You are working on an enzyme that obeys standard Michaelis-Menten kinetics. What variable is the V, dependant on if the concentration of the substrate is substantially higher than the concentration of the enzyme? [S] O [ES] O [P] not enough information provided
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- The total concentration of enzyme in a reaction, [E], is made up of the concentration of enzyme bound to substrate, [ES], and the concentration of enzyme still free in solution, [Ef]. Similarly, the total amount of substrate is made up of [Sf] and [ES]. We can assume that the concentration of enzyme is much less than that of the substrate, [E] << [S]. Assuming the steady state condition and the relationships between [E], [Ef] and [ES], and similar ones for S, given in lectures, derive an expression for the saturation factor, , in terms of [S] and . (Note that [E] and [S] denote the total amounts of enzyme and substrate added to the reaction, respectively. You may assume that [S]>>[E].)Given the following enzyme kinetics data, determine the maximal velocity and the Michaelis constant of the enzyme. Show your solutionsIdris has successfully extracted enzymatic proteins from the fish viscera (intestines and stomach). After homogenization and centrifugation, he managed to pool the crude enzyme extract. He is characterizing the enzymes. Please help Idris by answering the followingquestions: (a) How do I run the experiment to find the kinetic properties of the enzyme, KMand Vmax? (b) The enzyme decreased in activity in the presence of NaCl. How do I find out if NaCl is a competitive or non-competitive inhibitor? Explain.
- If you multiplied enzyme concentration by kcat, think about what you would get. Which one of the following would be suitable units? unitless, because the numerator and denominator would both have the same units O s1 M-1 (s) x (M) O MsYou will perform the protocol below for the calf intestinal alkaline phosphatase (CIP) provided. For each reaction, your final enzyme concentration should be 10 nM CIP. Note: Enzymes purchased are typically labelled with their “units of activity” (U), as this relates to how much enzyme is needed to catalyze a reaction. The 100 nM CIP provided has approximately 3 U/mL and was diluted 1 in 1,000 from a 500 U/mL purchased enzyme. 1) Create a table (similar to the one below) to help you determine and keep track of what to add to each of the cuvettes in which your reactions will be measured. The five different concentrations of PNPP should be: 25, 50, 100, 200, 300 μM. Each reaction will be in a final volume of 1 mL and contain 10 nM alkaline phosphatase. Concentrations of stock solutions: 1.0 mM PNPP, 100 nM calf intestinal phosphataseMost of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten plots: (a) Lineweaver-Burk equation is a manipulation of the Michaelis-Menten equation. Give the equation and state why it is necessary. (b) Is high or low Vmax preferable for an enzyme reaction? Give reason.
- Most of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten plots: Give the Michaelis-Menten equation of an enzyme reaction and draw the Michaelis-Menten plot of [S] versus V0.Shown below is Lineweaver-Burk plot for an enzymatic reaction at different substrate concentrations in the presence and absence of an inhibitor. The enzyme concentration is identical in both reactions: 1/v (sec/mM) 4.5 4 3.5 3 2.5 2 1.5 1 0.5 0 0 0.2 0.4 y = 0.997 +3.01x (+1) 0.6 1/[S] (mM-¹) y = 0.09999 + 3.01x 0.8 (-1) 1 (c) What is the type of inhibition mechanism? A. competitive inhibition B. uncompetitive inhibition (substrate-dependent) C. mixed inhibition (a) Does this enzyme obey Michaelis-Menten kinetics? (yes or no) Explain: D. noncompetitive inhibition (substrate-independent) E. allosteric inhibition 1.2 (b) What are the apparent values of Vmax and KM for each experiment (with and without inhibitor)? d) If the concentration of the inhibitor is 0.1 mM, what is the value of KI and/or K'I (whichever is relevant)?The total concentration of enzyme in a reaction, [E], is made up of the concentration of enzyme bound to substrate, [ES], and the concentration of enzyme still free in solution, [Ef]. Similarly, the total amount of substrate is made up of [Sf] and [ES]. We can assume that the concentration of enzyme is much less than that of the substrate, [E] << [S] Explain why [S] >> [ES] Hence explain why [Sf] ~ [S]
- In enzyme kinetics, for the reversible with one complex mechanism, please provide complete proof that the rate equation is the equation below. The variables denoted with f indicates forward direction while the variables denoted with b indicate backward direction.An enzymes catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained in the image provided. Plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reactions and reaction with inhibitor. Use the same graph for both plots Michaelis–Menten kinetics Lineweaver–Burk plot Calculate the following: Km of enzyme in the reaction without inhibitor Km' of the enzyme in the reation with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction What kind of inhibitor was added to the enzyme catalyzed reaction? Explain your answer in terms of changes in Km and Vmax.How will a graph of reaction rate (V) vs. [substrate] for an allosteric enzyme differ from the hyperbolic plot characteristic of enzymes having Michaelis-Menten kinetics?