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BCH 119S Lecture Notes - Lecture 13: Oxyanion Hole, Acid Catalysis, Pepsin

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fuchsiareindeer237

22 Dec 2016

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Jeffrey Barrick

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Many enzymatic reactions involve reactions between a _______________ and an. The majority of reactions in metabolism use ___ as an ______ because it has a partial. Acid-base reactions depend on _______________ to act as bases and acids. Bases: his, asp, glu acids: his, lys. Acid catalysis usually happens through direct _________ to substrate to activate the reaction. An intermediate is formed by the covalent joining of the substrate and enzyme, this intermediate goes on to further reaction with another reactant or the starting enzyme strucutre is regenerated through reaction with water. As the ph increases or decreases, the ionziation states of the amino acid side groups changes. If critical side groups are in the active site, change in ionziation alter the strength of substrate binding/catalytic activity. A maximum in the ph dependence curve occurs if there are __________________. Two ionizable groups, or if there are two steps in a reaction involving his in alternating protonated and unprotonated states.

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Related Questions

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."