Biochemistry
8th Edition
ISBN: 9781464126109
Author: Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr., Lubert Stryer
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 13, Problem 7P
Interpretation Introduction
Interpretation:
The mechanism of
Concept introduction:
ATPases belong to the class of enzymes catalyzing the ATP to ADP decomposition. This also results in the formation of a free phosphate ion. The reverse reaction is also catalyzed by the same enzyme. The energy is released during the dephosphorylation reaction. The process is widely used in all the forms of life.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
The preferred substrate is T because the enzyme half-saturates at 7.00 mM for T, but requires 28.0 mM for U, and 112 mM for S.
b
Question Content Area
The rate constant k 2 with substrate S is 9.60×107 sec-1, with substrate T, k 2 = 6.00×104 sec-1, and with substrate U, k 2 = 2.40×106 sec-1.
Calculate the catalytic efficiency with S, T, and U.
Catalytic efficiency with S =
Catalytic efficiency with T =
Catalytic efficiency with U =
Does enzyme A use substrate S, substrate T, or substrate U with greater catalytic efficiency?
Fumerase catalyzes the conversion of fumerate to malate.
fumerate + H2O ⇋ malate
The turnover number, kcat, for fumerase is 8.00×102 sec-1. The Km of this enzyme for fumerate is 5.00×10-3 μmol mL-1.
a
In an experiment using 2.00×10-3 μmol·mL-1, what is Vmax?
Suppose you wanted to make a buffer of exactly pH 7.00 using KH2PO4 and Na2HPO4. If the final solution was 0.18 M in KH2PO4, you would need 0.25 M Na2HPO4. Now assume you wish to make a buffer at the same pH, using the same substances, but want the total phosphate molarity ([HPO42−]+[H2PO−4]) to equal 0.20 M. What concentration of the Na2HPO4 would be required?
Chapter 13 Solutions
Biochemistry
Ch. 13 - Prob. 1PCh. 13 - Prob. 2PCh. 13 - Prob. 3PCh. 13 - Prob. 4PCh. 13 - Prob. 5PCh. 13 - Prob. 6PCh. 13 - Prob. 7PCh. 13 - Prob. 8PCh. 13 - Prob. 9PCh. 13 - Prob. 10P
Ch. 13 - Prob. 11PCh. 13 - Prob. 12PCh. 13 - Prob. 13PCh. 13 - Prob. 14PCh. 13 - Prob. 15PCh. 13 - Prob. 16PCh. 13 - Prob. 17PCh. 13 - Prob. 18PCh. 13 - Prob. 19PCh. 13 - Prob. 20PCh. 13 - Prob. 21PCh. 13 - Prob. 22PCh. 13 - Prob. 23PCh. 13 - Prob. 24PCh. 13 - Prob. 25PCh. 13 - Prob. 26PCh. 13 - Prob. 27PCh. 13 - Prob. 28PCh. 13 - Prob. 29PCh. 13 - Prob. 30PCh. 13 - Prob. 31PCh. 13 - Prob. 32P
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
- Match the three types of neurotransmitters to their relative size (largest to smallest): Largest Peptide neurotransmitter ✓ Second largest [Choose] Smallest > [Choose ] [Choose ] Amino acid neurotransmitter Peptide neurotransmitter Amine neurotransmitterarrow_forwardneed help not sure why its wrong please helparrow_forwardWhy the 2nd choice is correct?arrow_forward
- a) What are the differences between the Direct & Indirect Immunofluorescence Assays? (0.5 mark) b) What are the advantages of the Indirect Immunofluorescence Assays? (0.5 mark) c) A Super-Resolution Imaging Technique was developed in 2018 using imidazole, a His-tag ligand conjugated with a fluorophore to report the presence of a recombinant His-tag protein target, (Sci Rep, 2018, 8:5507). How does this technique improve the image quality? (2 marks)arrow_forwarda) What are the differences between the Direct & Indirect Immunofluorescence Assays? b) What are the advantages of the Indirect Immunofluorescence Assays? c) A Super-Resolution Imaging Technique was developed in 2018 using imidazole, a His-tag ligand conjugated with a fluorophore to report the presence of a recombinant His-tag protein target, (Sci Rep, 2018, 8:5507). How does this technique improve the image quality?arrow_forwardCalculate the number of ATP produced from oxidation of 1 molecule of glucosearrow_forward
- Example 1: 1. Suppose an enzyme (MW = 5,000 g/mole) has a concentration of 0.05 mg/L. If the kcat is 1 x 10 s, what is the theoretical maximum reaction velocity for the enzyme? A) 1050 µM/s. B) 100 µM/s. C) 150 μM/s. D) 105 μM/s.arrow_forwardIn 1956, E. P. Kennedy and S. B. Weiss published their study of membrane lipid phosphatidylcholine (lecithin) synthesis in rat liver. Their hypothesis was that phosphocholine joined with some cellular component to yield lecithin. In an earlier experiment, incubating 32 P-labeled phosphocholine at physiological temperature (37 °C) with broken cells from rat liver yielded labeled lecithin. This became their assay for the enzymes involved in lecithin synthesis. Determine the optimal pH for this enzyme and characterize the enzyme activity at different pH values. -O-P-O-CH2-CH₁₂-N(CH3)3 Phosphocholine H₂C-O-C-R HC-O-C-R2 + + + Cell fraction + ? HC-O-P-O-CH₁₂-CH₂-N(CH), O Phosphatidylcholine The researchers then centrifuged the broken cell preparation to separate the membranes from the soluble proteins. They tested three preparations: whole extract, membranes, and soluble proteins. Table 1 summarizes the results. Table 1: Cell fraction requirement for incorporation of 32p-phosphocholine into…arrow_forwardResearchers isolated an unknown substance, X, from rabbit muscle. They determined its structure from the following observations and experiments. (a) Qualitative analysis showed that X was composed entirely of C, H, and O. A weighed sample of X was completely oxidized and the H2O and CO2 produced were measured. This quantitative analysis revealed that X contained 40.00% C, 6.71% H, and 53.29% O by weight. (b) The molecular mass of X, as determined by mass spectrometry, was 90.00 atomic mass units (u). (c) Infrared spectroscopy showed that X contained one double bond. (d) X dissolved readily in water, and the solution demonstrated optical activity when tested in a polarimeter. (e) The aqueous solution of X is acidic. What is the empirical formula of X?arrow_forward
- Show work. don't give Ai generated solution....give correct solutionarrow_forwardBiochemistry What is the process of "transamination" in either the muscles or the liver, that involves keto acid or glutamic acid? Please explain how the steps work. Thank you!arrow_forwardBiochemistry Please help. Thank you What is the importance of glutamic acid in the metabolism of nitrogen from amino acids? (we know therole; it’s used to remove the nitrogen from amino acids so that the remaining carbon skeleton can bebroken down by the “usual” pathways, but what is the important, unique role that only glutamicacid/glutamate can do?)arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biology: The Dynamic Science (MindTap Course List)BiologyISBN:9781305389892Author:Peter J. Russell, Paul E. Hertz, Beverly McMillanPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
Biology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStax
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Biology: The Dynamic Science (MindTap Course List)
Biology
ISBN:9781305389892
Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax