TOMA given enzyme is able to utilize five different substrates. The Km's havemeasured for each substrate. Which substrate is most likely the biochemirelevant one in the cell? In other words, which one is most likely the predvivo substrate for this enzyme? (Choose the one best answer).Substrate 1 with KM= 4.7 × 10-1 M.Substrate 2 with Km = 1.5 × 10-2 M.Substrate 3 with KM = 1.5 x 10-8 M.×Substrate 4 with Km= 4.7 × 10-³ MSubstrate 5 with KM = 4. 7 × 10-5 M What is an order of the movement of electrons through the electron transport chain?Choose the one most correct answer.NADH->Complex II->Ubiquinone->Complex III -> Cyt C -> Complex IVFADH2 -> Complex II -> Ubiquinone -> Complex III -> Cyt C -> Complex IVFADH2->Ubiquinone->Complex I->Cyt C->Complex II->Complex IVFADH2 -> Complex I -> Cyt C -> Complex III -> Ubiquinone -> Complex IVE7

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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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Similar questions

In the same kinetics experiment above without the inhibitor, what is the fraction of occupied enzyme at substrate concentration 1microM ? How about when it's 1mM ?
Enzyme X has a Km of 2 µM and a kcat of 104 s1. In the presence of an inhibitor, Km increases to 4 µM but kcat doesn't change. Is the inhibitor competitive, uncompetitive, or mixed? And what are the value(s) of a and/or a'? Choose N/A if not applicable. Inhibitor = [ Select ] [ Select ] a = a'? = [ Select]
200 ml of a 2% protein solution containing an enzyme that you want to purify. Half of the sample is subjected to method A, consisting of fractionated precipitations and 5 ml of final solution are obtained, with a concentration protein equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml, with protein richness equal to 10 mg / ml and with an activity enzymatic also equal to 2000 U / ml. You want to know: a) Which of the two methods has provided the purest enzyme. b) By which of the methods the greatest amount of enzyme has been obtained.
I need help with parts d-g a.) For Ado: catalytic efficiency = 4.18 x 106 M-1s-1 For ATP: catalytic efficiency = 12.1 x 107 M-1s-1 b.) Both specificity constants are below the diffusion limit so neither substrate is limiting the reaction rate due to diffusion c.) Line weaver Burk equation for AdoK enzyme with Ado substrate: y = 0.68x + (2.04 x 104), where y = 1/vo and x = 1/[Ado]
The purpose of the progress curve is to determine if an enzymatic reaction rate remains constant for given concentrations of enzyme and substrate, for a given assay time (20 min). How long did the rate of reaction of WGAP remain constant in your experiments? How do you know? What would cause the reaction rate to not be constant and plateau after some time?
.When saturated with substrate, an enzyme has a maximum initial rate of 110 umoles of substrate converted to product per second. At a substrate concentration of 100 µM, the same enzyme converts substrate to product at a rate of 0.010 mmoles/sec. Assuming that Michaelis- Menten kinetics are followed, calculate the reaction rate when substrate concentration is 2 x 10 M.
-Inhibitor +Inhibitor [S] (mM) V0&νβσπ;(μmol/sec). νο&νβσπ: &ν βσπ (μmol/sec) 0.0001 33 17 0.0005 71 50 0.001 83 67 0.005 96 91 0.01 98 95 What is the Vmax of this enzyme WITH iinhibitor?
2. The enzymatic reaction rate r is given by equation 2 below as a function of substrate concentration Cs and kinetics parameters KM and rmax. Using linear and nonlinear regression in excel, evaluate the kinetic parameter constants of a biosystem given the gathered data from a series of batch runs
Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the catalytic efficiency for this reaction. Report your answer in scientific notation to three significant figures in units of M-1s-1.
Table 1. Kinetic parameters of a chosen model wild-type (WT) enzyme and three catalytically-improved mutants (M1 to M3). Enzyme variants k (8¹) WT MI M2 M3 50 500 1000 50 K₁, (μM) 10 100 100 1 k/K (HM¹¹ s¹) 5 The study above was done on a wildtype enzyme and three genetically-engineered mutants. The purpose was to find a mutation to improve the catalytic efficiency of the enzyme for industrial use. Which is the most accurate statement concerning the data? M2 is the optimal choice when substrate concentrations are saturating. The wildtype enzyme is still preferable to M3 when S<
what is the relation between K'eq and mass action ratio (Q) for biochem? specifically what are the signs of delta G and delta G' and when is the reaction near equilibrium
The 2 eynzymes are affected by a substrate. Choose all correct answers.

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