Which of the following accurately characterizes enzyme active sites? (Pick two.)Active sites form the greatest number of favorable electrostatic interactions with a reaction'ssubstrates.Active sites form the greatest number of favorable electrostatic interactions with a reaction'stransition state.Competitive inhibitors that resemble an enzyme's substrate bind more tightly to the active site thanthose that resemble products or transition states.Competitive inhibitors that resemble an enzyme's transition state bind more tightly to the active sitethan those that resemble products or substrates.

he accurate characterizations of enzyme active sites are:Active sites form the greatest number of…

Answered: Which of the following accurately…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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enzymes are naturally occurring catalysts responsible for various biochemical reactions. Give a modern and recent application of an enzyme used in a biochemical reaction a - the commercial or trade name of the catalyst and enzyme. b - the properties of the catalyst and enzyme (e.g., shape, size, colour, price). c - the advantages and the disadvantages of the chosen catalyst and enzyme d - catalytic reaction (e.g., the reactant, product, reaction equation, phase, selectivity, promoter, catalyst support, operating temperature & pressure).
Which statement is false of a competitive inhibitor? It irreversibly inhibits the enzyme by chemically modifying a group at the active site. It competes with substrate for binding to the active site. Its effects can be overcome by increasing the substrate concentration. It often resembles the substrate for the enzyme it inhibits.
Amylase is an enzyme found in saliva that breaks down starch. The enzyme is currently functioning at its optimal pH of 7 and optimal temperature of 32oC. Which of the following could result in an increase in the reaction rate? Providing an environment with a pH of 9. Decreasing enzyme concentration. Placing the reactants in an environment at 10oC. Increasing substrate concentration.
The active site of an enzyme has a serine residue (shown below). Which of the following describes the substrate? H2N- CH- -OH OH polar active site, interacting atoms in substrate could be C-H Ononpolar active site, interacting atoms in substrate could be C-H polar active site, interacting atoms in substrate could be N-H nonpolar active site, interacting atoms in substrate could be N-H
You are given a tube containing 275 ng of purified PCR product (DNA) that is 1262 bp long. How many picomoles of PCR product are in the tube? The average molecular weight of a deoxynucleotide monophosphate is 328 g/mol.
Which of the following statements is false regarding an enzyme's ability to catalyse a reaction? an enzyme provides a reaction surface and a hydrophilic environment for the reaction to take place an enzyme binds reactants such that they are positioned correctly and can attain their transition-state configurations an enzyme allows the reaction to go through a more stable transition state than would normally be the case an enzyme can weaken bonds in reactants through the binding process
Background: In this experiment, the lab instructor created a catecholase enzyme solution using white potatoes. The potato was the source of enzymes and cofactors in the experiment, as potatoes have sufficient amounts of catecholase and, therefore, cofactors for catecholase. A chilled potato had the peel removed by the instructor and then was chopped into pieces. The potato is peeled so that the brown skin does not interfere with the brown color of the benzoquinone. If this were to occur, the absorbance would seem higher due to the brown potato skin in the solution. The potato was chopped so that the blender did not need to work as hard to break open the cells. The instructor then placed the chopped, peeled potato into a chilled blender. The blender is chilled as heat will speed up the rate of reaction. Cold (chilled) distilled water was then added to the potatoes. This was done to break open the cells of the potato. The catecholase and cofactors are inside the potato cells; water is…
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes
An inhibitor was added to an enzyme and the expected rate of the reaction was not detected and the substrate was not utilized at all. This inhibitor is (choose one answer only): Is un-competitive, meaning the inhibitor binds to a site near the active site. Is competitive, meaning the inhibitor binds directly to the same active site as the subtrate. Is non-competitive, meaning the inhibitor binds to site other than the active site as the subtrate. Is irreversible, meaning the inhibitor binds covalently to the enzyme keeping the enzyme inactive permanently.
In a reaction, if the substance concentration equals Km and concentration of inhibitor equals Ki, what would be the degree of inhibition generated by a competitive inhibitor?
You 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?
Which of the following are characteristics of catabolic metabolic pathways? (Choose all correct answers). Overall oxidation of initial substrates so redox reactions involve use of NAD+ as oxidizing agent, converted to NADH. Large initial substrates are broken down to smaller final products. Overall reduction of intial substrates so redox reactions involve use of NADPH as reducing agent, converted to NADP+. The pathways are overall exergonic (negative delta G). Net production of ATP as a result of the pathway. Essentially irreversible

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