This reaction is catalyzed by adenylate kinase. How would the presence of this enzyme effect the DG°' and K'eq for the following Reaction? AMP + ATP ---> 2ADP no effect on Delta Go' and no effect on K'eq no effect on Delta Go' and increase K'eq increase Delta Go' and no effect on K'eq no effect on Delta Go' and decrease K'eq decrease Delta Go' and no effect on K'eq increase Delta Go' and decrease K'eq decrease Delta Go' and increase K'eq decrease Delta Go' and decrease K'eq increase Delta Go' and increase K'eq

How would you classify the enzyme that catalyzes the following reaction? -OOC. H Transferase Fumarate Hydrolase Ligase Isomerase Oxidoreductase H Lyase COO H₂O fumarase HRII!!!!! Hs OOC S-malate COO- OH

Which of the listed effects would be brought about by any enzyme catalyzing the following reaction? k1 S P where K'eg = [P]/[S] and AG°' = -RT In K'ea k2 (a) Decreased K'egi (b) increased k1; (c) increased K'ea; (d) increased AG*; (e) decreased AG*; (f) more negative AG°; (g) increased k2. Justify your answer using a reaction energy diagram. Problem 2. (a) The following data were obtained for an enzymatic reaction, in which the total enzyme concentration was 0.005 mM. Without plotting the data, can you estimate the approximate Km for this enzymatic reaction? How did you determine it?

Q11: For the following enzyme catalyzed reaction, indicate where the transition state occurs and whether you expect the enzyme to increase the transition towards the product? Product Reactant Reaction Progression Q12: For the following endergonic reaction, would you expect the presence of malate dehydrogenase to facilitate this reaction proceeding towards oxaloacetate, when both malate and oxaloacetate are present in equimolar amounts? ÇOO- fo0 NAD* COO- NADH + H* Но—с—Н 0=C CH2 CH2 malate CO" COO- dehydrogenase L-Malate Oxaloacetate AG'° = 29.7 kJ/mol AG Free Energy

na al Metalloproteases can contain a catalytic triad made up of: O D(H₂O)D O E(Ln*)S O None of the choices are correct O EKS ODHS

A medicinal chemist is trying to determine the mechanism of action of inhibitors she has synthesized. The relative change in KM and Vmax upon incubation of the targeted enzyme with each inhibitor is shown in the table below. Inhibitor A Inhibitor B Inhibitor C Using this data, the mechanism of action of Inhibitor B is: Competitive OTS‡ analog Non-competitive Mixed Inhibition КМарр- КМ 0 Uncompetitive app - Vmax <0 <0 0 Vmax

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What is the expected result if the enzyme monoamine oxidase is treated with the substrate analog named N,N-dimethylpropargylamine? H3C `N I CH3 N,N-dimethylpropargyl amine The product propargyl aldehyde (H-C=C-CH=O) will be formed and released. The product propargyl alcohol (H-CEC-CH₂-OH will be formed and released. The enzyme will be rapidly and covalently (irreversibly) inhibited. The enzyme will be reversibly and competitively inhibited in the presence of this substrate analog. a. b. monoamine oxidase C. d. MAO + O₂

Will an enzyme inhibited by EDTA, activate a water molecule for direct attack and hydrolysis? Will this enzyme use a covelent intermediate in its mechanism?

What subclass of enzymes catalyzes the following reaction? Select the single best answer. H H 0 | | H HN-C-CO, + 0,c-c-c-c-co, CH3 H H u་མང་ HH NH3 HC–C-CO, + 0,c-c———CO, HHH O Transaminase X $ O Kinase Decarboxylase O Protease