Explain why structure 4 is a more potent inhibitor (lower IC50 value) than inhibitor 3 and why structure 5 is a much weaker inhibitor (higher IC50 value) than 3 and 4.
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- An inhibitor "I" is added to the enzymatic reaction at a concentration of 1.0 g/L. The data obtained are shown in the table below. No Inhibitor With Inhibitor [S](g/L) v ([E0] = 0,015 g/L) (g/L.min) v ([E0] = 0,015 g/L)(g/L.min) 40 2,28 1,818 20 1,74 1,316 13,4 1,4 0,986 10 1,18 0,76 8 1 0,62 (a)What kind of inhibition occurred?(b)Determine Ki (in g/L) for the inhibition of the previous exercise.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 stabilizationWhy does a pure noncompetitive inhibitor not changethe observed KM?
- For 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 0.142The 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.Inhibitor X exerts which of the following effects on the above enzyme (maltase)? (inhibitor X changes maltase activity to a V o of 0.10 mM per minute when [S] = 0.125 mM, and a V o of 0.25 mM per minute when [S] = 0.50 mM)
- What type of reversible inhibitor are sulfanomides? Competitive Uncompetitive Mixed/Noncompetitive None of the aboveRank these substrates in order of best inhibitor (highest binding affinity) to worst inhibitor (lowest binding affinity). Rank from highest binding affinity to lowest binding affinity. To rank items as equivalent, overlap them.How are affinity labels and suicide inhibitors different from group specific covalent modifieres (in terms of irreversible inhibition)?