An enzyme-catalyzes the isomerization of substrate S to product P. The enzyme has a molecular weight of 120,000 g/mol. In assays using 1 μg of enzyme per assay the Km was 3 x 10^-3M and the Vmax was 2.75 μmole per minute. What would be the Kcat (turnover number or molecular activity) of the enzyme under these conditions? 2.75 min^-1? 3,300,000 min^-1? 330,000 s^-1? 19,800,000 min^-1? 5,500 s^-1?
Q: The catalytic efficiency of many enzymes depends on pH. Chymotrypsin shows a maximum value of kaKM…
A: Chymotrypsin is a protelytic enzyme acting in the digestive system of many organisms. It facilitates…
Q: Enzyme hydrolysis of glucose-6-sulfate occurs in a marine microorganism. The activity test is based…
A: Given: KM = 6.7 x 10-9 , Vmax= 300 nM min-1 = 300 x 10-9 m/ min-1, Substrate = 2 x 10-5 M Velocity =…
Q: ENZYME KINETICS ANALYSIS Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric…
A: Enzyme kinetic: [S]is the concentration of substrate V is the velocity The Lineweaver-Burk plot of…
Q: An enzymatic reaction with KM = 4.4 x 10-5 M, is carried out in 400 μL of of solution containing…
A: Given Values: Eo= 0.20 nmoles Vmax=6.6×10-3 M/s Km=4.4×10-5 M
Q: 1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the…
A: Hello. Since your question has multiple sub-parts, we will solve the first three sub-parts for you.…
Q: 1-In the first experiment, the researchers use a total enzyme concentration ([Et]) of 4 nM. They…
A: The Michaelis–Menten equation is the rate equation for a single-substrate enzyme-catalyzed reaction.…
Q: A. Determine the standard Gibbs free energy of the reaction. B. In dying E. coli cells, the…
A: Hexokinase is a initial glycolysis enzyme and rate limiting enzyme, catalyzes the phosphorylation of…
Q: Incubating 10µl of an LDH sample for 5 min in the presence of 60mM of lactate and 100mM NAD+…
A: Lactate Dehydrogenase (LDH) activity can be figured using a spectrophotometric assay. The reaction…
Q: The equil ibrium constant for the attachment of a substrate to the active site of an enzyme was…
A: The equilibrium constant of a chemical reaction is the value of its reaction quotient at chemical…
Q: Tris [tris(hydroxymethyl)aminomethane] is a common buffer for studying biological systems. (K, =…
A: pH generally refers to the periodic element and a unit of measurement and the full form is potential…
Q: An allosteric enzyme that follows the concerted mechanism has a T/R ratio of 500 in the absence of…
A: Enzymes are a type of catalyst that is responsible for enabling and accelerating many important…
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: The hypothetical enzyme happyase catalyzes the reaction SAD+ HΑPPY At maximum rate, the enzyme…
A: Turnover number and catalytic efficiency: Turnover number: It is the number of reactions occurring…
Q: 2. Initial rate data for an enzyme following Michaelis-Menten kinetics are shown below when the…
A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation…
Q: RuBP carboxylase is not an idel enzyme by any means. Describe some of the active site's and…
A: There are two stages to the photosynthetic process: Phases of photochemistry and biosynthesis…
Q: Compare Vmax and Km of the enzyme without inhibitor and in the presence of acetazolamide. Determine…
A: Michaelis menten constant, Km is the substrate concentration required to produce half maximum…
Q: A research group discovers a new version of happyase, that catalyzes the chemical reaction HAPPY…
A: Km is defined by the concentration of substrate allowing an enzyme to achieve half of the maximal…
Q: columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in…
A: Michaelis Menton equation relates velocity of enzymatic reaction with substrate…
Q: You are studying an enzyme that you isolated from cells growing at 25°C in an alkaline environment…
A: Vmax is the reaction rate given at the moment the enzyme is fully saturated by substrate. This…
Q: What is the concentration of enzyme (in mM) needed to achieve a Vmax of 8.00 mM/s if the enzyme has…
A:
Q: multiple choice, choose the correct answer You stumble upon a potential inhibitor (I) for HIV…
A: Introduction In non-competitive inhibition, the inhibitor and substrate can bind simultaneously to…
Q: Enzymes catalyze chemical reactions. What constitutes the active site of an enzyme? What are the…
A: Enzymes are specialized proteins that catalyze all biochemical reactions in the cell. Enzymes affect…
Q: 2. When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due…
A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation energy…
Q: Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed…
A: Enzymes are the protein molecules that increase the rate of reaction by decreasing the activation…
Q: 31. The velocity of a particular enzyme-catalyzed reaction varied with pH as shown in the adjacent…
A: Enzyme activity is at its maximum value at the optimum pH. As the pH value is increased above or…
Q: 2C Two homologues of this enzyme from different species both catalyze the reaction SY with distinct…
A: Hi! Thank you for the question. We are authorized to answer one question at a time, since you have…
Q: Many enzymes obey simple Michaelis–Mentenkinetics, which are summarized by the equationrate = Vmax…
A: Michaelis-Menton kinetics is an equation that describes the rate of enzymatic reactions by relating…
Q: It's a three part question based on the chart provided asking: a) Which of these enzymes has the…
A: For an enzyme catalyzed reaction, Km is the substrate concentration that is required to attain half…
Q: Legend: Blue – wild-type β-galactosidase Red – mutant β-galactosidase _________ a. What is the…
A: The amino acid sequence of a protein determines the structure and hence the function of a protein.…
Q: Glucose can be isomerized to fructose to glucose isomerase. The enzyme kinetics of this enzyme was…
A: From the Given Data, I have plotted the XY plot where, 1/S is on X-axis and 1/V on Y-axis. This is…
Q: Studies at diff erent pH’s show that an enzyme has two catalytically important residues whose pKs…
A: The pKa or pK value is the negative base-10 logarithm of the acid-base dissociation constant (Ka) of…
Q: 3. (а) 0.0050 M operate at one-quarter of its maximum rate? At what substrate concentration would an…
A: To study an enzyme kinetics, Michaelis-Menten kinetics equation is best known mathematical…
Q: Urease enzyme hydrolysed urea at [S]= 0.03 mmol/L with a Km value of around 0.06 mmol/L. The initial…
A: Vmax is the reaction's maximum speed at which all of the enzymes become saturated with the…
Q: An enzyme that follows simple Michaelis–Menten kinetics has an initial reaction velocity of 10…
A: GIVEN VALUES: Initial velocity= 10 μmol.min-1 Substrate concentration is 5 time the value of Km .…
Q: 2. A 500ul reaction containing 0.5 pmol of an enzyme following Michaelis –-Menten kineties with…
A: Enzyme increases the rate of the reaction without altering the equilibrium of the reaction. Enzymes…
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: An enzyme catalyzes a reaction with a Km of 7.50 mM and a Vmax of 2.90 mM · s-!. Calculate the…
A: Enzymes are highly specialized proteins that have extraordinary catalytic power, greater than that…
Q: The kinetic data for the activity of 0.01mM enzyme is shown below. The concentration of {S} is…
A:
Q: 8. In a separate enzyme happyase experiment using [Et] = 10 nM, the reaction velocity is measured at…
A: The [s] in the experiment is as follows:
Q: The Vmax for a particular enzyme is 10 nmols/L/s. The Km for its substrate is 5 microM. If the…
A: Given that, the Vmax for a particular enzyme is 10 nmol/L/s. The Km for its substrate is 5 uM. We…
Q: he Michaelis-Menten rate equation for reversible mixed inhibition is written as Vo max [S] akm + a'…
A: Michaelis-Menten equation represents enzyme-catalyzed reactions with a single substrate. Based on…
Q: 3. (а) 0.0050 M operate at one-quarter of its maximum rate? At what substrate concentration would an…
A: To study an enzyme kinetics, Michaelis-Menten kinetics equation is best known mathematical…
Q: 23. The graph below is a graph of Vmax (a) Label the graph clearly with both the Vmax and the Km.…
A: As given in the question, V/Vmax was plotted with substrate concentration. V= rate of a reaction…
Q: 1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the…
A: As per Michaelis Menton kinetics, Vmax is the maximum velocity which can be attained by enzyme…
Q: Consider two enzymes A and B, which are not related. However, the two enzymes coincidentally share…
A: Consider two enzymes A and B, which are not related. However, the two enzymes coincidentally share…
Q: The enzymatic activity of an enzyme with Kg = 2 mM that converts substrate S into product P is…
A: Enzymes are highly specialized proteins that have extraordinary catalytic power, greater than that…
Q: multiple choice, choose the correct answer Under which of the following conditions would an enzyme…
A: The enzyme is protein molecules that increase the rate of the reaction by decreasing the energy of…
Q: 2. Relation between Reaction Velocity and Substrate Concentration: Michaelis-Menten Еquation (a) At…
A: Michaelis-Menten model of enzyme kinetics is a very useful model which describe the relationship…
Q: a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of…
A: Michaelis Menton equation relates velocity of enzymatic reaction with substrate concentration.…
Step by step
Solved in 2 steps with 2 images
- An enzyme catalyzes the reaction M↽−−⇀N M ↽ − − ⇀ N . The enzyme is present at a concentration of 2.0 nM 2.0 nM , and the ?max V max is 2.1 μM s−1 2.1 μM s − 1 . The ?m K m for substrate M M is 6.3 μM 6.3 μM . Calculate ?cat k cat .What values of ?max and ?m would be observed in the presence of sufficient amounts of an uncompetitive inhibitor to generate an α′ of 1.9?(a) At what substrate concentration would an enzyme with a kcat of 30.0s−1 and a Km of 0.0050 M operate at one-quarter of its maximum rate?(b) Determine the fraction of Vmaxthat would be obtained at the following substratecon centrations [S]: ½Km, 2Km, and 10Km.(c) An enzyme that catalyzes the reaction X ⇌ Y is isolated from two bacterial species.The enzymes have the same Vmax but different Km values for the substrate X. Enzyme A has a Km of 2.0 μM, and enzyme B has a Km of 0.5 μM. The plot below shows the kinetics of reactions carried out with the same concentration of each enzyme and with [X] = 1 μM. Which curve corresponds to which enzyme?An enzyme has a rate enhancement of 1.3x106. Calculate the value of ΔΔG‡ at 25.0 °C in kJ mol-1. (Hint: be sure to pay attention to units and signs.) (R = 8.3145 J mol-1 K-1)
- An enzyme “happyase” catalyzes the reaction: sad to happy. For total enzyme concentration of 4 nM, the measured Vmax was 3.2 μM/S. What is the kcat for happyase ______ and what is its unit _____ (shown in fraction format, eg. M/S)multiple choice, choose the correct answer Under which of the following conditions would an enzyme fail to be accurately described by the M-M equation:1. kcat >> k1 or k-12. In the presence of a negative allosteric effector3. At low concentrations, the reaction is first order with respect to substrate concentration4. At high concentrations the reaction is zero order with respect to substrateThe Michaelis‑Menten equation models the hyperbolic relationship between [S] and the initial reaction rate ?0V0 for an enzyme‑catalyzed, single‑substrate reaction E+S↽−−⇀ES⟶E+PE+S↽−−⇀ES⟶E+P. The model can be more readily understood when comparing three conditions: [S]<<?m[S]<<Km, [S]=?m[S]=Km, and [S]>>?m[S]>>Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity ?0V0 where steady state conditions are assumed. [Etotal][Etotal] refers to the total enzyme concentration and [Efree][Efree] refers to the concentration of free enzyme.
- Many 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?a) Determine kcat (in units of sec-1) for a particular enzyme, given the following information: Vo = 144 mmol/min; [S] = 2 mM; Km = 0.5 mM; Enzyme Molecular weight = 40,000 mg/mmole; 8 mg of enzyme used in assay generating this data. b) In general, explain how the total enzyme concentration affects turnover number and Vmax?If an enzyme catalyzed reaction has a KM of 5mM and a Vmax of 60 nm/sec, the substrate concentration at 30 nM/sec is? Thank you.
- Choose the False statement about the parameters that quantitate enzyme catalysis A. V max is the velocity of enzymetic traction at high substrate concentration. B. V max is attained when all enzyme moleculesare present in the form of complex with substrate C. Rate of the reaction is different from the rate constant D. under the certain conditions, michaelis constant Km charatertizes potency of substrate binding. E rate constant is higher at larger substrate concentrationAn enzymatic reaction with KM = 4.4 x 10-5 M, is carried out in 400 μL of of solution containing 0.20 nmoles of enzyme. It is observed that Vmax = 6.6 x 10-3 M/s. What is the kcat value for the enzyme? (HINT: Keep an eye on the units)!!! a. 1.50 x 102 s-1 b. 7.56 x 10-5 min-1 c. 1.32 x 104 s-1 d. 3.3 x 106 s-1when saturated with substrate, an enzyme has a maximum initial rate of 110mumoles of substrate converted to product per second. At a substrate concentration of 100mu M, the same enzyme converts substrate to product at a rate of 0.010mmoles/ sec. Assuming that Michaelis - Menten kinetics are followed, calculate the reaction rate when substrate concentration is 2x10^-3M.