Match the following catalytic strategies with their example. Place a Letter on the picture. There are only two examples given. CH,OH CH,OH CH,OH CH,OH O H O H OH H. OH OH +HO → OH HON OH HO H. HO OH OH A. Oxidoreducatase OH OH OH OH B. Transferase C. Hydrolase D. Lyase NH3 E. Isomerase F. Ligase R-CH-COO Ooc-CH2-CH2-C-COO
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- Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.Look at the synthesis of citryl CoA by citrate synthase in the figure. Which of the 4 general catalytic mechanisms are present? Catalysis by approximation Covalent Catalysis General Acid-Base Catalysis Metal Ion CatalysisWhich of the following describe what enzymes such as Chymotrysin accomplish to allow products to form and be released by the enzyme active site? Group of answer choices catalyze chemical eactions that are thermodynamically unfavorable to occur establish a more stable transition state at a higher energy level to perform a catalysis reaction redce the chemical energy held within a chemical bond modify chemical structure of a substrate to "fit" within the active site
- Given the reaction below, what major class of enzyme will catalyze such reaction? Select the correct response: Isomerase Ligase Lyase Transferase Oxido-reductase • HydrolaseWhich of the following best indicates a reason why Hisneeds to be a good proton donor (not acceptor) in the catalytic triad mechanism? So that it can create the alkoxide ion. So that it can create a hydroxyde ion. None of the other options is suitable because His's only role is to be a proton acceptor. So that the first product forms and leaves with the correct number of H's. So that it can stabilize the transition state.How to differentiate the following simply by seeing the reaction: a. oxidoreductase b. transferase c. hydrolase d. lyase e. isomerase f. ligase
- Which of the following statements is true for the shown reaction? The reaction can occur in both cytosol and mitochondria Under starved conditions, the reaction becomes reversible to allow the synthesis of ketonebodies The reaction requires FMN as a cofactor Increase in NADH stimulates the reaction None of the aboveA(n) _________ reaction converts glycylalanine to glycine and alanine. This reaction requires __________. Blank 1 options- Oxidation-reduction Hydrolysis Isomerization Group transfer Internal rearrangement Blank 2 options- H2O and apeptidase or a protease H2O and a phosphatase ADP and a phosphatase NAD+ and a peptidase or a proteaseWhich of the following best explains why enzyme catalysis is affected by a change in pH? A. Change in pH alters ionization states of serine in the active site involved in nucleophilic catalysis B. The ionization states of his, asp and glu involved in acid/base catalysis are altered with change in pH C. Change in pH alters ionization states of contact amino acids in the active site D. All enzymes have optimum pH
- Which of the following statements is true for the shown reaction? Substrate level phosphorylation occurs during the reaction Phosphoryl transfer occurs during the reaction Both A and B Neither A nor BFor each of the statements below about the dUTPase enzyme, mark whether it is true or false. If it is false, change the language to make the statement true. _______If the dUTPase enzyme is the rate determining step in a larger metabolic pathway, the reaction likely lies near to equilibrium and is irreversible. _______For the dUTPase reaction, it is not likely that DG’ = DG°’ _______ dUTPase has a higher affinity for its substrate than for its product, but both of these are higher than the affinity for the transition state _______Kinetic analysis of dUTPase using Michaelis-Menten methods assumes that the formation of the E*S complex has a large negative value for DGWhen the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Zymogen activation Covalent modification Competitive inhibition Allosteric activation Allosteric inhibition