Which factor does NOT represent a barrier that prevents a reaction from taking place? substrate distortion the solvation shell of hydrogen-bonded water entropy of the molecules in solution standard free-energy change the need for proper alignment of catalytic functional groups on the enzyme
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- PREDICT In the following reaction series, which enzyme(s) is/are most likely to have an allosteric site to which the end product E binds? (a) enzyme 1 (b) enzyme 2 (c) enzyme 3 (d) enzyme 4 (e) enzymes 3 and 4Enzymes ................... the activation energy necessary for a reaction to take place. /A. IncreaseB. do not change C. Decrease D. are not involved withYou are observing an enzyme driven reaction. To the reaction mixture you add a chemical X which inhibits the reaction. If you add more substrate, the reaction rate approaches the Vmax of the uninhibited reaction. Furthermore, the structure of X is similar to the natural substrate. What kind of inhibitor is X?
- The statement that is not true about enzymes is...A. works optimally if it is in accordance with the required pHB. has active sites where enzyme reactions with substrates occurC. can work in all reaction temperature rangeD. can only work for certain reactionsE. is strongly influenced by reaction temperatureThe reason for the decrease in the rate of enzyme reaction as the temperature is increased beyond the optimal temperature isa. decrese in the kinetic energy of the reactantsb. decrease in activation energy of reactionc. denaturation of the enzyme d. inhibition of the enzymeDraw the structures of the amino acids whose side chainsmost commonly participate in catalytic mechanisms whenthey occur in the active sites of enzymes.
- When substrate [S] = Km, the velocity of an enzyme catalyzed reaction is about: * 0.1 Vmax. 0.2 Vmax. 0.5 Vmax. 0.9 VmaxThe active (catalytic) site of an enzyme contains the side chains of amino acid residues that areconserved because they participate in the protein’s catalytic activity. The bulk of the enzyme,however, is not part of the active site. A substantial amount of energy is required to synthesizeenzymes. Why are these molecules so large?enzyme e helps to catalyse the conversion of substrate s to product p which of the following parameters would change in response to increasing the concentration of E in this reaction - both the vmax and catalytic efficiency of enzyme e - the catalytic efficiency of enzyme e - both catalytic efficiency for E and affinity of enzyme e for substrate S - turnover number of enzymes - affinity of enzyme E for substrate S
- Enzyme function is often assisted by non-protein helpers or adjuncts, for catalytic activity. A ___ is an organic non-protein adjunct, and a ___ is an inorganic adjunct that may be involved in this function. A) coenzyme; cofactor B) substrate; cofactor C) reactant; substrate D) substrate; reactantAn allosterically regulated enzyme in the R state is unable to bind substrate at the activesite. TrueFalsean enzyme acts on a substrate X. The enzyme exists in four different forms, with different catalytic efficiencies. The table shows the kcatand KM values for each form of the enzyme. If the concentration of substrate X in a solution is 5 µM, which of the four forms of the enzyme is the most efficient? Form of Enzyme kcat (s-1) KM (µM) A 50 10 B 50 1 C 100 4 D 1000 100 a. Form A b. Form B c. Form D d. Form C