C7 Q2: Determine which of the graphs represents the relationship of reaction rate (velocity) and substrate concentration when theenzyme concentration of the non-allosteric enzyme is constant.Reaction velocitySubstrate concentrationDetermine how reaction rate (velocity) varies with substrate concentration.Rate increasesRate decreasesAnswer BankAnswer BankRate is unchanged Determine how reaction rate (velocity) varies with substrate concentration.Rate increasesAdditional substrate is added when substrate concentration is low.Rate decreasesAnswer BankRate is unchangedSubstrate is added when enzyme is saturated with substrate.Additional substrate is added when substrate concentration is high but is not yet saturating.

Enzyme is usually a protein that catalyzes a reaction by increasing the rate or the velocity of the…

Answered: Substrate concentration how reaction…

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

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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
Evaluate the following statements concerning enzyme kinetics. Which one of the statements is false? a. Enzyme saturation fluctuates. b. In an uninhibited enzymatic reaction system, adding an excess of substrate will increase the reaction velocity beyond Vmax. c. The Vmax of an enzyme kinetics graph represents the point at which the enzyme is saturated with substrate. d. Non-competitive inhibition of an enzymatic reaction can be overcome by adding more unaltered enzyme. e. The activation energy of a reaction can be reduced by the presence of an enzyme.
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.
Briefly describe the series of events must take place between the binding of substrate to enzyme, and the re-appearance of free enzyme and product.
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
Consider an enzyme-catalyzed reaction that follows Michaelis-Menten kinetics with KM =3.0 mmol·dm-3. What concentration of a competitive inhibitor with KI = 20 umol·dm-3 willreduce the rate of formation of product by 50% when the substrate concentration is held at 0.10mmol·dm-3.
A hypothetical enzyme that follows Michaelis-Menten kinetics functions has a substrate concentration 50mM at 50% of Vmax. Find the substrate concentration when the velocity of reaction is equal to 75% of Vmax.
in the concerted model of enzyme action when the L ratio (T/R) is 10,000 the velocity vs. Substrate plot results in what type of a curve.
Discuss the different factors affecting the rate of an enzymatic reaction. Explain enzyme kinetics including zero-order and first-order kinetics.
Graph a double reciprocal plot that satisfy the following: a. Michaelis-Menten kinetics enzyme, b. an inhibitor that binds only free enzyme (competitive), c. an inhibitor that binds only enzyme-substrate complex.
Which of the following statements are true about the relationships of [S], KM, and Vmax? (Choose all that are true) As the [S] is increased, vo approaches the limiting value, Vmax KM = Vmax/2 The rate of product formed, vo, is at Vmax when [S] <<< KM KM and Vmax assist in finding the rate of the enzyme catalyzed reaction only if the reaction is considered irreversible.
Paste your Microsoft Excel Graph of the kinetic analysis. Compute for Vmax and Km values and identify the mode of enzyme inhibition involved.

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Substrate concentration how reaction rate (velocity) varies with substrate concentration. Rate increases Answer Bank Rate decreases Rate is unchanged