The following data were obtained in a study of an enzyme that is known to follow the Michaelis-Menten kinetics. Approximately, what is the value of Km tor this enzyme?Substrate added,umol/LVo uM/sec48971751871921972161001000198OA 1 uMO8.2 pMOC 4 uM.OD. 8 uMOE 16 IMOF 1000 uMOG 97 uM/secOH 175 UM/sec

Michaelis menten constant, Km is the substrate concentration required to produce half maximum…

Answered: The following data were obtained in a…

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

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A particular reaction has a ΔG‡ of 37.0 kJ mol-1. In the presence of an enzyme, the same reaction has a ΔG‡ of 5.70 kJ mol-1. Calculate the value of ΔΔG‡ in kJ mol-1.
How to identify the Vmax and the Michaelis constant (Km) in an enzyme kinetics graph?
Chymotrypsin is an enzyme that is optimized to function in the small intestine (at a pH of ~7.4). Explain, given what you know about the chymotrypsin mechanism and what we learned about acid/base chemistry, why chymotrypsin would not be able to initiate catalysis if it were secreted into the stomach (pH ~2.5).
In mathematical terms, what characteristic of a graphed line is a measure of enzymereaction rate?
When 10 micrograms of an enzyme with a molecular mass of 80,000 Daultons (grams/mol) is added to a solution containing its substrate at a concentration 100 times the Km, it catalyzes the conversion of 65 micromoles of substrate into product in 3 minutes. What is the enzyme's turnover number (in units of min-1)?
From a kinetics experiment, the Vmax was determined to be 450µM∙min-1. For the kinetic assay, 0.1mL of a 0.05mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 125,000 g/mole. Assume a reaction volume of 700µL. Calculate the kcat (in sec-1) for the enzyme.
How can you find Kcat if you are only given Vmax, Km and [E] ? I tried using Kcat=Vmax/[E] but that didn't work. How do you know if [E] is the same as [E]total, and if it isn't how do you find it from this information: The Vmax for a particular enzyme is 10 nmols/L/s. The Km for its substrate is 5 microM. If the enzyme concentration is 10 nM, what is the kcat? a.80 nmoles/L/s b.8000 nmoles/L/s c.2 nmoles/L/s d.50 nmoles/L/s
The following data was obtained during kinetic analysis of an enzyme with and without an inhibitor. Substrate concentration (mM) Reaction rate without inhibitor (µM/s) Reaction rate with inhibitor (µM/s) 10 28 12 20 50 23 40 83 42 60 107 58 100 139 83 200 179 125 300 197 150 400 209 167 560 227 197 How do you calculate the KM for the enzyme in the absence of an inhibitor. And how do you calculate kcat with the given enzymatic concentration of 5 µM.
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The accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried out in the presence, or absence, of aninhibitor. Indicate what type of inhibition is predicted based on eachLineweaver–Burk plot. For each plot indicate which line corresponds to thereaction without inhibitor and which line corresponds to the reaction withinhibitor present.

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The following data were obtained in a study of an enzyme that is known to follow the Michaelis-Menten kinetics. Approximately, what is the value of K for this enzyme?