6 . Use the table of completely made-up data below to answer the following questions about a completelymade-up enzyme.Enzymeno enzymewild typeR225LR58LE167AK(AM)5.8 x 10*4.9 x 103.3 х 104.1 x 102.8 x 108.1 x 1026.7 x 102.2 x 10100.8856988:411724E201A105.6196л98.8C14ATI1.7a. Using the information in the table above, approximately what is the fold rate enhancementfor the wild type enzyme compared to the non-enzymatic reaction? 'b. Six different active site amino acid mutant enzymes were studied here. Comparing theseto the wild type, which of the amino acids listed play a role in catalysis? "c. Which of the amino acids listed are important for binding to the substrate, but notnecessarily for catalysis? ("

Fold rate enhancemenet =Rate after enhancementRate before enhancement Kcat (Turnover number) is…

Answered: . Use the table of completely made-up…

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

BIM-46187 is a protein inhibitor that binds to the a-subunit of the G, protein. It prevents the GDP/GTP exchange and prevents activity of the G protein. Which of the following would you expect to see lower levels of as a result? You can select more than one answer. S-S Mol. W: 795.11 Image: https://aobious.com/aobious/protein-inhibitors/1086-bim-46187.html Select one or more: O a. Cyclic AMP (CAMP) O b. Tyrosine kinase HSP O d. Adenylyl Cyclase (AC) O e. DAG O f. JAK O g. IP3
Refer to the following graph when answering questions. These words may be used to fill: competitive, uncompetitive, noncompetitive, irreversible. -1 mg , μmol min-1 v-1 0.2 0.1 THA -4-2 CBA + 2 4 [S]-1, (mM-1) Word 1, The value of Km for the enzyme depicted by curve A is 2, The value of Vmax for the enzyme depicted by curve A is 3, Curve B depicts the effect of an inhibitor on the system described by curve A. This inhibitor is a inhibitor. 4, Curve C depicts the effect of a different inhibitor of the system described by curve A. This second inhibitor is a inhibitor. D
-Inhibitor +Inhibitor [S] (mM). V&νβσπ:(μmol/sec) V0&νβσπ&ν βσπ;(μmol/sec) 0.0001 33 17 0.0005 71 50 0.001 83 67 0.005 96 91 0.01 98 95 What is the Vmax of this enzyme WITHOUT iinhibitor?
Given the line-weaver Burke plot below for Enzyme Y, identify the Vmax for Enzyme Y. -10 30 1/v 1/[S] 5 10 Enter the numerical value for Vmax only, no letters or symbols. Round answer to 2 significant figures.
Consider the Michaelis-Menten enzymes below and answer the following questions. Kcat (s') 9.5*105 1.4*10* 2.5*102 1.0*107 5.0*10 8.0*10² Enzyme Km (M) A В a. Which enzyme has the highest affinity substrate? How do you know? b. Which enzyme can convert the most substrate to product in a given period of time? How do you know? c. Which enzyme has the highest catalytic efficiency? How do you know?
Intracellular and extracellular enzymes require different extraction methods. Provide 2 examples of intracellular enzyme extraction methods and explain the reason for performing this step.
A. Lineweaver-Burk plot of the enzyme with increasing amounts of substrate in the absence or the presence of the inhibitor is shown below. Graph A : x-intercept Graph B : x-intercept = - 0.012, y-intercept = 0.8 Graph C : x-intercept = - 0.027, y-intercept = 0.8 Graph D : x-intercept = - 0.039, y-intercept = 0.8 - 0.007, y-intercept = 0.8 Graph A 4 Graph B Graph C Graph D 1 -0,04 -0,02 0,00 0,02 0,04 1/[Substrate] (uM) (i) Which graph indicates an enzymatic reaction without inhibitor? (ii) Which type of inhibitor is it? Briefly explain. (iii) Which graph indicates the highest concentration of inhibitor? (iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers. 1/Rate (umol/min)
S Savvas EasyBridge IS Savvas Realize asrealize.com/assignments/viewer/classes/61227fd32e855b44e0a77ded/assignments/96054946a5024ac29d3c30068e59b062/contents/c ming of Enzymes nzymes Drag each substrate to the enzyme with the matching active site. Enzymes 1. Changing environmental conditions, such as temperature or pH, can affect enzyme shape. How would this alter the enzyme's function? Substrates Type your answer here. acer
In the Lineweaver Burke plot shown below, which of the following is true? With inbito Wthout nhitor O Km is increasing. Vmax is decreasing Km is decreasing, Vmax is decreasing Km is increasing, Vmax is increasing Km is decreasing, Vmax is in QUESTION 35 As per the Enzyme commission classification, the tranferases belong to which of the following Class? O 2 O 4 O 3 Click Save and Submit to save and submit. Click Save All Answers to save all answers. 78 F Mostly cloudy
-Inhibitor +Inhibitor [S] (mM) V0&νβσπ;(μmol/sec). νο&νβσπ: &ν βσπ (μmol/sec) 0.0001 33 17 0.0005 71 50 0.001 83 67 0.005 96 91 0.01 98 95 What is the Vmax of this enzyme WITH iinhibitor?
When considering treatment options for SCID, enzyme replacement offers a permanent fix for patients while gen therapy offers short-term relief from symptoms True False
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.

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