AсWanWWWGHEDEMAKam2IncreasingCEa-1 (no inhibitor)Slope #KY......."7-157a>c²=1 [no inhibitoriSlope R1019-19aver-Burk plots in this figure represent the activities of enzymes in the4-5n. 155BDMIN-a'/KM0.8-1/V>~- -1/K001m(app)d'Nmaxa=2a=1.51[S] per mMinhibitora=10Slope K The Lineweaver-Burk plots in this figure represent the activities of enzymes in theabsence and presence of different types of inhibitors. Which one represents theactivity of the enzyme in the presence and absence of a pure noncompetitiveinhibitor? (choose the one best answer).OAOBOcOD

The Lineweaver–Burk plot or the double reciprocal plot is a graphical representation of the…

Answered: A C -1/a K 1-a' Wen a'Nmax (a-1) Var…

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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2. The two diagrams to the right il- lustrate plots of steady-state ki- netic studies to characterize the in- FB 0.8- nH = 3.5 0.6- teraction of heart muscle phos- phofructokinase-1 with a non-phy- siological, synthetic substrate fruc- tose-6-sulfate. Because the kcat is smaller than that for the natural 0.4- 0.2- 10 μΜ 20 μΜ 48 μΜ substrate, higher enzyme concen- trations could be used. The results show the influence of increasing 2- 3.2- 0.4- concentrations of ATP on the initial -0.6- > velocity of the enzyme catalyzed reaction in the presence of no AMP (•), 10 µM AMP (•), 20 µM AMP (-), and 48 µM AMP (-). -0.8- 4 12 20 28 36 44 52 60 68 76 84 92 1.2 1.6 2.0 2.4 [AΤP (μΜ) log[ATP] (µM) (a) how ATP interacts with the enzyme in the case of no AMP (•). Write the reaction in words catalyzed by the enzyme for the alternative substrate, describe (b) with respect to the binding of AMP and ATP to the allosteric effector sites on the enzyme. Explain the physical significance of the…
2. The two diagrams to the right il- lustrate plots of steady-state ki- 5FA 0.8 netic studies to characterize the in- nH = 3.5 0.6- teraction of heart muscle phos- phofructokinase-1 with a non-phy- siological, synthetic substrate fruc- tose-6-sulfate. Because the kcat is 0.4- 0.2- smaller than that for the natural 10 μΜ 20 μΜ 48 μΜ substrate, higher enzyme concen- trations could be used. The results show the influence of increasing 0.2 0.4 concentrations of ATP on the initial -0.6- > velocity of the enzyme catalyzed reaction in the presence of no -0.8 4 12 20 28 36 44 52 60 68 76 84 92 1.2 2.0 2.4 AMP (•), 10 µM AMP (•), 20 µM AMP (-), and 48 µM AMP (). [ΑΤPΙ (μM) log[ATP] (µM) (а) how ATP interacts with the enzyme in the case of no AMP (•). Write the reaction in words catalyzed by the enzyme for the alternative substrate, describe (b) with respect to the binding of AMP and ATP to the allosteric effector sites on the enzyme. Explain the physical significance of the displacement of the…
2. The two diagrams to the right il- lustrate plots of steady-state ki- netic studies to characterize the in- teraction of heart muscle phos- phofructokinase-1 with a non-phy- siological, synthetic substrate fruc- tose-6-sulfate. Because the kcat is smaller than that for the natural 5 0.8- NH = 3.5 0.6- 0.4- 0.2- 10 μΜ 20 μΜ 48 µM substrate, higher enzyme concen- trations could be used. The results show the influence of increasing 2 0.2- 0.4- concentrations of ATP on the initial -0.6- > velocity of the enzyme catalyzed reaction in the presence of no -0.8F 4 12 20 28 36 44 52 60 68 76 84 92 .2 2.0 2.4 ΑMP () , 10 μΜ AMP (+ ) 20 μΜ AMP (-), and 48 µM AMP (-). [AΤP] (μΜ) log[ATP] (µM) (a) . Write the reaction in words catalyzed by the enzyme for the alternative substrate, describe how ATP interacts with the enzyme in the case of no AMP (•). (b) ! with respect to the binding of AMP and ATP to the allosteric effector sites on the enzyme. Explain the physical significance of the displacement…
PTP1B Substrate kcat Km kcat/Km UM 10-7 x (s-1 M) DADEPYLIPQQG DADAPYLIPQQG DAAEPYLIPQQG AAAAPYLIPQQG 44.6 + 1.8 39.8 + 0.32 3.9 + 0.9 13.7 + 0.46 1.1 + 0.25 0.29 + 0.01 35.3 + 0.22 6.6 ± 0.22 0.53 + 0.02 34.7 + 0.25 52.7 ± 0.7 0.066 + 0.001 (d) (. ) The units for kcat/KM in the above are given according to standard scientific notation. On this basis what is the value of this kinetic parameter for the DADEPYLIPQQG substrate?
The following amino acids that are often found inside globulin molecules are () A, Tyr B, Phe C, Asn D, Glu True of false 1. In the de novo synthesis of purine nucleotides and pyrimidine nucleotides, base rings are first synthesized and then corresponding nucleotides are formed with phosphoribose. () 2. Transcription is the process of transferring genetic information from DNA to RNA. DNA is synthesized under the catalysis of RNA polymerase, and the direction of synthesis is from the 5 'end to the 3' end. () 3. The change of protein conformation is caused by the breaking of covalent bonds within the molecule. () 4. In very high and very low pH solutions, amino acids exist mainly in non-ionic form. () 5. The active center of an enzyme usually consists of several amino acid residues adjacent to each other in the primary structure. ()
1E In terms of binding adenylate kinase, the Kd for ATP is ~50 M and the KI for GMP-PCP is ~50 nM. Explain how this may be possible in terms of molecular interactions. Name 4 different types of molecular interactions that may contribute to the increased binding affinity exhibited by GMP-PCP. Please help me in details
Below is a plot of Vo vs. [S] for a specific allosteric enzyme under different conditions. Which of the following best describes the graph? 4 (S] O Adding a positive modulator to #2 would result in curve 3. Curve 1 represents maximum inhibition. Line 4 is valid exclusively for curves 1 and 2. Adding a positive modulator to #1 would result in curve 2. O Curve 3 represents the effect of a negative modulator added to curve 2.
Using the substrate Ac-Ser-Gln-Asn-Tyr*Pro-Val-Val-NH2 and 10 nM HIV-1 protease, an inhibitor showed competitive inhibition, and a family of lines of 1/v vs. 1/[substrate] at changing-fixed concentrations of this inhibitor were as below: Slope (apparent Km/Vmax) (sec): 17,241 21,072 24,904 28,735 32,567 [Inhibitor] (M): 0 10 20 30 40 The Ki value for this inhibitor is _________________
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1/Vo 1/[S] with I without I with I with I 1/vo without I *-*- 1/vo without I 1/[S] 1/[S] 3. The above graphs are lineweaver-burk plots that demonstrate how inhibitors affect Michaelis Menten enzymes. For each graph identify the type of inhibition and explain how you determined that this enzyme is kinetically demonstrating this type of inhibition.
16. The overall reaction for the glycolysis reaction is C6H₁2O6(aq) + 2NAD+ (aq) + 2ADP³(aq) + 2HPO(aq) + 2H₂O(1) 2CH3COCO₂ (aq) + 2NADH(aq) + 2ATP4 (aq) + 2H3O+ (aq). What is A,G at chemical equilibrium?
The enzyme serine hydroxymethy ltransferase (SHMT) catalyses the conversion of serine into glycine. The fo llowing table gives the initial rates, vo, for the SHMT-catalysed reaction of the substrate serine at var ious concentratio ns of serine, lSI.[S]/(mmol dm-3) 10 20 30 40vo(μmol dm-3 s-1) 1.63 2.94 4.10 4.95Use the data to determine the values of the MichaelisMenten constant, the maximum velocity of the reaction, and the maximum turnover number of the enzyme.

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