An enzyme following Michaelis-Menten kinetics was found to have highest activity at 37° C and pH7. If maximum velocity for the enzyme was 2.4 x 10 mol. Lits with initial enzyme concentration of 2.4nmol, then its turnover frequency will beO 10°mol/s10 mol/s10-2mol/sO None of these

The Michaelis-Menten equation is model of enzyme kinetics. It is mainly used to characterize the…

Answered: An enzyme following Michaelis-Menten…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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ver is given. A +B C+ D 1) Calculate AG for the above react un and indicáte whether the reaction is favorable or unfavorable [A] = 0.9 M 20°C AG° = 4 KJ/mol %3D [B] = 15mM [C] = 4mM [D] = 3 M R= 8.314 J/moleK %3D %3D 4.7 and explain how you know.
If 287.9 umol of enzyme X has a Vmax = 47.8 mmol/sec, what is the value of kcat %3D sec-1? Please report answer with 1 decimal place. Please do not report units. Your Answer: Answer units MacBook Air 888 F5 F4 F3 F2 %23 %24 %24
Calculate the Km of the enzyme with these parameters. kcat = 130s^-1 Vo = 3.0 μMs-1 S = 10 μM Et = 0.09 µM
Assume that in a certain cell, the ratio of products/reactants or Keg = 809.5 (Keq is dimensionless) for the reaction Glucose + 2ATP > Glucose-1,6-diP + 2ADP, at a particular instant, the concentrations of each compound were Glucose =2.4M, ATP =11.1M, ADP -12.8M and G-6-P -28.4M. Calculate the difference (dimensionless) between Keq and the ratio of products/ractants at this instance, in this cell, to five decimal places
Calculate the actual free energy of hydrolysis of ATP, delta Gp in the erythrocytes of a new species. The standard free-energy of hydrolysis of ATP is also -30.5kJ/mol in this species, but the concentrations in this specie's erythrocytes are 0.00760 mM ATP, 0.00063 mM ADP and 0.00273 mM Pi. Assume the pH is 7.0 and the body temperature of this species is 91.0oC. Calculate your answer as kJ/mol to two decimal places.
A particular reaction has a ΔG‡ of 30.0 kJ mol-1 at 25.0 °C. In the presence of an enzyme, the same reaction has a ΔG‡ of 1.50 kJ mol-1 at the same temperature. Calculate the rate enhancement of this enzyme. (R = 8.3145 J mol-1 K-1)
For an enzyme-catalyzed reaction, the velocity was determined at two different concentrations of the substrate. Estimate the value of Vmax. [S] (MM) 10 20 88 nmol/min 79 nmol/min 67 nmol/min V(nmol/min) 51 nmol/min 27 Not enough information is given to form a reasonable estimation. 48
An enzyme-catalyzed reaction has a KM of 20.0 mmol L-1 and Vmax of 17.0 pmol s-1. When a mixed inhibitor is added, the apparent KM is 50.0 mmol L-1 and the apparent Vmax is 5.20 pmol s-1. Calculate α.
Calculate theequilibrium constant and thefree energy of (Mg)ATP hydrolysis in a closed system in which concentrations of ATP, ADP and Piare, respectively, 3.5, 1.0, and 5 mMand 25 degrees Celsius. Is the reaction spontaneous?R = 8.314 J/(deg Kelvin-mol).
The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: Vo (micromol/min) Substrate added (mM) 200 1.0 400 2.0 800 4.0 1600 8.0 3200 16.0 The enzyme concentration used in all reactions is 106 M. Which of the following is true: O A) The Km for the reaction must be less than 1 mM ○ B) It is possible to determine Km for the reaction, but not Vmax or kcat OC) It is possible to determine only kcat, not Vmax or Km D) It is not possible to determine Vmax for the reaction OE) The ratio Vmax/Km for the reaction cannot be determined
What is the Vmax of an enzyme at 1 μM with -4G RT k = 6.2x 10¹2 s-1 (Ideal gas constant R = 8.314 J K-1 mol-1) cat 0.14 μM S-1 1.4 µM s-1 14 μM s-1 0.14 mM s-1 1.4 mM s-1 activation energy (AG) of 55000 J/mol at 298K?
Calculate AG for the below balanced redox reaction as written. You may find a list of standard reduction potentials useful. 3 12 (s) + 2 Al (s) → 61 (aq) + 2 Al3+ (aq) O-4.24 x 102 kJ/mol O-6.48 x 102 kJ/mol O -2.12 x 102 kJ/mol O-1.27 x 103 kJ/mol O-6.37 x 102 kJ/mol

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An enzyme following Michaelis-Menten kinetics was found to have highest activity at 37° C and pH 7. If maximum velocity for the enzyme was 2.4 x 10 mol. Lits with initial enzyme concentration of 2.4 nmol, then its turnover frequency will be O 10°mol/s O 10°mol/s O 10-2mol/s None of these