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- According to the graph above, which enzyme would best function in a neutral pH?PMSF is a protease inhibitor that binds to enzyme active site. What is the possible mode of inhibition? Competitive O Irreversible O Non-competitive O MixedI once got non specific and another time i got uncompetitive and anothe time i got transition state analog please put the right answer
- | 2 3 I 4 I 5 I 6 I 7 Directions: Graph the data (line graph); label both axes. DATA TABLE 1 Temperature (°C) Enzyme Activity 10 10 20 15 30 25 40 45 50 35 60 20 Temperature (C) 1. According to the graph, what is the best (optimum) temperature for enzyme activity? Explain your reasoning. 2. What happens to the enzyme above the optimum temperature? 26°F F12 PrtSc Insert Delete F7 FO F9 Backspac 7 8. R P G K 近Both questionsWhich of the following are true when enzymes and substrate interact? kı E + S ● ES- -P k-1 the rate of the formation of ES = k1 [ES] the rate of the formation of the product = k2[ES] k1 [ES] = k-1 [ES] the rate of breakdown of ES to reform the enzyme and substrate = K-1[E][S] the rate of formation of ES = k1[E][S]
- In serine protease catalytic triad mechanism, the first and second products that leaves the active site are Carboxylic acid and amide respectively Amide and carboxylic acid respectively Ester and amide respectively Carboxylic acid and ester respectivelyIn the Lineweaver Burke plot shown below, which of the following is true? With inbito Wthout nhitor O Km is increasing. Vmax is decreasing Km is decreasing, Vmax is decreasing Km is increasing, Vmax is increasing Km is decreasing, Vmax is in QUESTION 35 As per the Enzyme commission classification, the tranferases belong to which of the following Class? O 2 O 4 O 3 Click Save and Submit to save and submit. Click Save All Answers to save all answers. 78 F Mostly cloudyAn enzyme facilitate catalysis by formation of ester bond with an alcoholic substrate. Which amino acid residues can facilitate such mechanism of catalysis? Select the correct response: Cys and Met Lys and Arg Ser and Tyr Glu and Asp
- Don't give Handwritten answerThe active site of an enzyme has a serine residue (shown below). Which of the following describes the substrate? H2N- CH- -OH OH polar active site, interacting atoms in substrate could be C-H Ononpolar active site, interacting atoms in substrate could be C-H polar active site, interacting atoms in substrate could be N-H nonpolar active site, interacting atoms in substrate could be N-HA plot of 1½5 venut VSL, Glld a Br-weaver Burk or double-reciprocal plot, is a useful tool for identifying the type of Madily each gaph by dragging the endpoints to show the various types of enzyme inhibition. What is the inhibition mechanism for the competitive inhibitor? The inhibisr binde cenly in recemyne The inhibitor bindx only lo cozyme- substrate complexe The inhibike binds tas bath free enzyme and enzyme xubxirale completes with identical binding axolante. The inhibikr binds to both free enzyme and cozyme substrate completes with different binding constants. What is the inhibition mechaniam for the uncompetitive inhibitor? The inhibitor binds only to free ENZYMES. The inhibitor bind is both tree enzyme and enzyme auhdraic compleaca with identical binding coulants. The inhibar binds only in enzyme ubrale complex.ca. The inhibir bindis in bath free enzyme and cxyme aubairale complicaca with dill crcnt binding costanix. LAST Nompumps dve shk with inbibus WHEY Pullie mechanism kot…