Which of the following is NOT an assumption in the original Michaelis-Menten equation? O Initial Rate O Constant Enzyme O E define as sum of E+ ES O Steady State
Q: An enzyme is found that catalyzes the reaction: A B A researcher have determined KM and kcat to be 4…
A: Concentration can be expressed in various units like Molar(M) , millimolar (mM) , micromolar (μM) ,…
Q: in the concerted model of enzyme action when the L ratio (T/R) is 10,000 the velocity vs. Substrate…
A: Enzymes are biomolecules that catalyze (increases the rate of the reaction ) biochemical reactions .…
Q: Which of the following statements about the Michaelis Menten constant (Km) is correct...... A. can…
A: Michaelis Menten constant (Km); It is the concentration of substrate at which the reaction rate is…
Q: The Michaelis-Menten equation for the enzyme chymotrypsin is 0.14[S] v : 0.015 + [S] where v is the…
A: The interpretation of the Michaelis-Menten model were refined by Briggs and Haldane by an assumption…
Q: The AG of a reaction is -40 kcal/mol. The AG of the enzyme- catalyzed reaction is: Oa We cannot…
A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation…
Q: All of the following statements are true about the relationships between [S], Km and Vmax EXCEPT: a.…
A: Enzymes are the biocatalyst that increases the rate of biochemical reaction without itself being…
Q: If the KM of an enzyme is 100 µM and it's Vmax = 7.5 µM.s-'. Calculate initial velocity of the…
A: Enzymes are the biocatalysts that catalyze the chemical reactions in living cells. They accelerate…
Q: Cif only statement A is correct, Hif only statement B is correct, E if both statements are correct,…
A: In the Michaelis- Menton plot, x-axis represents substrate concentration and y-axis represents…
Q: An enzyme has a Vmax OI 1.2 µM . The Km Ior its substrate is 10 µM. Calculate the initial reaction…
A:
Q: Which of the following is/are true concerning the first law of thermodynamics?
A: Thermodynamics is the part of science that deals with heat and temperature, and their relation to…
Q: Why does Km approximate but is not precisely equaté to value of Kd? Reactants are converted to…
A: Almost all the biochemical reactions are catalyzed reactions. The biological catalyst is called…
Q: 1. Calculate the reaction Kcat for the Control in experiment (1). 2. Draw a velocity versus [S]…
A: Michaelis Menton equation relates velocity of enzymatic reaction with substrate concentration.…
Q: Which of the following statements abouta plot of Vo vs. [S] for an enzyme that follows Michaelis-…
A: Introduction: Enzymes are those proteins that increase the pace of the reaction without undergoing…
Q: Disease Z is marked by the accumulation of Metabolite M - a product of the reaction: L→M. This…
A: Enzyme inhibitors are the substances that bind to Enzyme either at active site or allosteric site so…
Q: [Substrate, uM] Vo with DEDS (µM/min) Vo without DEDS (µM/min) 3.333 0.774 1.196 4.000 0.877 1.316…
A: Given data of interest (X, Y) values where X denotes the substrate concentration in uM and Vo…
Q: If a competitive inhibitor of an enzyme is added to the mixture of the enzyme and its substrate, the…
A: An enzyme can bind either substrate (forming an ES complex) or inhibitor (EI) in competitive…
Q: In which of the following conditions is the Gibbs free energy negative? O reaction is at equilibrium…
A: The biological reactions are catalyzed by enzymes. The enzyme-catalyzed reactions are spontaneous…
Q: The Km value of an enzyme-catalyzed reaction and its Vmax is 70 mmol/min. What is the rate of the…
A: Enzyme kinetics, the study of chemical reactions that are catalyzed by the enzyme. Enzymes are used…
Q: In order for two molecular species to be considered independent in a reactive process, they must be…
A: These come under the topic of material balance and use stoichiometric analysis.
Q: Suppose the reaction system CH4 (g) + 202(g) = CO2(g) + 2H2O(1) has already reached equilibrium. The…
A: Oxidation of methane takes place in the bacterial group called methanotrophs. Methanotrophs oxidize…
Q: n an enzyme reaction the enzyme has a KM of 72 mM. At which substrate concentration will the rate of…
A: "Since you have asked multiple questions, we will solve the first two question for you. If you want…
Q: The table below contains experimental data for the enzyme A; substrate concentration (mM) and…
A: The Michaelis-Menten equation is used for calculating and analyzing the reaction enzyme kinetics.…
Q: The dissociation constant, Ks, for two different enzyme preparations, preparation A and preparation…
A: Ans- Dissociation constant is a parameter which indicates the binding association between the ligand…
Q: If the starting conditions were standard conditions (at 298 K) O The reaction would proceed from…
A: ∆G=-RT In(K'eq) A reaction moves in the forward direction (left to right) if the delta G for the…
Q: The following graphical patterns (Figure 1 A and 1B) obtained from kinetic experiments have several…
A: The Michaelis–Menten equation is modified by Lineweaver–Burk and they generate a new straightline…
Q: As it applies to biological systems, the second law of thermodynamics indicates that: O If left…
A: The energy transfer is not 100 percent efficient, much like other biochemical functions. In…
Q: The G° of the reaction of reactant X to product Y is the same in its catalytic reaction and the…
A: A catalyzed reaction means the reaction is catalyzed by the enzyme. Uncatalyzed reaction means the…
Q: Which of the following is incorrect about the "initial velocity" assumption? O a. Product is not…
A: Initial velocity is one of the parameters of enzyme that can be determined by using the formula Vo=…
Q: What is true about the Gibbs free energy change at equilibrium? O The value of delta G is minimum at…
A: Gibbs free energy is measure the maximum amount of work done in a thermodynamic system when the…
Q: The following results were obtained for an enzyme-catalysed reaction Substrate concentration (mmol…
A: Enzymes are highly specialized proteins that have extraordinary catalytic power, greater than that…
Q: nthe foilowing figure, one of the following statemants is FAISE With Inhibitor 1Wmax Without…
A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation energy…
Q: A single-step chemical reaction is represented below. A + B - AB + Heat Which of the following best…
A: Proteins are the polymer of amino acid. They are joined by the peptide bond.
Q: An enzyme is discovered that catalyzes the chemical reaction A team of motivated researchers sets…
A: Enzymes are the biomolecules which acts as catalysts for many biochemical reactions and increases…
Q: För an enzyme that displays Michaelis-Menten kinetics, the Vmax is 0.06 M/min at 0.8 M (enzymes…
A: Given, Vmax = 0.06 M/min at Substrate concentration , [S] = 0.8 M At Substrate concentration [S] =…
Q: Which of the following factors does NOT always alter the activity of the enzyme? Reactant…
A: INTRODUCTION Enzymes Enzymes are biological catalyst. Enzymes are proteins that increase the…
Q: An enzyme catalysed reaction has a Km of 8 mM and a Vmax of 13 nM.s-1. Use the Michaelis-Menten…
A:
Q: AG of a reaction is influenced by the temperature at which the reaction takes place. This is due to…
A: Gibbs free energy(∆G) is the amount of free energy available to a system to do useful work. Gibbs…
Q: Which of these statements about enzyme-catalyzed reactions is false? The activation energy for the…
A: An enzyme accelerates the rate of a chemical reaction several times as compared to the uncatalyzed…
Q: what is free Gibbs energy and write the expression of free energy change. Define the exergonic and…
A:
Q: The Lineweaver-Burke plots of a reaction without inhibitor and one with non-competitive inhibitor…
A: Enzymes are catalysts that enhance the rate of biochemical reactions.
Q: In order to start a chemical reaction, the chemical reaction requires an input of energy to push the…
A: Energy is used to do each and every work.Energy can neither be created nor be destroyed,it can only…
Q: An enzyme-catalyzed reaction is studied in the absence and presence of an inhibitor and the…
A: Enzymes are involved in the catalysis of various reactions. There are different classes of enzymes…
Q: A thermodynamically spontaneous reaction O A. happens quickly, with no addition o energy to the…
A: Answer. A thermodynamically spontaneous reaction is a process that proceeds on its own and does not…
Q: Which of the listed effects would be brought about by any enzyme catalyzing the following simple…
A: Introduction: Those compound that increases the rate of the reaction without undergoing any change…
Q: Which of the following commonly regulates enzyme activity in vivo? O a. An amino acid replacement O…
A: Introduction Enzymes are proteins that function as catalysts in biological reactions to speed up the…
Q: of ênergy are being minimized as the system and surroundings are coming to equilibrium. 20. A…
A: Gibbs free energy change, entropy change and enthalpy change of a system of the system by the…
Q: The enzyme E catalyzes the chemical reaction, X ⇌ Y. Imagine two different cases, a) initial…
A: Introduction According to the Michaelis-Menten equation, when the rate of an enzyme-catalyzed is…
Q: The following data describe an enzyme-catalyzed reaction. Plot these results using the…
A: Enzymes are biocatalysts that catalyze a biochemical reaction by lowering the activation energy. An…
Q: n enzyme-catalyzed reaction has a change in free energy equal to -20 kcal/mol. If ou double the…
A: Free energy determines whether a conversion of reactants to products will occur spontaneously or…
don't copy from internet
Step by step
Solved in 3 steps
- Use the concept of Hess' Law to determine AH for the process V 2X +Z given the following numbered processes: V 2 W AH1 W X + Y AH2 Z- 2Y AH3 ΔΗ+ ΔH +ΔΗ3 ΟΔΗ+ 2ΔΗ-ΔΗ3 ΟΔΗ+ 2ΔΗ2+ ΔΗ3 ΔΗ + ΔH,-ΔΗ3In considering active transport by Na + -K + -ATPase at body temperature (37 o C), 3 Na+ are pumped out of the cell and 2 K + are pumped in for each ATP that is hydrolyzed to ADP + P i . Given that underyour experimental conditions, the DG for ATP hydrolysis is -10 kcal/mol, and that V is -60 mV, and that the pump maintains the internal Na + at 10mM, external Na + at 120 mM, internal K + at 120 mM and external K + at 8mM, what is the efficiency of the pump (i.e., what fraction of the energy available from ATP hydrolysis is required to drive transport at the provided levels)?when the substrate concentration of certain enzyme is quarter than Michaelis constant, the velocity of enzyme will be... * 3/4 V max 1/5 V max Non of these 2/5 V max 1/4 V max 3/5 V max
- QUESTION 5 Consider the graph below. Reaction rate (v) Vmax 0 Effector 3 mM Effector 1 mM. Control 0 mM Ko.5 (3) Ko.5 (1) Ko.5 (0) [S] Which of the following conclusion(s) can be drawn from the data illustrated in the figure?The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V% for an enzyme-catalyzed, single-substrate reaction E + S=ES → E + P. The model can be more readily understood when comparing three conditions: [S] > Km- Match each statement with the condition that it describes. Note that "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] > Km Not true for any of these conditions [ES] is much lower than [Efree]. Reaction rate is independent of Increasing [Etotal] will lower Almost all active sites will Km- be filled. [S). [Efree] is about equal to [Etotal]. Show All W- 5179933 (3).docx 5179933 (4).docx PCR-MINI RES....docx MacBook ProMany enzymes obey simple Michaelis–Mentenkinetics, which are summarized by the equationrate = Vmax [S]/([S] + Km)where Vmax = maximum velocity, [S] = concentration ofsubstrate, and Km = the Michaelis constant.It is instructive to plug a few values of [S] into theequation to see how rate is affected. What are the rates for[S] equal to zero, equal to Km, and equal to infinite concen-tration?
- For an enzyme that has a Km of 25 mM, Vmax of 50 mM/s and kcat of 250 s-1, how long does a single reaction take? Select one: 50 ms 250 ms 4 ms 25 s 4 sA bacterial enzyme catalyzes the hydrolysis of maltose as shown in the reaction given below: Maltose + H2O -> 2 glucose If the reaction has a Km of 0.135 mM and a V max of 65 umol/min. What is the reaction velocity when the concentration of maltose is 1.0 mM? (Please take note of the units)An enzyme that follows simple Michaelis–Menten kinetics has an initial reaction velocity of 10 µmol⋅min-1 when the substrate concentration is five times greater than the KM. What is the Vmax of this enzyme in µmol⋅min−1?
- -Inhibitor +Inhibitor [S] (mM) V0&νβσπ; (μmol/sec). V0&νβσπ:&νβ σπ: (μmollsec) 0.0001 33 17 0.0005 71 50 0.001 83 67 0.005 96 91 0.01 98 95 What is the Km of this enzyme WITH iinhibitor?The enzyme phosphoserine phosphatase catalyses the reaction: phosphoserine + H2O → serine + Pi Kinetics measurements were performed using a range of Mg* concentrations and in the presence of different fixed concentrations of Ca-". The enzyme requires Mg²* for activity. The following data were recorded: [Ca²*] / mM 0.0 20.0 40.0 [Mg*]/ mM Initial velocity / µmol of product min 0.33 20.40 9.26 5.99 0.50 25.65 12.66 8.47 1.00 33.30 20.00 14.28 2.00 40.00 28.57 22.23 What type of inhibitor is Ca2* and what is its Kf? Suggest what role Mg** performs in the catalytic mechanism of phosphoserine phosphatase. Suggest how Ca2* inhibits the reaction.Regarding the reasoning for the Michaelis-Menten equation to be unsuitable for accurate analysis of experimental data, select all that apply: It is nonlinear It is only valid for reactions at equilibrium It is not valid under experimental conditions Extrapolation to Vm is inaccurate and therefore Km also cannot be accurately described