Warning: foreach() argument must be of type array|object, bool given in /var/www/html/web/app/themes/studypress-core-theme/template-parts/header/mobile-offcanvas.php on line 20

An enzyme can facilitate the rate of a reaction by A. stabilizing the transition state. B. binding very tightly to the substrate. C. binding very tightly to the product. D. preventing the substrate from changing its ionic state. E. preventing the reaction from proceeding in the reverse direction.

Short Answer

Expert verified
Answer: Enzymes primarily facilitate the rate of reactions by stabilizing the transition state, which lowers the activation energy required for the reaction to proceed more easily and at a faster rate.

Step by step solution

01

Understanding Enzymes

Enzymes are biological catalysts, which means they assist in accelerating chemical reactions in living organisms without undergoing any permanent change themselves. They are essential for numerous cellular processes and help control metabolic rates in cells.
02

Identify Enzymatic Functions

Each of the given options describes different ways an enzyme may potentially facilitate the rate of a reaction. It's important to understand how enzymes function at a molecular level and how they interact with the substrate and products.
03

Analyzing Each Option

We will now examine each option: A. Stabilizing the transition state: The transition state is the high-energy, unstable state that occurs during a chemical reaction. Enzymes can lower the activation energy required for the reaction, primarily by stabilizing the transition state. This helps to make the reaction proceed more easily and at a faster rate. B. Binding very tightly to the substrate: While enzymes do bind to the substrate, binding too tightly could potentially inhibit the reaction. Enzymes need to bind to the substrate with the right amount of affinity to facilitate the reaction effectively. C. Binding very tightly to the product: Similar to option B, enzymes do bind to the product, but binding too tightly could inhibit the release of the product and thus slow down subsequent reactions. D. Preventing the substrate from changing its ionic state: The function of enzymes does not directly involve changing the ionic state of the substrate. Instead, enzymes catalyze reactions by bringing substrates together and positioning them in a favorable manner. E. Preventing the reaction from proceeding in the reverse direction: While enzymes can slightly influence the direction of a reaction, they don't actively prevent reactions from going in the reverse direction. In essence, enzymes work to facilitate reactions in both directions, depending on the particular cellular conditions.
04

Determine the Correct Answer

Based on the analysis provided above, we can conclude that Option A - Stabilizing the transition state - is the correct answer, as it most accurately depicts how enzymes facilitate the rate of reactions.

Unlock Step-by-Step Solutions & Ace Your Exams!

  • Full Textbook Solutions

    Get detailed explanations and key concepts

  • Unlimited Al creation

    Al flashcards, explanations, exams and more...

  • Ads-free access

    To over 500 millions flashcards

  • Money-back guarantee

    We refund you if you fail your exam.

Over 30 million students worldwide already upgrade their learning with Vaia!

One App. One Place for Learning.

All the tools & learning materials you need for study success - in one app.

Get started for free

Most popular questions from this chapter

When added to a reaction, a catalyst A. supplies the heats of formation. B. alters the equilibrium constant \(K_{\text {eq }}\) to favor the formation of products. C. increases the rate at which equilibrium is reached. D. changes the order of the reaction (e.g., first order to second order E. alters the \(\Delta G_{0}\) of the reaction.

A man of Japanese ancestry found himself to be experiencing severe flushing and a very rapid heart rate after consuming one alcoholic beverage. His companion, a Caucasian male, did not have the same symptoms even though he had finished his second drink. These physiological effects are related to the presence of acetaldehyde \(\left(\mathrm{CH}_{3} \mathrm{CH} \mathrm{O}\right)\) generated from the alcohol. Acetaldehyde is normally removed by the reaction of mitochondrial aldehyde dehydrogenase which catalyzes the reaction $$\mathrm{CH}_{3} \mathrm{CHO}+\mathrm{NAD}^{+} \leftrightharpoons \mathrm{CH}_{3} \mathrm{COO}^{-}+\mathrm{NADH}+\mathrm{H}^{+}.$$ Acetaldehyde dehydrogenase is a(n) A. oxidoreductase. B. transferase. C. hydrolase. D. lyase. E. ligase.

Metal cations may do all of the following except A. donate electron pairs to functional groups found in the primary structure of the enzyme protein. B. serve as Lewis acids in enzymes. C. participate in oxidation-reduction processes. D. stabilize the active conformation of an enzyme. E. form chelates with the substrate, with the chelate being the true substrate.

A research technician who is working with organophosphate compounds is required to have a weekly blood test for acetylcholine esterase activity. Typically, esterase activity remains relatively constant for some time and then abruptly drops to zero. If this happens, the technician must immediately stop working with the organophosphate compounds. The organophosphate compounds form stable esters with a critical serine hydroxyl group in the esterase. In the esterase, serine transfers a proton to a histidine residue. Which of the following is correct? A. Serine is acting as a general acid. B. Histidine is acting as a general acid. C. Serine and histidine form a covalent intermediate. D. The enzyme would be relatively insensitive to pH changes. E. Serine is acting as a transition stabilization catalyst.

Gout is a disease in which uric acid is high in blood and urine. One patient who excreted three times normal uric acid had very high blood levels of PRPP, an intermediate in biosynthesis of AMP and GMP, which are precursors of ATP and GTP. Degradation of these products produces uric acid. The patient's PRPP synthetase had normal \(K_{m}\) and \(V_{\max }\) values but was insensitive to regulation by the end products of the pathway (ATP, GTP). These are negative allosteric modifiers of PRPP synthetase. All of the following statements about allosteric effectors are correct except they A. may increase the enzyme's affinity for its substrate. B. may decrease the enzyme's affinity for its substrate. C. bind at the substrate binding site. D. cause a conformational change in the enzyme. E. can change either the \(K_{m}\) or the \(V_{\max }\) of the reaction.

See all solutions

Recommended explanations on Chemistry Textbooks

View all explanations

What do you think about this solution?

We value your feedback to improve our textbook solutions.

Study anywhere. Anytime. Across all devices.

Sign-up for free