Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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- 1. The enzyme you are studying uses the substrate pictured at right. An inhibitor box in the freezer contains two tubes labeled Inhibitor #1 and Inhibitor #2, along with the structures of the compounds contained within them and their respective Ki. Which one is more likely to be the non-competitive inhibitor? Inhibitor #1 K₁ = 10 μM m CH₂OH OH -0, $ OH OH Inhibitor #2 K₁ = 50 μM Briefly Justify: OH CH₂OH OH OH OH Substratearrow_forward45. Which of the following is/are true? (MARK ALL THAT APPLY) Group of answer choices Enzymes lower the activation energy of the reaction Enzymes bind more strongly to the substrates than the transition state of the reaction Enzymes alter the standard free energy of the reaction. Enzymes force reactions to proceed in only one direction. Enzymes alter the equilibrium of the reaction. PreviousNextarrow_forward3. At what substrate concentration would an enzyme with a keat of 25.0 s¹ 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?arrow_forward
- The V vs. [S] plot for allosteric enzymes often has a ______ shape. hyperbolic sigmoidal cycloidal serpentine parabolicarrow_forward37. Consider the following energy diagram for an enzyme-catalyzed reaction. D B A C E G Which step is probably the slowest? a. A →B →C b. C D E c. E F G d. G H Iarrow_forward19. What is the optimal pH for catalase? Why do you think it becomes less effective at high or low pH? 20. Can you think of anywhere in the human body where enzymes would work BEST at a high pH? Please give an example and draw what that graph might look like. 21. What is the optimal temperature for catalase? Why do you think it becomes less effective at high or low temperatures? 22. Can you think of any organisms that would have enzymes specifically adapted to extreme low or high temperatures and would therefore function best at a different part of the graph? Please give an example and draw what that graph might look like.arrow_forward
- An enzyme mechanism generates a positive charge in the transition state. Stabilization of the transition state would be increased by the presence of [Select] destabilization would be increased by the presence of [Select ] Q Search **** do 4arrow_forwardF5arrow_forward6. What is a glycosyltransferase? Choose all that apply Group of answer choices Catalyzes the formation of a bond between a sugar and an amino acid An enzyme that cleaves a glycosidic bond An enzyme that catalyzes the formation of a glycosidic bond An enzyme that transfers nucleotide-sugars from the cytoplasm 7. Which statement(s) is/are true about inverting and retaining glycosyltransferases? a. Inverting glycosyltransferase catalyzes the epimerization of a sugar b. Inverting glycosyltransferase alters the anomeric configuration of the glycosyl donor c. Retaining glycosyltransferase never preserves the anomeric configuration of the glycosyl donor d. Inverting glycosyltransferase switch the order of acceptor and donor. e. An SN1 reaction mechanism results in exclusive retention of stereochemistry of the anomeric carbonarrow_forward
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