FUNDAMENTALS OF BIOCHEMISTRY WPNG 1-SEME
5th Edition
ISBN: 9781119750192
Author: Voet
Publisher: WILEY
expand_more
expand_more
format_list_bulleted
Question
Chapter 12, Problem 32CQ
Summary Introduction
To explain: The reason why uncompetitive and mixed inhibitors are generally considered to be more effective in vivo than competitive inhibitors.
Concept introduction: Enzyme inhibitors are those that block the enzyme activity. Enzyme inhibitors are of several types.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Insert Format Tools Extensions Help
Normal text ▾ Arial
C
2
10
3
+ BIUA
Student Guide (continued)
Record data and conclusions about the mystery food sample either below or in a lab notebook.
Step 2: Protein Test (Biuret Solution)
Gelatin
Water
[Mystery Food
(Positive Control)
(Negative Control)
Sample
pink purple
no change
no change
They mystery food sample does not contain protein because the color of the
test tube wasn't pink or purple
Color
Conclusion They mystery food sample does not contain protein because the color of the test tube
wasn't pink or purple
Step 3: Lipid Test (Sudan Red Solution)
Vegetable Oil
Water
(Positive Control)
(Negative Control)
Mystery Food
Sample
floating red
no change
floating red
the mystery food dosnt contain lipids because the test tube has floating red
75
%
87
8
9
7
ChromeOS C
Device will pow
26.battery lea
power
The rate data from an enzyme catalyzed reaction with and without an inhibitor present is found in the image.
Question: what is the KM and Vm and the nature of inhibition
1. Estimate the concentration of an enzyme within a living cell. Assume that:
(a): fresh tissue is 80% water and all of it is intracellular
(b): the total soluble protein represents 15% of the weight
(c): all the soluble proteins are enzymes
(d): the average molecular weight of the proteins is 150,000
(E): about 100 different enzymes are present
please help I am lost
Chapter 12 Solutions
FUNDAMENTALS OF BIOCHEMISTRY WPNG 1-SEME
Ch. 12 - Prob. 1ECh. 12 - Prob. 2ECh. 12 - Prob. 3ECh. 12 - Prob. 4ECh. 12 - 5. From the reaction data below, determine whether...Ch. 12 - Prob. 6ECh. 12 - 7. For an enzymatic reaction, draw curves that...Ch. 12 - 8. Explain why it is usually easier to calculate...Ch. 12 - Prob. 9ECh. 12 - 10. Identify the enzymes in Table 12-1 whose...
Ch. 12 - 11. Calculate KM and Vmax from the following...Ch. 12 - 12. Explain why each of the following data sets...Ch. 12 - 13. The KM for the reaction of chymotrypsin with...Ch. 12 - 14. Enzyme A catalyzes the reaction S ? P and has...Ch. 12 - 15. In a bisubstrute reaction, a small amount of...Ch. 12 - 16. In a bisubstrate reaction, a small amount of...Ch. 12 - Prob. 17ECh. 12 - 18. Molecule A is the substrate for enzyme X....Ch. 12 - 19. Determine the type of inhibition of an...Ch. 12 - 20. Estimate KI for a competitive inhibitor when...Ch. 12 - Prob. 21CQCh. 12 - 22 Is it necessary to know [E]T to determine (a)...Ch. 12 - 23. You are trying to determine the KM for an...Ch. 12 - 24. You are attempting to determine KM by...Ch. 12 - Prob. 25CQCh. 12 - 26. Enzyme X and enzyme Y catalyze the same...Ch. 12 - 27. Based on some preliminary measurements, you...Ch. 12 - 28. For the same enzyme sample described in...Ch. 12 - 29. For an enzyme catalyzed reaction, the presence...Ch. 12 - 30. Sphingosine-1-phosphate (S1P) is important for...Ch. 12 - 31. Ethanol in the body is oxidized to...Ch. 12 - Prob. 32CQCh. 12 - MORE TO EXPLORE What kind of inhibitor is...
Knowledge Booster
Similar questions
- The following data were recorded for the enzyme catalyzed conversion of S -> P Question: what would the rate be at 5.0 x 10-5 M [S] and the enzyme concentration was doubled? Also, the rate given in the table is from product accumulation after 10 minuets of reaction time. Verify these rates represent a true initial rate (less than 5% turnover). Please helparrow_forwardThe following data was obtained on isocitrate lyase from an algal species. Identify the reaction catalyzed by this enzyme, deduce the KM and Vmax , and determine the nature of the inhibition by oxaloacetate. Please helparrow_forwardIn the table below, there are sketches of four crystals made of positively-charged cations and negatively-charged anions. Rank these crystals in decreasing order of stability (or equivalently increasing order of energy). That is, select "1" below the most stable (lowest energy) crystal. Select "2" below the next most stable (next lowest energy) crystal, and so forth. A B 鹽 (Choose one) +2 C +2 +2 (Choose one) D 鹽雞 (Choose one) (Choose one)arrow_forward
- 1. Draw the structures for the fats A. 16:2: w-3 and B. 18:3:49,12,15 2. Name each of the molecules below (image attached)arrow_forwarddraw the structures for the fats A. 16:2:w-3 B 18:3:9,12,15arrow_forward1. Below is a template strand of DNA. Show the mRNA and protein that would result. label the ends of the molecules ( refer to attached image)arrow_forward
- Attach the followina labels to the diagram below: helicase, single stranded binding proteins, lagging strand, leading strand, DNA polymerase, primase, 5' ends (3), 3' ends (3) (image attached)arrow_forward1. How much energy in terms of ATP can be obtained from tristearin (stearate is 18:0) Show steps pleasearrow_forwardMultiple choice urgent!!arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. Freeman
Lehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
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
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
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