BCH 119S Study Guide - Midterm Guide: Enzyme Kinetics, Enzyme Inhibitor, Turnover Number

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7 Mar 2017

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Chapter 6 enzymes: types of catalysis. B) low barrier h bond the h is shared equally between the original bond donor and acceptor enzymes increase reaction rates by bringing reacting groups into close proximity . Specifity pocket on the n terminus of the sissile peptide bond: protease inhibitors limit protease active and act as substrates but aren"t completely hydrolyzed. Vo = vmax[s]/km+[s: km = substrate concentration at with vo = vmax, kcat = how fast an enzyme acts once bound i) ii) iii) Kcat = vmax/[e] for simple reactions, kcat = k2. Vmax = rxn velocity when both substrates reach maximum saturation level other s-shaped graph: allosteric enxymes binding of one substrate affects catalytic activity of the. Negative effector for allosteric enzymes causes enzyme to switch to low activity mode (t) positive effector causes it to be allosterically more active ii) i) c)

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Ignore the circled answers, some of them are wrong but I don't know which. What are the correct answers for questions 1-5?

Which of the following is not correct concerning the action of enzymes 1. a. An enzyme lowers the Energy of the products and thus makes the reaction more favorable. A 1:1 Enzyme substrate complex (ES) must be formed before the enzyme can convert the substrate to product. e3 An enzyme speeds up both the forward reaction and the reverse reaction. d. Enzymes ean are stereoselective because the active site is 3-Dimensional and preferentially binds one enantiomer over the other. e. A mutational change of any residue in the active site ofan enzyme has a significant effect on the activity of the enzyme. Procaine Hydrochloride is a local anesthetic often used by dentists. The structure shown to the right represents procaine in the active site of the enzyme procaine esterase. Consider this substrate in the active site of the enzyme to answer the next three questions. Assume pH 7. 2. What type of residue might be located as a binding (recognition) residue at location #2? a. A polar noncharged residue that can form a Hydrogen bond. b. A negatively charged residue that can form an ion-ion interaction (salt bridge). c. A nonpolar residue that can be favorably involved in a hydrophobic interaction. A positively charged residue that can form a salt bridge. ea Any type of residue since there is no significant feature on the substrate to bind to. 3. Which of the following might be a likely binding residue at location #3? Asp residue a. Lys residue b. Ala residue e) he residue c. Met residue 4. Which of the following amino acid residue side chains would never be a catalytic residue in the active site of an enzyme? Glutamic acid a. Serine Histidine Phenylalanine b. c. Cysteine 5. Which of the following is correct conceming Michaelis Menten kinetics for enzyme catalyzed reactions? a. The V max is obtained when [S] is equal to 2 KM b. KM is equal to V occurs the when the enzyme is saturated with substrate The kinetic plot of velocity vs. [S] is linear. e. A useful approximation is "The larger the KM, the better the Eto S binding."

BCH 119S Study Guide - Midterm Guide: Enzyme Kinetics, Enzyme Inhibitor, Turnover Number

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