Q14: The turnover number is defined as the maximum number of substrate molecules that can be converted into product moleculesper unit time by an enzyme molecule. The concentration of enzyme active sites is not necessarily equal to the concentration ofenzyme molecules, because some enzyme molecules have more than one active site. If the enzyme molecule has one active site,the turnover number is given byturnover number =Rmax[E]tturnover number ==k2If the enzyme molecule has more than one active site, then [E], is multiplied by the number of active sites to determine itseffective concentration.Determine the value of the turnover number of the enzyme carbonic anhydrase, given that Rmax for carbonic anhydrase equals249 µmol · L¯¹. s¯¹ and [E], = 2.62 nmol · L-¹. Carbonic anhydrase has a single active site.Incorrect(Rmax is often written as Vmax)652.38 x10-38-1

We need all the quantities in each parameter to be in the same unit, if we are to use them in an…

Answered: The turnover number is defined as the…

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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Choose only the letter, no explanation needed. Enzyme activity is affected by a variety of factors. What factor causes the enzyme to denature if it becomes extremely high? * Choices: A. Water's Effect B. pH C. Temperature D. Activator's Effect An inhibitor binds to the enzyme's active site, preventing the substrate from binding to it. What conclusions can you make from this situation? * A. No reaction occurred B. Non-competitive inhibition occurred C. Enzyme activity occurred D. Competitive inhibition occurred Each enzyme is very selective when it comes to its substrate. What can you conclude from this statement? * A. Any substrate can bind to the active site. B. Enzymes are used up in the reaction. C. Only a specific substrate can bind to the active site. D. Enzymes break down when not used. Lock : Key :: Active Site : _____________________________ * A. Substrate B. Active Site C. Coenzyme D. Cofactor Enzymes only speed up biological functions, so they are NOT used up in the…
Which of the following is NOT true about enzymes? Enzyme inhibitors interact reversibly or irreversibly with an enzyme to alter its Km and /or Vmax values. Enzymes typically act under milder conditions of temperature and pH than non-enzyme chemical catalysts. Zymogens are the inactive precursors of enzyme. Nucleophilic groups can catalyze reactions through the transient formation of covalent bonds with the substrate. Transition state stabilization can significantly increase the activation energy for a reaction.
When the enzyme hexokinase binds to glucose and ATP it undergoes a conformational change. All of the following are true about this enzyme-substrate binding EXCEPT: The active site changes shape so that it binds more tightly to the substrates The substrates are optimally positioned for the reaction to occur The substrates become contorted or strained, which increases their reactivity The activation energy of the reaction increases
The enzyme activity is: A. to The number of grams of substrate that react to form product, per mole of enzyme, per unit of time. b. The number of moles of substrate that react to form product, per gram of enzyme, per unit time. c. The number of moles of substrate that react to form product, per mole of enzyme, per unit time d. The number of grams of substrate that react to form product, per gram of enzyme, per unit of time.
Which of the following describe what enzymes such as Chymotrysin accomplish to allow products to form and be released by the enzyme active site? Group of answer choices catalyze chemical eactions that are thermodynamically unfavorable to occur establish a more stable transition state at a higher energy level to perform a catalysis reaction redce the chemical energy held within a chemical bond modify chemical structure of a substrate to "fit" within the active site
"An enzyme reaches a maximum rate at high substrate concentration because it has a fixed number of active sites where substrate binds", is true or false.
Indicate whether each of the following statements about an enzyme active site is true or false. It is the location where substrate molecules are produced. It always has a fixed, rigid geometry. It always has a geometrical shape exactly complementary to that of substrate. It always accommodates several structurally related substrates. It is the location where substrate molecules are converted to product molecules. It always has a shape that has a degree of flexibility to it. It always accommodates only one specific substrate.
Indicate whether each of the following statements about an enzyme active site is true or false. a. It is the location where substrate molecules are produced. b. It always has a fixed, rigid geometry. c. It always has a geometrical shape exactly complementary to that of substrate. d. It always accomodates several structurally related substrates. e. It is the location where substrate molecules are converted to product molecules. f. It always has a shape that has a degree of flexibility to it. g. it always accomodates only one specific substrate.
Identify the type of enzyme inhibition each of the following inhibitor characteristics is associated with: 1. An inhibitor that decreases enzyme activity by binding to a site on the enzyme other that the active site. 2. An inhibitor that inactivates enzymes by forming a strong covalent bond of the enzyme acitve site.
Which of the following does NOT describe enzyme-catalyzed rate acceleration derived from the binding of substrate to enzyme a. repulsion between like charges b. substrate proximity and orientation c. reduction of entropy (increased order) d. desolvation of the substrate by the enzyme active site e. introduction of strain in bonds that need to break
an enzyme acts on a substrate X. The enzyme exists in four different forms, with different catalytic efficiencies. The table shows the kcatand KM values for each form of the enzyme. If the concentration of substrate X in a solution is 5 µM, which of the four forms of the enzyme is the most efficient? Form of Enzyme kcat (s-1) KM (µM) A 50 10 B 50 1 C 100 4 D 1000 100 a. Form A b. Form B c. Form D d. Form C
The concept of “induced fit” refers to the fact that: a. enzyme specificity is induced by enzyme-substrate binding. b. enzyme-substrate binding induces an increase in the reaction entropy, thereby catalyzing the reaction. c. enzyme-substrate binding induces movement along the reaction coordinate to the transition state. d. substrate binding may induce a conformational change in the enzyme, which then brings catalytic groups into proper orientation. e. when a substrate binds to an enzyme, the enzyme induces a loss of water (desolvation) from the substrate.

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