Give a complete and well descriptive definition of the following: 1.1 Enzyme catalysis 1.2 Co-enzyme 1.3 Negative heterotropic co-cooperativit
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Give a complete and well
descriptive definition of the following:
1.1 Enzyme catalysis
1.2 Co-enzyme
1.3 Negative heterotropic co-cooperativit
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Solved in 2 steps
- Mechanisms of catalysis : 2.1 Acid-base catalysis summary + example 2.2 Electrostatic catalysis summary + example 2.3 Covalent catalysis summary + example 2.4 Enzymen catalysis summary 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) 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.…An enzymes catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained in the image provided. Plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reactions and reaction with inhibitor. Use the same graph for both plots Michaelis–Menten kinetics Lineweaver–Burk plot Calculate the following: Km of enzyme in the reaction without inhibitor Km' of the enzyme in the reation with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction What kind of inhibitor was added to the enzyme catalyzed reaction? Explain your answer in terms of changes in Km and Vmax.The protein catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide:2 H2O2 (aq) → 2 H2O (l) + O2 (g)and has a Michaelis-Menten constant of 25 × 10-3 mol·dm-3 and a turnover number of 4.0×107s-1.The total enzyme concentration is 0.016×10-6 mol·dm-3 and the initial substrate concentration is4.32×10-6 mol·dm-3 Calculate the maximum reaction rate (????) for this enzyme, and the initial rateof this reaction. Note that catalase has a single active site.
- An enzymes catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained in the image provided. Plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reactions and reaction with inhibitor. Use the same graph for both plots Calculate the following: Km of enzyme in the reaction without inhibitor Km' of the enzyme in the reation with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction What kind of inhibitor was added to the enzyme catalyzed reaction? Explain your answer in terms of changes in Km and Vmax.List three effects of macromolecular crowding on the properties of enzymes and the reactions they catalyze.Discuss how the equation for enzymatic reaction (given below) was demonstrated in the experimental results in Table 1. Use the appropriate color codes (-), (+), (++), (+++) to describe the expected results in Table 1 Table 1. Enzyme Action MIXTURE ENZYME ACTIVITY Water + catechol (tt A) Enzyme + catechol (tt B) Water + enzyme (tt C)
- Please note the following Lineweaver-Burk plot for the enzyme Virbraniumase reacting with a substrate: -0.4 . 1/V 5 4 3 2 -0.2 0 0.2 y = 5.2781x + 1.3338 R² = 0.9967 0.4 0.6 0.8 1/[S] 1 Based on the information provided, what is the Vmax for this reaction?Which of the following statements are true for BOTH the "transition state" and an "intermediate" of reaction? (This is a multi-select question, select all that apply.). Both are only observed in enzyme-catalyzed reactions. Both can be converted to product(s) or might decompose back to the reactant(s). Neither are part of the "net equation" for the reaction. Both contain covalent bonds are in the process of breaking and/or forming. Both are part of every chemical reaction. (i.e. the mechanisms of all chemical reactions, whether enzyme catalyzed or not, will have involve both a transition state and an intermediate).The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) [S] (uM) Inhibitor + Inhibitor 1.3 2.50 0.62 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What class of reversible enzyme inhibitor is being employed in this enzyme reaction?
- The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose 6-phosphate. After the reactants and products were mixed and allowed to reach equilibrium at 25°C, the concentration of glucose 1-phosphate was 4.5 mM and that of glucose 6-phosphate was 86 mM. Calculate Keq' and AG for this reaction. The reaction coordinate diagram for an enzyme-catalyzed reaction is shown below. How many transition states and intermediates are in the reaction? Is the reaction thermodynamically favorable? Which step is the rate-determining step of the reaction? G Reaction coordinateFor each pair of biomolecules, identify the type of reaction (oxidation‑reduction, hydrolysis, isomerization, group transfer, or internal rearrangement) required to convert the first molecule to the second. In each case, indicate the general type of enzyme and cofactor(s) or reactants required, and any other products that would result A(n) (hydrolysis, oxidation reduction, group transfer, isomerization, internal rearrangment) reaction converts glycylalanine to glycine and alanine. This reaction requires (NAD+ and a peptidase or protease, ADP and a phosphatase, H2O and a phosphatase, H2O and a peptidase or a protease)For each pair of biomolecules, identify the type of reaction (oxidation‑reduction, hydrolysis, isomerization, group transfer, or internal rearrangement) required to convert the first molecule to the second. In each case, indicate the general type of enzyme and cofactor(s) or reactants required, and any other products that would result A(n) (hydrolysis, oxidation reduction, group transfer, isomerization, internal rearrangment) reaction converts glycerol to dihydroxyacetone. This reaction requires (NADH and a dehydrogenase, NADH and a phosphatase, NAD+ and a dehydrogenase, NAD+ and a phosphatase) and also produces (NAD+ and H+, NAD+ and H2O, NADH and H+, NADH and H2O).