How many kJ/mol must an enzyme lower the activation energy of the reaction to make it useful? We known that in the absence of a catalyst a certain biochemical reaction occurs x times per second at normal body temperature which is 37 degrees C. The reaction needs to occur 5000 times faster than when it's uncaralyzed in order to be physiological useful. For this problem use the Arrhenius expression for the rate constant k to derive the equation for deltaEa under constant temperature.

Q: An enzyme catalyzes a reaction with a Km of 5.00 mM and a Vmat of 2.25 mMs. Calculate the reaction…

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Q: 2. Which of the following kinds of catalysis can be explained by the adsorption theory? A. enzyme…

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Q: For an enzyme -catalyzed reaction, Km=10.0 mmol dm³, vmax=0.250 mmol dm3 s-l; [E]o= 2.3 x 10-6 mmol…

A: Calculation of Kb: Kb=vmax[E]0=0.250 mmol dm-3 s-12.3×10-6 mmol dm-3=0.11×106 s-1

Q: The enzyme catalase catalyzes the decomposition of H₂O₂ to H₂O and O₂. Use the [H₂O₂] (mmol·L-¹) R…

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A: It is given that the energy of activation (Ea) of uncatalyzed reaction is 125 KJ/mol or 125000 J/mol…

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Q: 4. The following rate constants have been determined for a Michaelis –Menen enzyme: ki = 2.5 x 10$…

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A: The rate of a reaction is defined as change in concentration of reactants or products with respect…

Q: 1. Initial rates of enzyme-catalyzed reaction for various substrate concentrations are listed below:…

A: Rate(V) mol/(L.min)*106 Substrate concentration (s) (mol/L (1/v)*10-6 1/s 177 0.0041 0.00565…

Q: For the attachment of a substrate to the active site of an enzyme: k1 S+E→ SE k-1 The equilibrium…

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Q: Which one of the following is true regarding our coverage of enzyme kinetics? Increasing the…

A: Fourth option is correct.

Q: For enzymatic reaction, a mechanism was proposed by Michaelis and Menten as follows: E  +  S  ↔ ES;…

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Q: 8.14 Isocitrate lyase catalyzes the following reaction: isocitrate ion → glyoxylate ion + succinate…

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Q: Determine the value of the turnover number of the enzyme catalase, given that RmaxRmax (Vmax)(Vmax)…

A: Step 1: In case of enzyme catalysis, the total number maximum molecules that can be converted into…

Q: (i) For the following reaction catalysed by an enzyme E E +S ES k-1 2, E + P outline the…

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Q: max represents the rate of reaction for an enzyme-substrate pairing under what conditions? A) when…

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Q: What is the value for the dissociation constant Kd,C ’ of the enzyme-cofactor complexing the…

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Q: For the following reaction catalysed by an enzyme E k1 E + S = ES k-1 E + P • describe the meaning…

A: Since you have posted a question with multiple sub-parts, we will solve first three subparts for…

Q: An enzyme catalyzes a reaction with a KmKm of 7.507.50 mM and a VmaxVmax of 3.00 mM⋅s−1.3.00 mM⋅s−1.…

A: Given: Km = 7.50 mM  Vmax = 3.00 mM⋅s−1

Q: How do we measure enzyme kinetics? a. By measuring the initial rate (or velocity) b. By…

A: Given: Measurement of enzyme Kinetics:

Q: By what factor is the rate of a reaction changed if an enzyme lowers the Ea by 6.0 kJ/mol at 37°C?

A: Given:  Temp = 37°C = 310K. Ka= 6KJ/mol Now using Arrhenius Eqn:   ln (K)= Ea/RT  Ea = ln(K) RT  Ea…

Q: Michaelis-Menten kinetics is sometimes referred to as “saturation” kinetics. Why?  22. Give the…

A: Since you are posted with multiple questions. As per the rule, I am answering first question only.…

Q: 3. The following data for the first-order decomposition of penicillin are obtained from Swintosky et…

A: Arhenius Equation: ln k =-EaRT +ln A

Q: 25. A student measures the following initial rate data for an enzyme that obeys Michaelis- Menten…

A: As the enzyme obeys Michaelis-Menten kinetics, so the plot of 1/[V0] vs 1/[S] would be linear. From…

Q: The turnover number of an enzyme obeying Michealis-Menten kinetics is equal to: O kcat KM O k1/k.1 O…

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Q: 10.38. The following data relate to an enzyme reaction. 10³[S]/mol dm³ 105 V/mol dm³ s-1 2.0 13 4.0…

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Q: 2.2 Suppose that the following sequence describes the reactions of two different substrates…

A: solution               Find the rate of equation by making the Michaelis - Menten assumption = ?

Q: The enzyme-catalysed conversion of a substrate at 25 oC has a Michaelis constant of 0.045 mol dm-3.…

A: Enzyme catalyzed reaction: to catalyze such reactions enzyme is used as a catalyst that binds to one…

Q: What parameters associated with enzyme activity are related to the Arrhenius equation? How can those…

A: EXPLANATION: ⦁ The dependence of the rate constant in a chemical reaction is given in Arrehenius…

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Q: E17F.5(b) The enzyme-catalysed conversion of a substrate at 298K has K 0.032mol dm and concentration…

A: Given:KM = 0.032 mol.dm-3Vmax = 4.25×10-4 mol.dm-3s-1.Enzyme concentration [ET] = 3.60×10-9…

Q: Certain bacteria use the enzyme penicillinase to decom- pose penicillin and render it inactive. The…

A: Given,       Michalis - Menten constants for pencillinase to decompose penicillin  are Km = 5×10-5…

Q: Explain why the velocity constant (k) of the complex reaction [Co(NH3)5N3]2+ with [Cr(H2O)6]2+ is on…

A: The combination of the appropriate ligands to the metal ion provides the corresponding coordination…

Q: How can we explain the enzyme’s sigmoidal kinetics in light of the structural observations?

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Q: Discuss the featu res. applications. and limitations of the Michaelis-Menten mechanism of enzyme…

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Q: The enzyme examase catalyses the following reaction, A - B where A is the reactant and B is the…

A: To find: To find the specific activity of examase using the given chemical reaction

Q: what is the approximation used to derive the reaction rate for an enzyme catalysed reaction that…

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Q: The ha lf-l ife of pyruvic acid in the presence of an aminotransferaseenzyme (which converts it to…

A: For the first-order reaction, the half-life relates to the rate constant (k) as follows: t12 =…

Q: Suppose that a certain biologically important reaction is quite slow at physiological temperature…

A: Arrhenius equation is given by,

Q: In order to describe the reaction sequence of two different substrates catalyzed by an enzyme; E +…

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Q: The activation energy for the denaturation of a protein is 385 kJ/mol. At what temperature will the…

A: Given Ea = 385 kJ T1 = 25°C

Q: The catalytic efficiency of an enzyme is given by the ratio kcat/Km. What is the limiting factor…

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Q: 15. Consider an enzyme that has a kcat that is 1000.0 times larger than kuncat at 15°C. If the…

A: T = 15°C  Or T = 15+273 = 288 K  16.5 KJ/mol enzyme decreases the activation energy for the…

Q: The data in the table below describe an enzymatic reaction. The relative molecular mass of the…

A: Molecular mass of enzyme     = 50000 gmol Concentration of the enzyme = 2 × 10-3 gcm-3

Q: The steady state assumption, as applied to enzyme kinetics, implies: A. Km = Ks. %3D B. the enzyme…

A: The steady state approximation can be applied to enzyme kinetics. An enzyme is a biological catalyst…

Q: Which of the following is true about Michaelis-Menten kinetics? A   It assumes covalent binding…

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Q: Calculate the activation energy for vacancy formatin in Aluminuim, given that the equibilirium…

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