What is the Vmax of an enzyme at 1 µM with an activation free energy (AG#) of 55000 J/mol at 298K?-AG #RTkcat= 6.2× 10¹²(Ideal gas constant R = 8.314 J K¯1 mol-¹1)0.14 μM s-1-1S-11.4 μM s14 μM s-10.14 mM s-11.4 mM s-1

Catalytic efficiency of enzymatic reaction (turnover)K values tell the speed or rate with which a…

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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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You are evaluating the kinetics of an enzyme catalyzed reaction containing 5.5 μM total enzyme and 11.2 μM substrate. At this substrate concentration, you determine that the Vo = 88.6 μmol mL-¹. s-¹. If the Vmax 833.3 mM s the KM is: . == " 30.9 μΜ 10.4 μΜ Ο 124.6 μΜ 234 μΜ 94.5 μM
An enzyme catalyzes a reaction with a Km of 9.50 mM and a Vmax of 2.10 mM · s-1. Calculate the reaction velocity, vo, for each substrate concentration. [S] = 3.25 mM vo : mM · s-1 [S] = 9.50 mM mM · s-1 Vo :
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?
What is time constant ? The steel ball bearings of 40 mm diameter and initially at uniform temperature of 600 °C are quenched in an oil bath maintained at 50 °C temperature. The heat transfer coefficient between the ball bearing and oil is 325 W/m2-K and the thermodynamics properties of the bearing can be taken as : k 45 W/m-K and thermal diffusivity a = 1.25 x 10-5 m/s. Determine : The time duration for which bearing must remain in oil to attain 225 °C temperature. b. The instantaneous heat transfer rate from the bearings when they are first immersed in oil and when they reach 225 °C.
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Inside cells, the AG value for the hydrolysis of ATP to ADP + Pi is approximately -50 kJ/mol (-12 kcal/mol). Calculate the approximate ratio of [ATP] to [ADP][Pi ] in cells at 37°C. AG = AG + RT InKe R= 8.315 x 10³ kJ mol deg T= 298 K Table 15.1 Standard free energies of hydrolysis of some phosphorylated compounds Compound kJ mol- kcal mol- Phosphoenolpyruvate 1,3-Bisphosphoglycerate Creatine phosphate ATP (to ADP) -61.9 -14.8 -49.4 -11.8 -43.1 -10.3 -30.5 - 7.3 - 5.0 Glucose 1-phosphate Pyrophosphate Glucose 6-phosphate -20.9 -19.3 -4.6 -13.8 3.3 Glycerol 3-phosphate - 9.2 2.2 biochemistry
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a) Calculate the enzyme and specific activity of a reaction with 3 μM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200 L M-1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) above
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)
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What is the Vmax of an enzyme at 1 µM with an activation free energy (AG*) of 55000 J/mol at 298K? -4G* RT k=6.2x 10¹² cat (Ideal gas constant R = 8.314 J K¹ mol-¹) 0.14 μM S-1 1.4 μM s-1 14 μM s-1 0.14 1.4 mM S-1 0000 mM s-1

What is the Vmax of an enzyme at 1 µM with an activation free energy (AG) of 55000 J/mol at 298K? -4G RT k=6.2x 10¹² cat (Ideal gas constant R = 8.314 J K¹ mol-¹) 0.14 μM S-1 1.4 μM s-1 14 μM s-1 0.14 1.4 mM S-1 0000 mM s-1