A. Bringing substrates closer together B. Breaking bonds in the enzyme to provide energy C. Modifying the local charge environment D. Forming transient covalent bonds between enzyme and substrate
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Biochemistry question:
Enzymes decrease the activation energy by NOT doing which of the following?
The answer choices are in the attached image. Please help . Thank you
Step by step
Solved in 2 steps
- a. How does an enzyme speed up the reaction of a substrate? b. After the products have formed, what happens to the enzyme?Match the definition to the term: v Choose... Temporary molecule that is formed when substrate attaches to the enzyme Substrate Product Compound that enters the reaction Substance that functions as a biological catalyst Enzyme Specific portion of the enzyme where the substrate attaches Result of enzyme reaction Active Site Enzyme-substrate complex Choose.... To catalyze a biochemical reaction, an enzyme typically dissociates into additional reactant molecules, thereby increasing the геaction ratе decomposes and releases energy to increase the number of successful collisions between reactant molecules binds temporarily to reactant molecules to lower the activation energy of the reaction drives the reaction to completion by consuming byproducts of the reaction CLEAR ALL
- on Which of the following statements about enzymes is CORRECT? Select one:* O A. Enzymes slow down chemical reactions so that they occur properly O B. Enyzmes are carbohydrates OC. Enzymes are specific for their substrate O D. Enzymes cannot be reused A substrate is: Select one: O A. A molecule that dissolves in a solvent O B. The molecule an enzyme acts on OC. A dissolving substance in a solution а a L O DMatch the following terms with the best definition. Enzyme Product Substrate Active Site A. A macromolecule serving as a catalyst. B. A material resulting from a chemical reaction. C. The reactant on which an enzyme works. D. Location on an enzyme where the reaction is catalyzed.IV. Label the following picture: Activation energy, with an enzyme, without an enzyme, product and substrate, time, energy (vyou do not have to label all the arrows)
- A. Which enzyme model involves the enzyme staying the same shape when the substrate binds to it? (lock and key, induced fit) B. If an inhibitor has similiar structure to that of a substrate, does it act as a competitive or noncompetitive inhibitor? C. What is the surface for an active site for an ezyme that binds the substrate to that site?1a.Sketch a graph that shows an enzyme that functions at an optional pH of b. which organ of the body does it likely to work at? 2. On the same graph from la, sketch another line/curve that shows what happen to the enzyme activity (in #1a) if a constant [ ] of inhibitors is added.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 temperature
- Classify the items as competitive or noncompetitive inhibitors for control of enzyme action. Bind to the allosteric site on the enzyme Not influenced by the concentration of substrate Resemble the substrate Do not resemble thhe substrate Bind to active site of the enzyme________ are always changed by participating in a reaction. a. Enzymes c. Reactants b. Cofactors d. CoenzymesWhich statements are true? The transition state is the highest free energy that a reaction reaches during its progress from reactants to products. Enzymes alter the free energy of the transition state but not its chemical nature. High affinity binding of substrate by enzymes alters the equilibrium between reactants (substrates) and products. High affinity binding of substrate by enzymes can impede reaching the transition state. Steric and electrostatic interactions between the enzyme and substrate usually disfavor the ground state of substrate and favor the formation of the transition state. If ∆G‡(catalyzed) is less positive than ∆G‡(uncatalyzed) then the enzyme is enhancing the rate of the reaction. Low affinity binding of substrate by the enzyme must always lead to a slower rate of reaction compared to the uncatalyzed rate. There is no barrier to substrate binding to an enzyme, only to the chemical step.
