. Skoog, F. James Holler, Stanley R. Crouch

Publisher:Douglas A. Skoog, F. James Holler, Stanley R. Crouch

Chapter34: Particle Size Determination

Section: Chapter Questions

Problem 34.10QAP

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An enzyme-catalyzed reaction is studied in the absence and presence of an inhibitor and the following data was obtained. [S] in mmoles/L Velocity in mmoles/L/min-1 No inhibitor With inhibitor 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 Calculate the Km of the enzyme in the reaction without inhibitor ________________________ Km’ of the enzyme in the reaction with inhibitor ________________________ Vmax of the uninhibited reaction ________________________ Vmax’ of the inhibited reaction ________________________
Give the Vmax and Km for this enzyme that obeys Michaelis-Menten kinetics. Use 2 sig figs.
The kinetics of an enzyme are measured as a function of [S] in the presence and absence of 2 mM I. Compute Km and Vmax in the absence and presence of I S] (uM) V (uM/min) without I with I 3 10.4 4.1 5 14.5 6.4 10 22.5 11.3 30 33.8 22.6 90 40.5 33.8
Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) 0.20 per minute 0.50 per minute 1.0 per minute 2.0 per minute 5.0 per minute
In a Lineweaver-Burk plot of enzyme kinetic data, the x-intercept is –2.5 mM-1, what is the Km of the enzyme
a) Determine kcat (in units of sec-1) for a particular enzyme, given the following information: Vo = 144 mmol/min; [S] = 2 mM; Km = 0.5 mM; Enzyme Molecular weight = 40,000 micrograms/micromole; 8 micrograms of enzyme used in assay generating this data. b) In general, explain how the total enzyme concentration affects turnover number and Vmax?
The following table indicates the rates at which a substrate reacts as catalyzed by an enzyme that follows the Michaelis-Menten mechanism: (1) in the absence of inhibitor; (2) and (3) in the presence of 10 mM concentration, respectively, of either of two inhibitors. Assume [E]T is the same for all reactions.(a) Determine KM and Vmax for the enzyme. For each inhibitor determine the type of inhibition and KI and/or K’I. What additional information would be required to calculate the turnover number of the enzyme? (b) For [S] = 5 mM, what fraction of the enzyme molecules have a bound substrate in the absence of inhibitor, in the presence of 10 mM inhibitor of type (2), and in the presence of 10 mM inhibitor of type (3)?
A protein catalyzes the following reaction and had a Michaelis-Menten constant of Km=25 mM and a turnover number of 4.0 x 107 s-1. The total enzyme concentration is 0.012 µM and the initial substrate concentration is 4.76 µM. The enzyme has a single active site. Calculate the values of Vmax and V0 for this enzyme. 2H2O2 (aq) -----> 2H2O(l) + O2(g) Vmax= Vo=
An enzyme-catalyzed reaction has a Km of 1.4 mM and a Vmax of 7 nM/s. What is the initial velocity when the substrate concentration is 0.6 mM?
Salicylic acid salts inhibit the catalytic action of a glutamate dehydrogenase. Determine the type of inhibition by graphical analysis of the Following data. Assume that the salicylate concentration remains constant and is 40 mM. Also calculate the KM for the substrate and the dissociation constant for the enzyme-inhibitor complex. [S] mM 1.5 2.0 3.0 4.0 8.0 16.0 Without salicylate Product (mmol/min) 0.21 0.25 0.28 0.33 0.44 0.4 With salicylate Product (mmol/min) 0.08 0.10 0.12 0.13 0.16 0.18
Although there are accurate graphical methods available for determining Vmax and Km of an enzyme-catalyzed reaction, sometimes these parameters can be quickly estimated by examining the values of Vo as [S] increases. Estimate the values of Vmax and Km of the reaction catalyzed by an enzyme in which the following data were obtained:
If the enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM, what is its Km? Calculate Vmax of the above enzyme (lactase). Calculate the slope on a Lineweaver-Burk plot (Km/Kmax) for the above enzyme (lactase).