Organic Chemistry - Standalone book
10th Edition
ISBN: 9780073511214
Author: Francis A Carey Dr., Robert M. Giuliano
Publisher: McGraw-Hill Education
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Chapter 27.5, Problem 9P
Interpretation Introduction
Interpretation:
The fact that whether
Concept introduction:
For a spontaneous reaction, the value of change in Gibb’s free energy or
The relation between
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3) Calculate the physiological AG for the reaction: Phosphocreatine + ADP - creatine + ATP at
25 °C as it occurs in the cytosol of neurons, in which phosphocreatine is present at 4.7 mM,
creatine at 1.0 mM, ADP at 0.20 mM, and ATP at 2.6 mM, knowing that Phosphocreatine + H20
- creatine + Pi AG° = -43 kJ/mol and ATP + H20 ADP + Pi AG = -30.5 kJ/mol
The second step in the catabolism of most amino acids is the removal of the nitrogen atom from glutamate by oxidative
deamination. In this reaction, glutamate is converted to an a-keto acid.
Modify the structure to show the a-keto acid product.
?-
||
с
I
CH₂
I
H₂N-
&
+ remaining products
enzyme
CH₂
I
CH₂
+ NAD+ + H₂O
CH₂
Incorrect
Enter the chemical formulas for the remaining products.
remaining products: NADH + H+ + NH
Identify the enzyme that catalyzes the reaction.
The enzyme that catalyzes the reaction is glutamate
dehydrogenase.
OH
OH
For the following carbohydrates, please indicate the TRUE alternative:
(a) The carbohydrate V is reducing and is hydrolyzed by an enzyme of the type β galactosidase
(b) Carbohydrate VI is not reducing or mutating.
(c) Carbohydrates I and IV have β-glucosidic bond, while carbohydrate II has α-glucosidic bond.
(d) Carbohydrate III is neither reducing nor hydrolyzed by an α-type enzyme such as maltase.
(e) Carbohydrate I is reducing and mutating.
Chapter 27 Solutions
Organic Chemistry - Standalone book
Ch. 27.1 - Problem 27.1 Write a structural formula for the...Ch. 27.1 - Prob. 2PCh. 27.1 - Prob. 3PCh. 27.2 - Prob. 4PCh. 27.3 - Prob. 5PCh. 27.3 - Prob. 6PCh. 27.5 - Prob. 7PCh. 27.5 - Prob. 8PCh. 27.5 - Prob. 9PCh. 27.6 - Prob. 10P
Ch. 27.7 - Prob. 11PCh. 27.9 - Prob. 12PCh. 27.12 - 27.13 Modify Figure 27.12 so that it corresponds...Ch. 27.13 - Prob. 14PCh. 27 - Prob. 15PCh. 27 - Prob. 16PCh. 27 - Prob. 17PCh. 27 - Nebularine is a toxic nucleoside isolated from a...Ch. 27 - Prob. 19PCh. 27 - The 5-nucleotide of inosine, inosinic acid...Ch. 27 - Prob. 21PCh. 27 - (a) The two most acidic hydrogens of uracil have...Ch. 27 - The phosphorylation of -D-glucopyranose by ATP...Ch. 27 - When 6-chloropurine is heated with aqueous sodium...Ch. 27 - Prob. 25PCh. 27 - Prob. 26PCh. 27 - Prob. 27PCh. 27 - Prob. 28PCh. 27 - Oligonucleotide Synthesis In Section 27.6 we noted...Ch. 27 - Oligonucleotide Synthesis In Section 27.6 we noted...Ch. 27 - Oligonucleotide Synthesis In Section 27.6 we noted...Ch. 27 - Oligonucleotide Synthesis In Section 27.6 we noted...Ch. 27 - Oligonucleotide Synthesis In Section 27.6 we noted...Ch. 27 - Oligonucleotide Synthesis In Section 27.6 we noted...
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- Would a lipase hydrolyze two triglycerides, one containing only oleic acid and the other containing only palmitic acid, with equal ease?arrow_forwardAssume that in a certain cell, the ratio of products/reactants or Keq = 747.1 (Keq is dimensionless) for the reaction Glucose + ATP <> Glucose-6-P + ADP, at a particular instant, the concentrations of each compound were Glucose =2.0M, ATP =7.7M, ADP =10.2M and G-6-P =21.5M. Calculate the difference (dimensionless) between Keq and the ratio of products/ractants at this instance, in this cell, to five significant figures.arrow_forward. Each gram of mammalian skeletal muscle consumes ATP at a rate of about 1x 10-3 mol/min during contraction. Concentrations of ATP and creatine phosphate in muscle are about 4 mM and 25 mM, respectively, and the density of muscle tissue can be taken to be about 1.2 g/cm'. (a) How long could contraction continue using ATP alone? (b) If all creatine phosphate were converted into ATP and utilized as well, how long could contraction continue? (c) What do these answers tell you?arrow_forward
- Summerize importan functions of Glutathione Reductase. Where it is made? In all cells or only specific organs/ tissues?arrow_forwardAn enzymatic assay was performed using the enzyme phophofructokinase-1, which catalyses the committed step of the glycolysis pathway. What is the final concentration of the fructose 6-phosphate substrate in a test tube containing the following: 250 µL of 150pM fructose 6-phophate, 100 µL 20 mg.ml-1 phosphofructoskinase-1 and 150 µL 100mM buffer pH 7.5arrow_forwardConsider the reaction: FADH2 + ½O2 ↔ H2O + FAD Which of the following best describes the reaction? A. -1.035 V; nonspontaneous B. -1.035 V; spontaneous C. +1.035 V; nonspontaneous D. +1.035 V; spontaneousarrow_forward
- When the following reaction reached equilibrium the concentration of glucose 1-phosphate is 34mM, and the concentration of glucose 6-phosphate is 190mM. At standard temperatures and pressure, calculate the Keq and the ΔGo' glucose 6-phosphate <---(phosphoglucoisomerase)---> glucose 1-phosphate Keq= ΔGo' =arrow_forwardTPP is a coenzyme for transketolase, the enzyme that catalyzes the conversion of a ketopentose (xylulose- 5-phosphate) and an aldopentose (ribose-5-phosphate) to an aldotriose (glyceraldehyde-3-phosphate) anda ketoheptose (sedoheptulose-7-phosphate). Notice that the total number of carbons in the reactants and products is the same (5 + 5 = 3 + 7). Propose a mechanism for this reaction.arrow_forwardConsider the following reaction: (P, is inorganic phosphate, i.e., HPO4² and H₂PO4) glucose + P + 3.3 kcal glucose-6-phosphate + H₂O If the energy used for the reaction is obtained from the hydrolysis of ATP (AH = -7.3 kcal.mol), the reaction will go to completion. Select one: O True O Falsearrow_forward
- At active muscle I. PCO2 is high II. acidity is low III. carbamate forms IV. hemoglobin is stabilized in the T state O lonly O II, III and IV O I and III O I, II, III and IV O I, III and IVarrow_forwardTPP is a coenzyme for transketolase, the enzyme that catalyzes the conversion of a ketopentose (xylulose5-phosphate) and an aldopentose (ribose-5-phosphate) to an aldotriose (glyceraldehyde-3-phosphate) and a ketoheptose (sedoheptulose-7-phosphate). Notice that the total number of carbons in the reactants and products is the same (5 + 5 = 3 + 7). Propose a mechanism for this reaction.arrow_forwardThe isoelectric point, pl, of the protein trypsin is 10.5, while that of glyceraldehyde-3-phosphate dehydrogenase is 6.55. What is the net charge of trypsin at pH 5.1 ?[ What is the net charge of glyceraldehyde-3-phosphate dehydrogenase at pH 6.1 ?[ The isoelectric point of glutamic acid is 3.22; asparagine, 5.41. During paper electrophoresis at pH 6, toward which electrode does glutamic acid migrate? | During paper electrophoresis at pH 6.5, toward which electrode does asparagine migrate? [arrow_forward
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