2. The two diagrams to the right il-lustrate plots of steady-state ki-netic studies to characterize the in-FB0.8-nH =3.50.6-teraction of heart muscle phos-phofructokinase-1 with a non-phy-siological, synthetic substrate fruc-tose-6-sulfate. Because the kcat issmaller than that for the natural0.4-0.2-10 μΜ20 μΜ48 μΜsubstrate, higher enzyme concen-trations could be used. The resultsshow the influence of increasing2-3.2-0.4-concentrations of ATP on the initial-0.6->velocity of the enzyme catalyzedreaction in the presence of noAMP (•), 10 µM AMP (•), 20 µMAMP (-), and 48 µM AMP (-).-0.8-412202836445260687684921.21.62.02.4[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 displacement of the Hill plots to the right in panel B10 (µmoles/min/mg)A (A - "A) bo|

Phosphofructokinase-1 (PFK-1) is a rate limiting enzyme of the glycolytic pathway. PFK-1 catalyzes…

Answered: 2. The two diagrams to the right il-…

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

See similar textbooks

Similar questions

16c
The purified OXA-M290 enzyme can now be tested to determine which β-lactamase inhibitor is most effective. This inhibitor could be prescribed in combination with a β-lactam antibiotic to treat the infection caused by the E. coli KGH1 strain. Before testing inhibitors against OXA-M290, the kinetic activity of this enzyme must first be measured. The activity of OXA-M290 is measured using nitrocefin, a chromogenic β-lactam antibiotic. When nitrocefin is hydrolyzed by a β-lactamase, it changes from yellow to red in colour. The nitrocefin hydrolysis product has an extinction coefficient of 20,500 M-1 cm-1 at 486 nm. The hydrolysis of 60 μM nitrocefin by 1 nM OXA-M290 is monitored using a microplate reader. The absorbance of the wells in the plate is measured at 486 nm every 30 seconds. This experiment is carried out with three replicates, generating the following data: Time (min) Absorbance of Replicate 1 Absorbance of Replicate 2 Absorbance of Replicate 3 0.5 0.0984…
Predict the effect of each of the following amino acid substitutions on the KM and kcat of the enzyme-catalyzed reactions
Conversion of F1,6BP to GA3P and DHAP by aldolase is striking in that it is strongly unfavorable when all species are at 1 M (∆G°’ = +22.8 kJ/mol) but favorable when the species are at their physiological conditions (∆G = -5.9 kJ/mol). Based on ∆G°’ and ∆G of aldolase and TIM, and using a reasonable physiological value of 15 mM for the concentration of F1,6BP, calculate the concentrations of GA3P and DHAP under physiological conditions (use T = 37°C). Why is the reaction so much more favorable under these conditions than when all species are at 1 M?
Multivitamin B complex are essential compounds that are used as derivatives for compounds necessary for many metabolic activities. Give 3 vitamin B compounds and explain where and how they are used along the metabolic pathway.
PTP1B Substrate kcat Km. kcat/Km UM 10-7 x (s-1 M) DADEPYLIPQQG DADAPYLIPQQG DAAEP YLIPQQG 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 ) The units for kcat/KM in the above are given according to standard scientific notation. On this (d) ( basis what is the value of this kinetic parameter for the DADEPYLIPQQG substrate?
I have a question, what are these ''a'' means in this plot? Normally its 1/vmax or -1/km. Please be specific. Thank you.
distribution of Benzene in a 4-compartment PBK model after an exposure of 6h. Convert Berkeley Madonna code to Matlab. Note: The parameters in the table below are for a mouse model. 1a) What are the two type of products containing Benzene consumers were recently concerned about. Which of these two different type of products is likely more harmful? (hint: check news/reports and social media channels) 1b) Plot Jresp along with the concentrations of Benzene in blood, fat, non-fat and liver in a 24h window (pdf). Why is Jresp slightly decreasing within 6h of exposure? Here is the Berkeley Madonna code: {Top model} METHOD RK4 STARTTIME = 0 STOPTIME = 24 DT = 0.02 {Reservoirs Blood, Fat, NonFat and Liver} d/dt (NF) = + Jnf INIT NF = 0 d/dt (F) = + Jf INIT F = 0 d/dt (B) = - Jnf - Jf - Jl + Jresp INIT B = 0 d/dt (L) = + Jl - Jmetab INIT L = 0 {Flows} Jnf = Qnf*(Cb-Cnf) Jf = Qf*(Cb-Cfv) Jl = Ql*(Cb - Clv) Jmetab = vmax*Cl/(Km +…
A16 Compound A is the substrate for two enzymes, E, and E2, involved in the synthe- sis of an amino acid and an antibiotic, respectively. Their reaction rates, r, and r2, at an arbitrary concentration of E, and E, were measured at different concen- trations of A. However, the data were not labeled properly (shown in Table P.4.1), and the student who did the measurement needs help to sort out which dataset is for E,. Determine the K and rmax for both enzymes, with respect to the concen- tration of A. Which set of data is more likely to be for E, and which for E, and why? Table P.4.1 Reaction kinetics of a common substrate A for two enzymes. Concentration of 0.2 0.6 1.2 3. 4 5 8 9 12 15 A (mM) Reaction rate (r.) (mmol/L'min) Reaction rate (r,) (mmol/L'min) 3.33 4.29 4.62 4.76 4.84 4.88 4.9 4.92 4.94 4.95 4.96 4.97 0.09 0.23 0.38 0.5 0.6 0.67 0.71 0.75 0.8 0.82 0.86 0.80
Since all of the B-lactams that you have tested are susceptible to hydrolysis by PAESBL-1, the hospital will not be able to use a single 8-lactam to combat this P. aeruginosa isolate. You need to consider alternative strategies. From the following list, select all of the strategies that might successfully overcome the broad substrate specificity PAESBL-1: Check all that apply. using multiple B-lactams simultaneously (e.g., rather than treating with amoxicillin alone, treat with the three B-lactams: amoxicillin, cephalothin, and imipenem). O using a reversible inhibitor of PAESBL-1 instead of a 8-lactam. Treat future infections by O combining a reversible inhibitor of PAESBL-1 with one or more 8-lactams. O using an irreversible inhibitor of PaESBL-1 instead of a B-lactam. O combining an irreversible inhibitor of PAESBL-1 with one or more -lactams. O O O O
Within the body, CoQ 10 can be found in an oxidized or reduced form (also known as ubiquinone and ubiquinol). Describe how these structures differ and the biochemical role of coenzyme Q10.
As stated in the text, mammalian cells can become resistant to the lethal action of methotrexate by the selective survival of cells con- taining increases in dihydrofolate reductase gene copy number so that intracellular levels of the enzyme become very high. What other biochemical or genetic changes in cells could cause them to become resistant to methotrexate?

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS