The allosteric inhibitor of an 1 poi enzyme . Causes the enzyme to work faster O Binds to the active site O Participates in feedback regulation O Denatures the enzyme O None of these
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- Below is a segment of a cell's collection of biochemical pathways. M is a product of one series of these reactions. It is also a regulatory molecule. Look at the pathway below and indicate the position(s) at which M is most likely to act as a feedback inhibitor when its concentration gets too high.The effectiveness of allosteric effectors in regulating metabolic pathways is based on their ability to— interact with multiple substrate-binding sites on the target enzyme(s). interfere with competitive inhibitors. alter the concentration of the target enzyme(s). denature the target enzyme(s). change the conformation of the target enzyme(s).T/F Both competitive and noncompetitive inhibitors bind reversibly to an enzyme (E), thereby inhibiting its activity. These two kinds of inhibitors share the same site on the enzyme.
- The 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 enzymeAn allosterically regulated enzyme in the R state is unable to bind substrate at the activesite. TrueFalseKM is— a measure of substrate turnover. the rate at which the enzyme binds the substrate. an indicator of how strongly an enzyme binds its substrate. the rate constant for the reaction ES —> E + P. a measure of enzyme efficiency.
- A competitive inhibitor binds to the - active site of theenzyme - a substrate -N termininus of the enzyme -more than one of theseThe α-ketoglutarate dehydrogenase catalyzes the oxidation of α-ketoglutarate and in this reaction two electrons are stored in the form of: a. GTP b. cAMP c. NADH d. ATP e. FADH2Inhibitor X exerts which of the following effects on the above enzyme (lactase)? (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) pure non-competitive inhibition uncompetitive inhibition competitive inhibition all of the above none of the above
- The reason for the increase in the rate of an enzyme reaction when the temperature is increased isa. decrease in kinetic energy of reactantb. increase in kinetic energy of reactantc. increase in activation energy of reactiond. decrease in activation energy of reactionEnzymes can: make exothermic reactions into endothermic reactions. change the direction of a biochemical pathway. contain multiple subunits and be very complex (e.g., ATP synthase) be broken down into monosaccharide subunits. None of these.Exposure to radiation can ________________ an enzyme and change its shape to the point where it becomes inactive.a. catalyzeb. decomposec. synthesized. denature
