Essential Organic Chemistry (3rd Edition)
3rd Edition
ISBN: 9780321937711
Author: Paula Yurkanis Bruice
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Textbook Question
Chapter 18, Problem 37P
Explain why serine proteases do not catalyze hydrolysis if the amino acid at the hydrolysis site is a D-amino example, cleaves on the C-side of L-Arag and L-Lys, but not on the C-side of D-Arg and D-Lys.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Explain why serine proteases do not catalyze hydrolysis if the amino acid at the hydrolysis site is a d-amino acid. Trypsin, for example, cleaves on the C-side of L-Arg and L-Lys, but not on the C-side of D-Arg and D-Lys.
which amino acids has a side chain that can serve as a hydrogen bond donor but not acceptor in its predominant form at pH7
Draw three-dimensional representations of the following amino acids. Explain their structures.
(a) L-phenylalanine
(b) L-histidine
(c) D-serine
(d) L-tryptophan
Chapter 18 Solutions
Essential Organic Chemistry (3rd Edition)
Ch. 18.1 - Prob. 1PCh. 18.2 - If H218O were used to hydrolyze lysozyme, which...Ch. 18.3 - Which of the following amino acid side chains can...Ch. 18.3 - Arginine and lysine side chains fit into trypsins...Ch. 18.4 - Which of the following amino acid side chains can...Ch. 18.4 - Prob. 6PCh. 18.5 - Prob. 7PCh. 18.5 - Draw the mechanism for the hydroxide-ion-catalyzed...Ch. 18.5 - What advantage does the enzyme gain by forming an...Ch. 18.7 - Prob. 10P
Ch. 18.7 - Prob. 11PCh. 18.8 - How many conjugated double bonds are there in a....Ch. 18.8 - Instead of adding to the 4a-position and...Ch. 18.8 - In succinate dehydrogenase, FAD is covalently...Ch. 18.8 - Prob. 15PCh. 18.9 - Acetolactate synthase is another TPP-requiring...Ch. 18.9 - Acetolactate synthase can also transfer the acyl...Ch. 18.9 - Prob. 18PCh. 18.9 - Prob. 19PCh. 18.10 - Prob. 21PCh. 18.11 - Prob. 23PCh. 18.11 - Which compound is more easily decarboxylated?Ch. 18.11 - Explain why the ability of PLP to catalyze an...Ch. 18.11 - Explain why the ability of PLP to catalyze an...Ch. 18.12 - What groups are interchanged in the following...Ch. 18.13 - Why is the coenzyme called tetrahydrofolate?Ch. 18.13 - What amino acid is formed by the following...Ch. 18.13 - How do the structures of tetrahydrofolate and...Ch. 18.13 - What is the source of the methyl group in...Ch. 18 - Prob. 32PCh. 18 - Prob. 33PCh. 18 - From what vitamins are the following coenzymes...Ch. 18 - Prob. 35PCh. 18 - For each of the following reaction, name both the...Ch. 18 - Explain why serine proteases do not catalyze...Ch. 18 - Prob. 38PCh. 18 - For each of the following enzyme catalyzed...Ch. 18 - Trisephosphate isomerase (TIM) catalyzes the...Ch. 18 - Prob. 41PCh. 18 - What acyl groups have we seen transferred by...Ch. 18 - When UMP is dissolved in T2O, exchange of T for H...Ch. 18 - Prob. 44PCh. 18 - When transaminated, the three branched-chain amino...Ch. 18 - Aldolase shows no activity if it is incubated with...
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
- Estimate the pI of each tripeptide in Problem 27.46. Draw a structural formula of these tripeptides. Mark each peptide bond, the N-terminal amino acid, and the C-terminal amino acid. (a) Phe-Val-Asn (b) Leu-Val-Glnarrow_forward22-30 (a) Use the three-letter abbreviations to write a representation of the following tripeptide: (b) Which amino acid is at the C-terminal end, and which is at the N-terminal end?arrow_forwardWhy is amino acid activation called the second genetic code?arrow_forward
- (a) Draw the structure of the two possible dipeptides that can be formed by combining valine and phenylalanine. (b) In each dipeptide, label the N- and C-terminal amino acids. (c) Name each peptide using three-letter symbols.arrow_forwardDraw three-dimensional representations of the following amino acids.(a) l-phenylalanine (b) l-histidine (c) d-serine (d) l-tryptophanDraw three-dimensional representations of the following amino acids.(a) l-phenylalanine (b) l-histidine (c) d-serine (d) l-tryptophanarrow_forwardDraw three-dimensional representations of the following amino acids. l-histidinearrow_forward
- Write the complete structures for the following peptides. Tell whether each peptide is acidic, basic, or neutral.(a) methionylthreonine (b) threonylmethioninearrow_forwardWhat type of interaction (IMF) would be present between side chains of the following amino acid residues? Explain your answers. a) 2 phenylalanine residues b) Methionine and valine residues c) Glutamate and arginine residuesarrow_forwardDraw the amino acids and peptide fragments formed when the decapeptide A–P–F–L–K–W–S–G–R–G is treated with each reagent or enzyme: (a) chymotrypsin; 8 pt helvetica roman (b) trypsin; (c) carboxypeptidase; (d) C6H5N = C = S.arrow_forward
- Calculate the attraction between an arginine and glutamate at pH 7 under thefollowing conditions:a) in air, spaced 5 Å apartb) in water, spaced 5 Å apartc) in ethanol, spaced 5 Å apartarrow_forwardArginine and lysine side chains fit into trypsin’s binding pocket . One of these side chains forms a direct hydrogen bond with serine and an indirect hydrogen bond (mediated through a water molecule) with aspartate. The other side chain forms direct hydrogen bonds with both serine and aspartate. Which is which?arrow_forward
arrow_back_ios
arrow_forward_ios
Recommended textbooks for you
- Introduction to General, Organic and BiochemistryChemistryISBN:9781285869759Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar TorresPublisher:Cengage LearningOrganic And Biological ChemistryChemistryISBN:9781305081079Author:STOKER, H. Stephen (howard Stephen)Publisher:Cengage Learning,General, Organic, and Biological ChemistryChemistryISBN:9781285853918Author:H. Stephen StokerPublisher:Cengage Learning
- Chemistry for Today: General, Organic, and Bioche...ChemistryISBN:9781305960060Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. HansenPublisher:Cengage LearningOrganic ChemistryChemistryISBN:9781305580350Author:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. FootePublisher:Cengage Learning
Introduction to General, Organic and Biochemistry
Chemistry
ISBN:9781285869759
Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Publisher:Cengage Learning
Organic And Biological Chemistry
Chemistry
ISBN:9781305081079
Author:STOKER, H. Stephen (howard Stephen)
Publisher:Cengage Learning,
General, Organic, and Biological Chemistry
Chemistry
ISBN:9781285853918
Author:H. Stephen Stoker
Publisher:Cengage Learning
Chemistry for Today: General, Organic, and Bioche...
Chemistry
ISBN:9781305960060
Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen
Publisher:Cengage Learning
Organic Chemistry
Chemistry
ISBN:9781305580350
Author:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote
Publisher:Cengage Learning
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY