Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
8th Edition
ISBN: 9780134015187
Author: John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Textbook Question
Chapter 19.3, Problem 19.4P
Describe the reactions that you would expect these enzymes to catalyze.
- (a) Alcohol dehydrogenase
- (b) Aspartate transaminase
- (c) Tyrosine-tRNA synthetase
- (d) Phosphohexose isomerase
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different
specificities.
(a) These proteases are considered serine proteases because the active sites contain serine, histidine
and aspartate. Describe the roles that each of these amino acid residues play in hydrolyzing protein
substrates.
(b) The active site pockets of chymotrypsin, trypsin, and elastase are shown in the image below.
Based on the image, which side chain of the amino acids would they prefer to cleave respectively, Ala,
Arg, or Trp? Explain your answers.
Val 216KVal 190
Asp 189
Chymotrypsin
Trypsin
Elastase
Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different
specificities.
(a) These proteases are considered serine proteases because the active sites contain serine, histidine
and aspartate. Describe the roles that each of these amino acid residues play in hydrolyzing protein
substrates.
(b) The active site pockets of chymotrypsin, trypsin, and elastase are shown in the image below.
Based on the image, which side chain of the amino acids would they prefer to cleave respectively, Ala,
Arg, or Trp? Explain your answers.
Val 216
Val 190
Asp 189
Chymotrypsin
Trypsin
Elastase
Identify each reaction catalyzed by (a) a nucdeotidase; (b) a phosphorylase;
(c) a phosphoribosyltransferase.
GMP
A
D
E
Guanine
Guanosine
F
Chapter 19 Solutions
Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
Ch. 19.1 - Prob. 19.1PCh. 19.1 - The enzyme LDH converts lactate to pyruvate. In...Ch. 19.2 - The cofactors NAD+, Cu2+, Zn2+, coenzyme A, FAD,...Ch. 19.3 - Describe the reactions that you would expect these...Ch. 19.3 - Prob. 19.5PCh. 19.3 - Prob. 19.6PCh. 19.3 - Prob. 19.7PCh. 19.3 - Prob. 19.8PCh. 19.4 - Prob. 19.9KCPCh. 19.5 - Prob. 19.10KCP
Ch. 19.5 - Prob. 19.11PCh. 19.5 - Prob. 19.12PCh. 19.6 - Prob. 19.13PCh. 19.6 - Prob. 19.14PCh. 19.7 - (a) L-Threonine is converted to L-isoleucine in a...Ch. 19.8 - AZT (zidovudine) inhibits the synthesis of the HIV...Ch. 19.8 - Prob. 19.3CIAPCh. 19.8 - Prob. 19.16PCh. 19.9 - Does the enzyme described in each of the following...Ch. 19.9 - Prob. 19.18PCh. 19.9 - Compare the structures of vitamin A and vitamin C....Ch. 19.9 - Prob. 19.20PCh. 19.9 - Prob. 19.21KCPCh. 19.9 - Prob. 19.22PCh. 19.9 - Prob. 19.4CIAPCh. 19.9 - Prob. 19.6CIAPCh. 19.9 - Prob. 19.7CIAPCh. 19.9 - Enzyme levels in blood are often elevated in...Ch. 19.9 - Prob. 19.9CIAPCh. 19.9 - Prob. 19.23PCh. 19 - Prob. 19.24UKCCh. 19 - Prob. 19.25UKCCh. 19 - Prob. 19.26UKCCh. 19 - Prob. 19.27UKCCh. 19 - Prob. 19.28APCh. 19 - Explain how the following mechanisms regulate...Ch. 19 - Prob. 19.30APCh. 19 - Prob. 19.31APCh. 19 - Prob. 19.32APCh. 19 - Prob. 19.33APCh. 19 - Prob. 19.34APCh. 19 - Prob. 19.35APCh. 19 - Prob. 19.36APCh. 19 - Prob. 19.37APCh. 19 - Name an enzyme that acts on each molecule. (a)...Ch. 19 - Name an enzyme that acts on each molecule. (a)...Ch. 19 - What features of enzymes make them so specific in...Ch. 19 - Describe in general terms how enzymes act as...Ch. 19 - Prob. 19.42APCh. 19 - Prob. 19.43APCh. 19 - Prob. 19.44APCh. 19 - Prob. 19.45APCh. 19 - Prob. 19.46APCh. 19 - Prob. 19.47APCh. 19 - What is the difference between the lock-and-key...Ch. 19 - Why is the induced-fit model a more likely model...Ch. 19 - Prob. 19.50APCh. 19 - Prob. 19.51APCh. 19 - How do you explain the observation that pepsin, a...Ch. 19 - Prob. 19.53APCh. 19 - Prob. 19.54APCh. 19 - Prob. 19.55APCh. 19 - Prob. 19.56APCh. 19 - Prob. 19.57APCh. 19 - The text discusses three forms of enzyme...Ch. 19 - Prob. 19.59APCh. 19 - Prob. 19.60APCh. 19 - Prob. 19.62APCh. 19 - Prob. 19.63APCh. 19 - The meat tenderizer used in cooking is primarily...Ch. 19 - Prob. 19.65APCh. 19 - Why do allosteric enzymes have two types of...Ch. 19 - Prob. 19.67APCh. 19 - Prob. 19.68APCh. 19 - Prob. 19.69APCh. 19 - Prob. 19.70APCh. 19 - Prob. 19.71APCh. 19 - Prob. 19.72APCh. 19 - Prob. 19.73APCh. 19 - Prob. 19.74APCh. 19 - Prob. 19.75APCh. 19 - Prob. 19.76APCh. 19 - Prob. 19.77APCh. 19 - Prob. 19.78APCh. 19 - Prob. 19.79APCh. 19 - Prob. 19.80CPCh. 19 - Prob. 19.81CPCh. 19 - Prob. 19.82CPCh. 19 - Prob. 19.83CPCh. 19 - Prob. 19.84CPCh. 19 - Prob. 19.85CPCh. 19 - Prob. 19.86CPCh. 19 - Prob. 19.87CPCh. 19 - Prob. 19.88GPCh. 19 - The ability to change a selected amino acid...Ch. 19 - Prob. 19.90GPCh. 19 - Prob. 19.91GP
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
- The glycine cleavage system is a group of four enzymes that together catalyze the following reaction: Use the following information to determine the sequence of reactions carried out by the glycine cleavage system:a. The first enzyme is a PLP-requiring decarboxylase.b. The second enzyme is aminomethyltransferase. This enzyme has a lipoate coenzyme.c. The third enzyme synthesizes N5,N10-methylene-THF and also forms +NH4.d. The fourth enzyme is an FAD-requiring enzyme.e. The cleavage system also requires NAD+ .arrow_forward(b) Biotin is a coenzyme required for a key step in gluconeogenesis. (i) To which enzyme is biotin linked and what is the nature of the bond? (ii) What properties do the biotin and the linkage have that enable biotin to interact with two distinct active sites in this enzyme? (iii) What chemical steps take place at each of these active sites (no need to specify the complete reactions)?arrow_forwardWhich folate structure (from the list below)(a) is the substrate for the enzyme that is inhibited by methotrexate andtrimethoprim?(b) has the most highly oxidized one-carbon substituent?(c) is used in the conversion of serine to glycine?(d) transfers its one-carbon substituent to a B12 coenzyme? What amino acid is synthesized as the end result of this reaction?(e) is the coenzyme for the thymidylate synthase reaction?(f) is not known to exist in nature?(g) is used in purine nucleotide synthesis?arrow_forward
- 3) Histone deacetylases (HDACs) are zinc-dependent enzymes that catalyse the conversion of acetyllysine to lysine. e) HN a) Propose the mechanism for the HDAC-catalysed reaction. b) What is the role of zinc ion in HDAC catalysis? c) d) f) HDAC NH₂ Draw the pH-activity profile for HDAC-catalysed conversion of acetyllysine to lysine. Explain. Suggest two acetyllysine analogues that are substrates for HDACs. One should be a better substrate than acetyllysine, whereas the other one should be a worse substrate than acetyllysine. Explain. Mutations in the HDAC sequence could lead to a loss of the catalytic function. Which mutations are problematic? Lysine acetylation is a reversible reaction using acetyl-CoA as a co-substrate. Which coenzymes are required for synthesis of acetyl-CoA in nature? Propose the mechanism.arrow_forwardCompare the pathways of purine and pyrimidine nucleotide synthesis with respect to (a) precursors, (b) energy cost, (c) acquisition of the ribose moiety, and (d) number of enzymatic steps.arrow_forwardWhich of the following regulatory mechanisms will specifically inhibit pyrimidine synthesis (and not also purine synthesis)? (A) allosteric regulation of aspartate transcarbamoylase by CTP(B) allosteric regulation of aspartate transcarbamoylase by ATP(C) synergistic inhibition of PRPP synthetase by AMP/GMP/IMP(D) synergistic inhibition of PRPP amidotransferase by AMP/GMP/IMP (E) feedback inhibition of ribonucleotide reductase by dATParrow_forward
- UDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order to catalyse the transfer of a glucuronic acid group from UDP-GA to a drug molecule, releasing UDP from the active site as a product. UDP is then regenerated by the activity of another enzyme. What terms could be used to describe UDP-GA?arrow_forwardAfter being stabilized with supplemental oxygen, a blood transfusion, and medication to help with the pain, JJ was prescribed the drug hydroxyurea to help increase the level of fetal hemoglobin (ay2) in the red blood cell. Though the exact pharmacological effect of hydroxyurea is unclear in the treatment of Sickle Cell Disease, it is known that the drug is an inhibitor of ribonucleotide reductase and acts to transiently inhibit deoxyribonucleotide synthesis in dividing cells. Q5: In which phase of the cell cycle does hydroxyurea produce its main effect?arrow_forwardDescribe two reasons why the reaction glutamine synthetase performs is important to the body.arrow_forward
- (a) Write a balanced equation for the conversion of aspartate into glucose through the intermediate oxaloacetate. Which coenzymes participate in this transformation? (b) Write a balanced equation for the conversion of aspartate into oxaloacetate through the intermediate fumaratearrow_forwardThe amount of glucose 6-phophate that is used by the glycolytic or pentose phosphate (b) pathways is determined by the current metabolic state of the cytosol. This regulation is achieved in part via allosteric regulation of the first committed step of the pentose phosphate pathway. (i) What metabolite is the key allosteric regulator of the pentose phosphate pathway, and what enzyme does this metabolite regulate? (ii) What happens to glucose 6-phopshate in the limiting case when this metabolite is in excess? (iii) What happens to glucose 6-phophate in the limiting case when this metabolite is absent?arrow_forward(a) What is the role of Glu 270 in catalysis? (b) What is the role of Arg 145 in catalysis?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
Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License