The hypothetical enzyme happyase catalyzes the reaction SAD+ HΑPPY At maximum rate, the enzyme converts 35,000 substrate molecules per minute. The initial reaction rate was measured to be vo = 10.2 μΜ -1 at enzyme and substrate concentrations of 18 nM and 43 µM, respectively. Calculate the catalytic efficiency of the enzyme in M-
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- when 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.(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?The kinetic data of an enzymatic reaction shown in the following table: a. Calculate the Km and Vmax of the reactionb. A competitive inhibitor is added to the reaction at a concentration of 5 μM, determine the new Vmax of the reaction and what happened to the Km value.
- Another member of your research group studied the kinetics of theGAPDH from the organism. They also determined if the GAPDH fromthe organism is also inhibited by the known inhibitor of GAPDH fromhumans. From the following data, determine the KM (Michaelis-Menten Constant) and the Vmax(maximum velocity) of the enzyme without and with the inhibitor.A hypothetical enzyme that follows Michaelis-Menten kinetics functions has a substrate concentration 50mM at 50% of Vmax. Find the substrate concentration when the velocity of reaction is equal to 75% of Vmax.The 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.
- Enzyme A catalyzes the reaction S → P and has a KM of 50 μM and a Vmax of 100 nM s–1. EnzymeB catalyzes the reaction S → Q and has a KM of 5 mM and a Vmax of 120 nM s–1. When 100 μM ofS is added to a mixture containing equal amounts of enzymes A and B, which reaction product (Por Q) will be more abundant after 1 minute of reaction?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?At what substrate concentration would an enzyme with a kcat of 25.0 s-1 and a KM of 3.5 mM operate at 25% of its maximal rate? How many reactions would the enzyme catalyze in 45 seconds when it is fully saturated with substate, assuming the enzyme has one active site?
- An enzyme-catalyzed reaction has a Km of 4 mM and a Vmax of 5x10-3 uM/s. What is the reaction velocity when the substrate concentration is: 5 mM 4 mMImagine you have an enzyme-catalyzed reaction where the enzyme has a Km of 2 mM and a Vmax of 10 nM/s. What is the reaction velocity if the substrate concentration is 5 mM? Work Needs to be Shown.Consider an enzyme-catalyzed reaction that follows Michaelis-Menten kinetics with KM =3.0 mmol·dm-3. What concentration of a competitive inhibitor with KI = 20 umol·dm-3 willreduce the rate of formation of product by 50% when the substrate concentration is held at 0.10mmol·dm-3.