Biochemistry (Looseleaf)
9th Edition
ISBN: 9781319114800
Author: BERG
Publisher: MAC HIGHER
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 10, Problem 27P
Interpretation Introduction
Interpretation:
The single amino acid that can be substituted to prepare a modified
Concept introduction:
The organic compounds that contain
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Help please. This question is specifically asking for the identification of the biomolecules that are attached to the sphingosine core, then we need to answer what bond causes those biomolecules to be connected to the sphingosine, what reaction created that bond (maybe addition or oxidation etc.), what were the starting materials and lastly what reagents or conditions are needed for the reaction to occur. Thank you!
I. Active site analysis.
Below is a diagram of a putative active site for Monoamine oxidase. As we learned, the purpose of
tertiary structure is to form a scaffold so you can orient just a few amino acids in the right orientation
to promote binding and/or catalysis. The position where this occurs is the active site. The amino acid
architecture of an active site is designed to bind substrates. Amino acid side chains are capable of
hydrogen bonding, ionic and hydrophobic interactions. Fill in each amino acid that you think is
suitable for interacting with the part of the substrate it is closest to. Assume the pH will be at 7.0
a.a.#1
a.a.#2
a.a.#6
HO
Lond
NH₂
НО
a.a.#5
OH
a.a.#3
a.a.#4
elearn.squ.edu.om/mod/qui
ystem (Academic)
The enzyme asparaginase is used to reduce the level of asparagine in blood in the treatment of leukemia.
Which of the following forms of Asparaginase would be most useful if the blood asparagine level is 0.2 mM?
Select one:
O a. Km = 2.0 mM; Vmax = 0.1 mM/hour
O b. Km = 0.1 mM; Vmax = 0.5 mM/hour
%3D
О с. Кm
0.2 mM; Vmax = 0.1 mM/hour
O d. Km = 0.1 mM; Vmax = 0.1 mM/hour
O e. Km = 0.2 mM; Vmax = 0.5 mM/hour
Clear my choice
In a steady state (of ES formation and ES breakdown)
Select one:
a The rate of formation of ES is equal to the rate of its degradation during the reaction
Chapter 10 Solutions
Biochemistry (Looseleaf)
Ch. 10 - Prob. 1PCh. 10 - Prob. 2PCh. 10 - Prob. 3PCh. 10 - Prob. 4PCh. 10 - Prob. 5PCh. 10 - Prob. 6PCh. 10 - Prob. 7PCh. 10 - Prob. 8PCh. 10 - Prob. 9PCh. 10 - Prob. 10P
Ch. 10 - Prob. 11PCh. 10 - Prob. 12PCh. 10 - Prob. 13PCh. 10 - Prob. 14PCh. 10 - Prob. 15PCh. 10 - Prob. 16PCh. 10 - Prob. 17PCh. 10 - Prob. 18PCh. 10 - Prob. 19PCh. 10 - Prob. 20PCh. 10 - Prob. 21PCh. 10 - Prob. 22PCh. 10 - Prob. 23PCh. 10 - Prob. 24PCh. 10 - Prob. 25PCh. 10 - Prob. 26PCh. 10 - Prob. 27PCh. 10 - Prob. 28PCh. 10 - Prob. 29PCh. 10 - Prob. 30PCh. 10 - Prob. 31PCh. 10 - Prob. 32PCh. 10 - Prob. 33PCh. 10 - Prob. 34PCh. 10 - Prob. 35PCh. 10 - Prob. 36PCh. 10 - Prob. 37PCh. 10 - Prob. 38PCh. 10 - Prob. 39PCh. 10 - Prob. 40PCh. 10 - Prob. 41PCh. 10 - Prob. 42PCh. 10 - Prob. 43P
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Accepting. Which of the following compounds readily accepts amino groups from amino acids? a. Glutamine b. Isocitrate c. Malate d. a-Ketoglutarate-Ketoglutaratearrow_forward- Keto counterparts. Name the a-ketoacida-ketoacid that is formed by the transamination of each of the following amino acids: Co, a. Alanine b. Leucine c. Aspartate d. Phenylalanine e. Glutamate f. Tyrosinearrow_forwardBIOCHEMISTRY DRAWING. pls accept question only if 100% confident please and thank you. Enalapril is inactive until acted upon by an esterase. Draw the structure of the resulting bioactive derivative. Hintarrow_forward
- . Provide an explanation for the fact that a-D-mannose is more stable than B-D-mannose, whereas the opposite is true for glucose.arrow_forwardan inorganic ion. Such as metal ion, that improves the fit of an enzyme with its substrate is a(n)?arrow_forwardBe sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Val, Met, Asp (2 equiv), Phe, Trp, Ile, Lys, and forms the following fragments when partially hydrolyzed with HCl: Ile-Asp-Phe, Lys-Met-Val-Trp, and Phe-Asp-Lys-Met. Trp Leu Phe Leu Val Lys Gly Tyr Xarrow_forward
- Sweet proteins. List the key classes of glycoproteins, their defining characteristics, and their biological functions.arrow_forwardBe sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Thr, Phe, Ile (2 equiv), Asp, Cys, Val, Leu, and forms the following fragments when partially hydrolyzed with HCl: Thr-Ile-Phe, Phe-Ile-Asp-Val, and Asp-Val-Cys-Leu.arrow_forwardCrohn’s disease. Omega-3 fatty acids have been tested asa means to prevent relapse of Crohn’s disease. Two large,randomized, placebo-controlled studies have shown nosuch benefit from omega-3 fatty acids. Suppose you areasked to design an experiment to further study this claim.Imagine that you have collected data on Crohn’s relapsesin subjects who have used these omega-3 fatty acids and similar subjects who have not used them and that you canmeasure incidences of relapse for these subjects. Statethe null and alternative hypotheses you would use in yourstudy.arrow_forward
- Enteric bacteria .lactic acid, and propionic bacteria have distinctive metabolic traits that can be used to characterized and identify these organisms .Describe the metabolic characteristics of these organisms name a genus that belong to each group, initiated in what way these organisms can be differentiated.arrow_forwardSIGNALS AND TARGETS. Listed below are sample polypeptides/proteins with their signal molecule/peptide. Answer the questions that follow. If you are asked to give the amino acid sequence, provide the sequence using the three-letter names of the amino acids (eg. ser-ala-met). Catalase with H2N-...KERINGKERIANGEKSAMSKL-COOH Provide the amino acid sequence of the signal peptide Where will this polypeptide be transported? (specify the compartment) What is the name of the specific receptor of this polypeptide? The receptor may also have what alternative function?arrow_forwardany biochemistry expect. please help, it's my last attempt..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. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals 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 LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals 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