BIOCHEM-ACHIEVE(FIRST DAY DISCOUNTED)
9th Edition
ISBN: 2818000069358
Author: BERG
Publisher: MAC HIGHER
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 23, Problem 7P
Interpretation Introduction
Interpretation:
Cofactors needed by the aminotransferases should be determined.
Concept introduction:
Transamination is also known as an amino transfer. It is a
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
- 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. Tyrosine
Od. Vitamin B2
s page
Hexokinase catalyzes phosphorylation of glucose to clucose-6-phosphate, where ATP is used as a donor of phosphate group, this
an example of:
Select one:
NAVIGATION
a. Oxidoreductase
b. Ligase
c. Lyase
d. Transferase
Next page
a. Protein X can be phosphorylated. Why would the phosphorylated form of protein X elute AFTER the unphosphorylated form from an ANION exchange column? Please describe in terms of: The chemical properties of phosphorylation modification
b. The chemical properties of an anion exchange column and how it works
c. Why is an inhibitor that mimics the transition state more effective at enzyme inhibition than an inhibitor that mimics the substrate?
d. Protein X can be covalently modified with many methyl groups. What two general properties would be different between the unmethylated protein versus the methylated protein?
Chapter 23 Solutions
BIOCHEM-ACHIEVE(FIRST DAY DISCOUNTED)
Ch. 23 - Prob. 1PCh. 23 - Prob. 2PCh. 23 - Prob. 3PCh. 23 - Prob. 4PCh. 23 - Prob. 5PCh. 23 - Prob. 6PCh. 23 - Prob. 7PCh. 23 - Prob. 8PCh. 23 - Prob. 9PCh. 23 - Prob. 10P
Ch. 23 - Prob. 11PCh. 23 - Prob. 12PCh. 23 - Prob. 13PCh. 23 - Prob. 14PCh. 23 - Prob. 15PCh. 23 - Prob. 16PCh. 23 - Prob. 17PCh. 23 - Prob. 18PCh. 23 - Prob. 19PCh. 23 - Prob. 20PCh. 23 - Prob. 21PCh. 23 - Prob. 22PCh. 23 - Prob. 23PCh. 23 - Prob. 24PCh. 23 - Prob. 25PCh. 23 - Prob. 26PCh. 23 - Prob. 27PCh. 23 - Prob. 28PCh. 23 - Prob. 29PCh. 23 - Prob. 30PCh. 23 - Prob. 31PCh. 23 - Prob. 32PCh. 23 - Prob. 33PCh. 23 - Prob. 34PCh. 23 - Prob. 35PCh. 23 - Prob. 36PCh. 23 - Prob. 37PCh. 23 - Prob. 38PCh. 23 - Prob. 39PCh. 23 - Prob. 40PCh. 23 - Prob. 41PCh. 23 - Prob. 42PCh. 23 - Prob. 43PCh. 23 - Prob. 44PCh. 23 - Prob. 45PCh. 23 - Prob. 46PCh. 23 - Prob. 47PCh. 23 - Prob. 48PCh. 23 - Prob. 49P
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
- . 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_forwardI. 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.#4arrow_forwardAccepting. Which of the following compounds readily accepts amino groups from amino acids? a. Glutamine b. Isocitrate c. Malate d. a-Ketoglutarate-Ketoglutaratearrow_forward
- IX. Insulin, a hormone vital in blood sugar regulation and having a polypeptide chain with disulfide linkages, loses its regulatory activity when heated at nearly 100°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of insulin relative to its native structure and function. I--arrow_forwardOnly a few amino acid residues are actually involved in catalysis in enzymes, yet enzymes are constructed of at least 100 amino acids, and often many more. Suggest some functions for the noncatalytic amino acids.arrow_forwardV-A. Which of the following amino acids will elute first in a cation-exchange column using a buffer at pH 7? 1. Asp or Lys 2. Arg or Met 3. Gly or Val 4. Ser or Alaarrow_forward
- a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).arrow_forwarddisease. As such, a frontline treatment for Type 2 diabetes is the drug metformin, which acts indirectly to inhibit gluconeogenesis in the liver. You are a research biochemist who would like to develop new drugs that act to directly inhibit gluconeogenesis. You have just gained access to a library of thousands of small molecules of unknown activity, and you would like to identify lead compounds that have specific inhibitory activity against steps in the gluconeogenesis pathway. (a) into PEP in order to screen for inhibitors of enzymes specific to gluconeogenesis. Which enzymes do you need to purify, what cofactors and allosteric effectors do they require, and which reactants do you need to add to reconstitute the reactions for the first bypass? Which intermediates and products are generated? Your first approach is to reconstitute the initial set of bypass reactions that convert pyruvate (b) vitro reconstitution? What additional steps and enzymes are required in liver cells but are…arrow_forward.Intramitochondrial ATP concentrations are about 5 mM, and phosphate con- centration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions. The energy charge is the concentration of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]arrow_forward
- Answer TRUE or FALSE.a. A simple enzyme contains only nonprotein.b. The difference between a cofactor and a coenzyme is that a cofactor may be inorganic ororganic; a coenzyme is an organic cofactor.c. The enzyme involved in the discoloration of cut fruits and vegetables is called benzoquinonase.d. Lycopene is the compound responsible for the “grapefruit effect.”arrow_forwardA7. Consider what can be concluded about the catalytic site (substrate binding site) of phosphatase and the binding site of NaF from the type of inhibition shown by NaF for phosphatase and illustrate it schematically. The inhibition typre is pure noncompetitive inhibition.arrow_forwardan inorganic ion. Such as metal ion, that improves the fit of an enzyme with its substrate is a(n)?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
Macromolecules | Classes and Functions; Author: 2 Minute Classroom;https://www.youtube.com/watch?v=V5hhrDFo8Vk;License: Standard youtube license