Given the active site diagram and reaction mechanism, indicate the mechanism of irreversible inhibition for the inhibitor provided.
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I once got non specific and another time i got uncompetitive and anothe time i got transition state analog please put the right answer
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- What enzyme kinetic parameters are apparantly impacted by uncompetitive inhibitors? Vmax Km Both Km and Vmax Neither Km nor VmaxSuppose that the data below are obtained for an enzyme catalyzed reaction in the presence and absence of inhibitor Y. [S] (mM) V (mmol/mL*min) Without Y With Y 0.2 5.0 2.0 0.4 7.5 3.0 1.8 10.0 4.0 1.0 10.7 4.3 2.0 12.5 5.0 4.0 13.6 5.5 a.) Determine the type of inhibition that has occurred b.) Does inhibitor Y combine with E, with ES or with both? Explain c.) Calculate the inhibitor constant, Ki, for substance Y, assuming that the final concentration of Y in the reaction mixture was 0.3mMIn the scheme for enzymatic catalysed reaction proposed by Michaelis and Menten, the steps involve reversible formation of enzyme-substrate (ES) complex followed by conversion of the complex to the product (P). a) Derive the rate equation for enzymatic process. State an assumption made in this derivation. Terbitkan persamaan kadar tindak balas bagi proses enzim. b) By showing appropriate reaction mechanisms and rate equations, explain how enzyme catalytic reactions may be affected by competitive inhibition
- What are the measures to inhibit the Maillard reaction in undesirable situations. please explain detailedFor the following aspartase reaction in the presence of the inhibitor hydroxymethylaspartate, determine Km and whether the inhibition is competitive or noncompetitive. You have to plot thegraph on the graph paper and also by using excel.[S] V, No Inhibitor V, Inhibitor Present(molarity) (arbitrary units) (same arbitrary units) 1 x 10-4 0.026 0.0105 x 10-4 0.092 0.0401.5 x 10-3 0.136 0.0862.5 x 10-3 0.150 0.1205 x 10-3 0.165 0.142when 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.
- The enzyme β-methylaspartase catalyzes the deamination of β-methylaspartate. For this aspartate reaction in the presence of the inhibitor hydroxymethylaspartate (3.8 M), determine KM and whether the inhibition is competitive or noncompetitive (KI = 1.0 M). [S], M V w/o inhibitor, M/s V w/ inhibitor, M/s 1x10-4 0.0259 0.0098 5x10-4 0.0917 0.040 1.5x10-3 0.136 0.086 2.5x10-3 0.150 0.120 5x10-3 0.165 0.142 In the ABSENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= __________ (1[S])(1[S]) + __________, and the KM is __________ M. In the PRESENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= ____________ (1[S])(1[S]) + ___________, and the KM is ___________ M. The type of inhibition is ____________. Round-off all answers to two (2) significant figures.The following data was obtained during kinetic analysis of an enzyme with and without an inhibitor. Substrate concentration (mM) Reaction rate without inhibitor (µM/s) Reaction rate with inhibitor (µM/s) 10 28 12 20 50 23 40 83 42 60 107 58 100 139 83 200 179 125 300 197 150 400 209 167 560 227 197 How do you calculate the KM for the enzyme in the absence of an inhibitor. And how do you calculate kcat with the given enzymatic concentration of 5 µM.Where do each of these 5 main themes occur in the chymotrypsin mechanism? 1) substrate specificity 2) induced fit 3) covalent catalysis 4) acid/base catalysis 5) transition state stabilization
- Lysozyme residues Asp 101 and Arg 114 are required for effi cient catalysis, although they are located at some distance from the active site Glu 35 and Asp 52. Substituting Ala for either Asp 101 or Arg 114 does not signifi cantly alter the enzyme’s tertiary structure, but it signifi cantly reduces its catalytic activity. Explain.What enzyme kinetic parameters are apparently impacted by competitive inhibitors? Vmax Km Both Km and Vmax Neither Km nor VmaxWhy does a pure noncompetitive inhibitor not changethe observed KM?