The effect of temperature on the hydrolysis of lactose by a ß-galactosidase is shownbelow in Table 1. The temperature coefficient, Q10 is the factor by which the rateincreases by raising the temperature 10°C. The universal gas constant, R is 8.314J/mol.K.(a)(b)Table 1: Data of Vmax over temperatureT (°C)2030354045Vmax (umoles/min.mg protein)4.508.6511.8015.9621.36Plot the graph of In Vm vs 1/T using any spreadsheet software (include allappropriate labels and equation).Calculate the activation energy Ea and temperature coefficient Q10.

First we need to do some conversions. The temperature should be converted to kelvin (K) and the Vmax…

Answered: The effect of temperature on 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

See similar textbooks

Similar questions

Given that the AG" values for the hydrolysis of glucose 1-phosphate and glucose 6-phosphate are approximately -21 kJ/mol and –14 kJ/mol, respectively, which statement is true regarding the isomerization shown? glucose 1-phosphate → glucose 6-phosphate O The reaction can likely proceed in either direction and will therefore depend on the concentrations of glucose 1-phosphate and glucose 6-phosphate. O Only the anabolic direction will occur because the free energy change is positive. O The reaction will proceed in both directions simultaneously. This reaction can only proceed in one direction and must be the rate limiting reaction for this point in metabolism.
The conversion of dihyroxyacetone phosphate to glyceraldehyde 3-phosphate, catalyzed by triose phosphate isomerase, has an equilibrium constant of Keq’ = 0.0475. Calculate the standard free-energy change for this reaction at 25ºC and pH 7.0.
Following is a Dixon plot for PNPP inhibition by inorganic phosphates. What answer choice shows the correct combination of the mode of inhibition and Ki of the EI complex? - Mixed inhibition, Ki= -21.2 uM - Mixed inhibition, Ki= 1/16.5 uM - Competitive inhibition, Ki= 16.5 uM - Competitive inhibition , Ki= -1/16.5 uM - None of the above
If the enzyme lactase has a Vo of 0.40 mM per minute when [S] = 1.25 mM, and a Vo of 1.0 mM per minute when [S] = 5.0 mM, what is its Vmax? Calculate the Km of the above enzyme. Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the above enzyme.
(b) You are investigating the effects of several agents on the activity of alcohol dehydrogenase. The enzyme activity data are shown in the table below. Construct a [substrate] vs. activity plot and a double-reciprocal plot for this enzyme. Be sure to label all axes. Determine the Vmax and KM for AD from the graphs in each type of plot. AD activity (nM/min) AD activity + agent A (nM/min) AD activity + agent B (nM/min) [Alcohol] (nM) 0.1 14 2 0.5 50 7 8. 1.0 65 10 30 2.0 72 12 45 4.0 80 14 62 8.0 85 15 75 32.0 90 16 90
Chymotrypsin is an enzyme that is optimized to function in the small intestine (at a pH of ~7.4). Explain, given what you know about the chymotrypsin mechanism and what we learned about acid/base chemistry, why chymotrypsin would not be able to initiate catalysis if it were secreted into the stomach (pH ~2.5).
ver is given. A +B C+ D 1) Calculate AG for the above react un and indicáte whether the reaction is favorable or unfavorable [A] = 0.9 M 20°C AG° = 4 KJ/mol %3D [B] = 15mM [C] = 4mM [D] = 3 M R= 8.314 J/moleK %3D %3D 4.7 and explain how you know.
Can you graph the data
From a kinetics experiment, the Vmax was determined to be 450µM∙min-1. For the kinetic assay, 0.1mL of a 0.05mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 125,000 g/mole. Assume a reaction volume of 700µL. Calculate the kcat (in sec-1) for the enzyme.
Determine the values of KM and Vmax for the decarboxylation of a β-keto acid given the following data.
An enzyme-catalyzed reaction has a KM of 20.0 mmol L-1 and Vmax of 17.0 pmol s-1. When a mixed inhibitor is added, the apparent KM is 50.0 mmol L-1 and the apparent Vmax is 5.20 pmol s-1. Calculate α.
8L.3.4

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