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In all enzymes the active site A. contains the substrate binding site. B. is contiguous with the substrate binding site in the primary sequence. C. lies in a region of the primary sequence distant from the substrate binding site. D. contains a metal ion as a prosthetic group. E. contains the amino acid side chains involved in catalyzing the reaction.

Short Answer

Expert verified
Answer: A. contains the substrate binding site and E. contains the amino acid side chains involved in catalyzing the reaction.

Step by step solution

01

Understand enzyme structure and active site function

In order to understand the properties of enzyme active sites, it's important to remember that enzymes are proteins with a specific 3-dimensional shape, which allows them to catalyze biochemical reactions. The active site of an enzyme is the region where the reaction occurs, and it is formed by a specific arrangement of amino acid residues.
02

Evaluate each statement for correctness

Now, let's analyze each statement and determine if it is true for the active site of all enzymes: A. contains the substrate binding site. B. is contiguous with the substrate binding site in the primary sequence. C. lies in a region of the primary sequence distant from the substrate binding site. D. contains a metal ion as a prosthetic group. E. contains the amino acid side chains involved in catalyzing the reaction.
03

Choose the correct statement

Evaluating each of the given statements, we can determine the correct answer: A. True. The active site contains the substrate binding site, where the enzyme interacts with its substrate. B. False. The active site may not be contiguous with the substrate binding site in the primary sequence. The correct formation of the active site depends on the folding of the protein, which brings the specific amino acid residues, possibly distant in the primary sequence, together in 3D space. C. False. The statement contradicts statement A, which is true. D. False. Although some enzymes have metal ions as prosthetic groups, it is not a universal feature of all enzymes. E. True. The active site consists of specific amino acid side chains that play a role in the catalytic reaction.
04

Final answer

Based on the analysis, there are two correct statements: A and E. Therefore, the correct answer is: A. contains the substrate binding site. E. contains the amino acid side chains involved in catalyzing the reaction.

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Most popular questions from this chapter

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.

Turnover number \(\left(k_{\mathrm{ca}}\right)\) A. is a ratio of the rate constants for the formation of ES and of product. B. has units of 1/time. C. is inversely related to how fast the reaction is. D. for a mutant enzyme can change without any change in the \(K_{m}\) of the reaction. E. has units of substrate concentration.

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.

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.

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. Organophosphate compounds inactivate the esterase by A. competitive inhibition. B. uncompetitive inhibition. C. noncompetitive inhibition. D. suicide inhibition. E. irreversible inhibition.

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