Туре of Reaction Catalyzed Classification 1. Oxidoreductases Oxidation-reduction reactions 2. Transferases Transfer of functional groups 3. Hydrolases Hydrolysis reactions 4. Lyases Group elimination to form double bonds 5. Isomerases Isomerization 6. Ligases Bond formation coupled with ATP hydrolysis (а) CO0 H-C-CH3 -H3C-C-H NH3 NH; (b) Ç00- H C=0 + + H* c=0 + 0=c=0 CH3
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Which type of enzyme (Table) catalyzes the following (given) reactions?
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- Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.Enzymes act by reducing the activation energy of areaction. Describe several ways in which this isaccomplished.What enzyme kinetic parameters are apparantly impacted by uncompetitive inhibitors? Vmax Km Both Km and Vmax Neither Km nor Vmax
- when saturated with substrate, an enzyme has a maximum initial rate of 110mumoles of substrate converted to product per second. At a substrate concentration of 100mu M, the same enzyme converts substrate to product at a rate of 0.010mmoles/ sec. Assuming that Michaelis - Menten kinetics are followed, calculate the reaction rate when substrate concentration is 2x10^-3M.The metabolism of alcohol pathway is showed in the figure characterized by biotransformation of: (Figure : Ethanol Metabolism Pathway - ADH : Alcohol dehydrogenases, ALDH: Aldehyde dehydrogenase ) (a) reaction phase I with two oxidations (b) reaction phase II with oxidation and sulfonation (c) reaction phase II with two hydrolysations (d) reaction phase II with two oxidations (e) reaction phase I with hydrolysis and oxidationCatalase breaks down hydrogen peroxide about107times faster than the uncatalyzed reaction. If the latter required one year, how much time would be needed by the catalasecatalyzed reaction?
- Mechanisms of catalysis: 2.5 Mechanism of chymotrypsin summary. These mechanisms involve several of the above-mentioned catalyses. In these summaries, do not just draw a diagram of the proposed mechanisms. It is more important to understand which reaction steps involve what kind of catalysis and how these help to reduce the activation energy needed for the reaction (e.g. a step in the reaction mechanism could be electrostatic catalysis to stabilise the transitions state)Whatis the main idea behind the conformational coupling mechanism for ATP synthase? Describe the three conformational states.6. Cycle of tricarboxylic acids (TCA):• importance for cellular metabolism;• intracellular localization of TCA enzymes;• sequence of TCA reactions;• TCA enzymes and coenzymes;• substrate phosphorylation reactions in TCA;• decarboxylation reactions in TCA;• enzymes and coenzymes in dihydrogen reactions in TCA;• mechanisms of regulation of TCA.
- A catalyst like lactase that assists in the metabolism od milk is best described as Group of answer choices homogeneous heterogeneous enzymatic non-truseable 7, What graph will demonstrate that experimental concentration data fit a second-order reaction? Group of answer choices ln[reactant] vs. time ln(k) vs. 1/T 1/[reactant] vs. time [reactant] vs. time ln(k) vs. EaMechanisms of catalysis: 2.6 Mechanism of lysozyme summary. These mechanisms involve several of the above-mentioned catalyses. In these summaries, do not just draw a diagram of the proposed mechanisms. It is more important to understand which reaction steps involve what kind of catalysis and how these help to reduce the activation energy needed for the reaction (e.g. a step in the reaction mechanism could be electrostatic catalysis to stabilise the transitions state)The comparison of the active site geometries of chymotrypsin and subtilisin under the assumption that their similarities have catalytic signifi cance has led to greater mechanistic understanding of both these enzymes. Discuss the validity of this strategy.