Biochemistry: The Molecular Basis of Life
6th Edition
ISBN: 9780190209896
Author: Trudy McKee, James R. McKee
Publisher: Oxford University Press
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Chapter 6, Problem 6Q
Summary Introduction
To review:
The treatment that can be administered to infants suffering from Menkes’ syndrome, so that the symptoms of the disorder can be avoided.
Introduction:
Copper acts as a cofactor for enzymes like lysyl oxidase and superoxide dismutase. Copper is mainly present in the protein called ceruloplasmin, which is a deep blue glycoprotein. Itsmajor function is to transport and maintain the levels of the copper (Cu2+ ) ions in the body. Ceruloplasmin also maintains the iron
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Consider the mechanism of enolase, as indicated below. Which of the following
correctly describes the roles of the Mg2+ as illustrated in the figure? (This is a multi-
select question).
Mg2+
Mg2
Enolase
PO3-
OH
-C-C-H
H OH
HO
H-N-H
Lys 345
Glu211
2-Phosphoglycerate bound to enzyme
Mg2+
Mg2
PO3-
OH
C-C-H
OH
HO
H
H-N*-H
Lys 345
O
Glu211
Enolic intermediate
HOH
PO3-
H
Phosphoenolpyruvate
The metal ion (Mg2+) is helping to stabilize the extra negative charge that
developed on the carboxyl group in the enolic intermediate.
The metal ion (Mg2+) is serving as a general base, removing a proton in order to
improve the quality of the nucleophile.
The metal ion (Mg2+) is assisting in the oxidation of the carboxyl carbon through
metal ion catalysis.
The metal ion (Mg2+) is helping to orient the substrate properly in the active site.
The metal ion (Mg2+) is accepting a proton in order to improve the quality of the
leaving group.
Which of the following statements is true about the chymotrypsin reaction?
1. The catalytic triad at the active site is formed by three residues: His, Gly, and Ser
2. When the substrate is p-Nitrophenylacetate, the rate-limiting step is the release of p-Nitrophenolate.
3. During the reaction, LBHB forms when the proton is donated to His from Ser or water.
4. The chymotrypsin reaction involves “only” specific acid-base catalysis
5. The “oxyanion hole” is formed by the amide nitrogens of Ser and Glu
There is another class of aldolase enzymes known as Class II. These enzymes are found in fungi, algae, and some bacteria. This class differs for Class I in that these enzymes do not have a Lys residue associated with their active sites, but contain a divalent cation (usually Zn2+ or Fe2+) in the active site. Outline a possible mechanism for a Class II aldolase and explain the function of the metal ion in the reaction.
Chapter 6 Solutions
Biochemistry: The Molecular Basis of Life
Ch. 6 - Prob. 1QCh. 6 - Prob. 2QCh. 6 - Prob. 3QCh. 6 - Prob. 4QCh. 6 - Prob. 5QCh. 6 - Prob. 6QCh. 6 - Prob. 7QCh. 6 - Prob. 8QCh. 6 - Prob. 9QCh. 6 - Prob. 1RQ
Ch. 6 - Prob. 2RQCh. 6 - Prob. 3RQCh. 6 - Prob. 4RQCh. 6 - Prob. 5RQCh. 6 - Prob. 6RQCh. 6 - Prob. 7RQCh. 6 - Prob. 8RQCh. 6 - Prob. 9RQCh. 6 - Prob. 10RQCh. 6 - Prob. 11RQCh. 6 - Prob. 12RQCh. 6 - Prob. 13RQCh. 6 - Prob. 14RQCh. 6 - Prob. 15RQCh. 6 - Prob. 16RQCh. 6 - Prob. 17RQCh. 6 - Prob. 18RQCh. 6 - Prob. 19RQCh. 6 - Prob. 20RQCh. 6 - Prob. 21RQCh. 6 - Prob. 22RQCh. 6 - Prob. 23RQCh. 6 - Prob. 24RQCh. 6 - Prob. 25RQCh. 6 - Prob. 26RQCh. 6 - Prob. 27RQCh. 6 - Prob. 28RQCh. 6 - Prob. 29RQCh. 6 - Prob. 30RQCh. 6 - Prob. 31RQCh. 6 - Prob. 32RQCh. 6 - Prob. 33RQCh. 6 - Prob. 34RQCh. 6 - Prob. 35RQCh. 6 - Prob. 36RQCh. 6 - Prob. 37RQCh. 6 - Prob. 38RQCh. 6 - Prob. 39RQCh. 6 - Prob. 40RQCh. 6 - Prob. 41RQCh. 6 - Prob. 42RQCh. 6 - Prob. 43FBCh. 6 - Prob. 44FBCh. 6 - Prob. 45FBCh. 6 - Prob. 46FBCh. 6 - Prob. 47FBCh. 6 - Prob. 48FBCh. 6 - Prob. 49FBCh. 6 - Prob. 50FBCh. 6 - Prob. 51FBCh. 6 - Prob. 52FBCh. 6 - Prob. 53SACh. 6 - Prob. 54SACh. 6 - Prob. 55SACh. 6 - Prob. 56SACh. 6 - Prob. 57SACh. 6 - Prob. 58TQCh. 6 - Prob. 59TQCh. 6 - Prob. 60TQCh. 6 - Prob. 61TQCh. 6 - Prob. 62TQCh. 6 - Prob. 63TQCh. 6 - Prob. 64TQCh. 6 - Prob. 65TQCh. 6 - Prob. 66TQCh. 6 - Prob. 67TQCh. 6 - Prob. 68TQCh. 6 - Prob. 69TQCh. 6 - Prob. 70TQCh. 6 - Prob. 71TQCh. 6 - Prob. 72TQCh. 6 - Prob. 73TQCh. 6 - Prob. 74TQCh. 6 - Prob. 75TQCh. 6 - Prob. 76TQCh. 6 - Prob. 77TQCh. 6 - Prob. 78TQCh. 6 - Prob. 79TQCh. 6 - Prob. 80TQCh. 6 - Prob. 81TQ
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- Ethylene glycol (HO−CH2−CH2−OH) is a major component of antifreeze. In the body, it is first converted to HOOC−CHO (oxoethanoic acid) and then to HOOC−COOH (oxalic acid), which is toxic. What class of enzyme catalyzes both of the reactions of ethylene glycol? The treatment for the ingestion of ethylene glycol is an intravenous solution of ethanol. How might this help prevent toxic levels of oxalic acid in the body?arrow_forwardWrite out the balanced chemical equation for the FIRST round of oxidation of C16:cis-9.arrow_forwardMost individuals with genetic defects in oxidative phosphorylation are found to have relatively high concentrations of alanine in their blood. how this in biochemical terms? please help :)arrow_forward
- Hexokinase catalyzes the first step of glycolysis, in which glucose is phosphorylated to form glucose‑6‑phosphate. Give two reasons why a Mg2+ cation is required to facilitate this reaction.arrow_forwardIn 1937, two German biochemists published a paper proposing these reactions as part of glucose oxidation: citrate → isocitrate → α-ketoglutarate →succinate → fumarate → malate → oxaloacetate. Adding succinate, fumarate, or malate to thin slices of tissue increased oxygen consumption, supporting the hypothesis that these molecules are intermediates in the process. However, they were puzzled by the observation that these intermediates were still present in the reaction mixture at the end of the experiment. They had thought that intermediates would be consumed as they were converted to the next molecule in the pathway. What explains the observation that these intermediates were still present? a) The pathway is a cycle, constantly regenerating intermediates as glucose is broken down. b) Succinate, fumarate, and malate are not reactants but catalysts, and catalysts are not consumed in the process. c) Succinate, fumarate, and malate increase metabolism and therefore oxygen consumption,…arrow_forwardThe mechanism involved in the reaction catalyzed by phosphoglyceromutase is known to involve a phosphorylatedenzyme intermediate. If 3-phosphoglycerate is radioactively labeledwith 32P, the product of the reaction, 2-phosphoglycerate, does nothave any radioactive label. Design a mechanism to explain these facts.arrow_forward
- The following reaction is catalyzed by this type of enzyme? Coo COO™ I HIC-H H-C-H COO™ succinate isomerase hydrolase O ligase transferase oxidoreductase succinate dehydrogenase FAD FADH2 H-C || C-H COO fumaratearrow_forwardWhich class of enzymes catalyzes the following reactions? CH2- CH2- CH2 H2- C- CH2 AST CH2-C CH2 CH-NH + C=O + C=0 + CH-NH ČO0 Čo0 ČO0 ČO0" Aspartate Oxoglutarate Oxaloacetate Glutamate Select one: a. Oxidoreductase O b. Isomerase O c. Ligase d. Transferasearrow_forwardThioesters play important roles in glycolysis and tca cycle. List which reactions involve thioesters.arrow_forward
- The phosphorylation and oxidative decarboxylation of oxaloacetate by inorganic phosphate (Pi) to make phosphoenolpyruvate and carbon dioxide is endergonic under intracellular conditions. It is characterized by this equation: Oxaloacetate + Pi ←→ Phosphoenolpyruvate + H2O + CO2 ΔG’ = +24.6 kJ/mol The synthesis of GTP from GDP and inorganic phosphate (Pi) in solution is endergonic under intracellular conditions, and it is characterized by this equation: GDP + Pi ←→ GTP + H2O ΔG’ = +30.5 kJ/mol Write a new net thermodynamically coupled reaction equation that describes the synthesis of phosphoenolpyruvate from oxaloacetate using the hydrolysis of GTP to power the reaction and calculate the new net ΔG’ of this reaction. Show all of your work.arrow_forwardThiamine is the vitamin precursor for a co-enzyme called thiamine pyrophosphate or TPP. A patient diagnosed with thiamine deficiency exhibited fatigue and muscle cramps. The muscle cramps have been related to the accumulation of specific metabolic acids. On the following list, circle the metabolic acids that are most likely to accumulate in a thiamine deficiency? Note: There may be more than one. Isocitrate Pyruvate Succinate α-ketoglutarate Malate Fumarate (b) Provide a brief explanation for your answer to 1 (a) herearrow_forwardDraw the products of the reaction of xylulose-5-phosphate and erythrose-4-phosphate catalyzed by transketolase in the pentose phosphate pathway. Provide the structure in the protonation state found in physiological conditions. H H H OH FO HO-H H-OH H OPO3²- Q transketolase Draw glyceraldehyde-3- phosphate H H- H H H O OH OH OPO3²- Draw fructose-6- phosphate Q I Iarrow_forward
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