The table below provides kinetic information when ADH is reacted with ethanol alone, NAD+ alone, and ethanol with NAD+ For the experiment that reacted both ethanol and NAD+ with ADH, estimate Vmax and KM for ADH

The table below provides kinetic information when ADH is reacted with ethanol alone, NAD+ alone, and ethanol with NAD+ For the experiment that reacted both ethanol and NAD+ with ADH, estimate Vmax and KM for ADH

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

See similar textbooks

Similar questions

Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. Consider that ADP is five times more abundant than AMP. a. Calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. b. Calculate ∆G' for ATP hydrolysis under these conditions (∆G0' for ATP hydrolysis is -32.2 kJ/mol) The energy charge is defined as ( [ATP] + 1/2 [ADP] ) / ( [ATP] + [ADP] + [AMP] )
Write out the full redox reaction that happens when both of these reactions are added to the same reaction where there is 1M concentrations of each reactant and products, pH7, and temeprature is 290K. Identify which compounds will be reduced and which compounds will be oxidized. redox reaction 1: Pyruvate¯ + 2H+ + 2e¯ → lactate¯ E'o(V) = -0.185 redox reaction 2: NAD+ + H+ + 2e¯ → NADH E'o(V) = -0.320
The following Michaelis-Menten plot shows the response of phosphofructokinase-1 (PFK-1), an enzyme in the glycolytic pathway, to the presence of ATP and AMP. Based on the data below, which of the following statements apply? Select all that apply. No inhibitors (low (ATP)) 1 mM ATP + 0.1 mM AMP 1 mM ATP 1.0 2.0 (Fructose-6-phosphate) mM Fig. : Regulation of PFK activity AMP is an allosteric modifier that enhances the binding of the substrate fructose 6-phosphate а. O b. AMP is an allosteric modifier that reduces the binding of the substrate fructose 6-phosphate ATP is an allosteric modifier that reduces the binding of the substrate fructose 6-phosphate O c. O d. ATP is an allosteric modifier that enhances the binding of the substrate fructose 6-phosphate Phosphofructokinase activity
Could you explain step by step how to solve this? I'm not sure how to get all the numbers that are shown in the solved answer.
The typical Michaelis-Menten equation mathematically describes the overall rate of the reaction as V (this is because biologists don't like math). What does V actually mean? (write the definition of V in differential equation form). V= d( )/dt Reaction rate Substrate concentration V max ·½V TURK
Consider the following redox reaction: lactate + NAD = pyruvate + NADH + H+ The relevant reductive half reactions are as follows: pyruvate + 2e + 2H+ lactate NAD+ + 2e+ H* = NADH E' -0.185 V = E' -0.320 V What is the AE' of the redox reaction? -0.505 V -0.135 V 0.135 V ○ 0.505 V
Using understanding of the thermodynamics laws, explain the energy transformations for the following processes. a. Glucose – Pyruvase + 2ATF + 2NADH b. Pyruvate – Acetyl-CoA + NaDH c. Citric acid – Oxoloacetate + 3NaDH + FADH2 + ATP d. H20 at PSII – ATP e. Photon at PSI – NADPH f. Co2 + RuBp – 3PG + ATP + NADPH – G3P (1/6 of which is converted to glucose)
You obtain a calculated Vmax of 4.26uM/s and a Km of 122.5uM from a kinetics experiment performed using 0.5uM enzyme. What is the catalytic efficiency of this enzyme?
Find the net potential
Consider the following equilibrium at 298 K. R=8.314 J/K-mol Acetyl-CoA + Oxaloacetate + H20 Citrate + COASH + H* Which one of the following is the correct value for K'eg ifAG" = -32.2 kJ/mol? O 1.11 0.987 1.01 x 10-13 13.0 9.92 x 1012 2480 4.42 x 105 2.27 x 10-6 1.01 -2480 2.56 -13.0 1.08 -0.0130 0.0130 0.926
By what factor is sample A2 more concentrated than sample A1?
Calculate the ΔG for Malate dehydrogenase reaction of CAC if the concentration of oxaloacetate is 1x 10-8 M, malate is 0.2 mM, NAD+ is 10 mM and NADH is 0.1 mM in rat liver mitochondria. ΔGo’ for this reaction is 30 kJ/mole. Please write the units of the final answer and the formula you are using to solve. R = 0.008314kJ/K*mol, T = 298K