EBK ORGANIC CHEMISTRY STUDY GUIDE AND S
6th Edition
ISBN: 9781319385415
Author: PARISE
Publisher: VST
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 27, Problem 27.66AP
Interpretation Introduction
Interpretation:
The explanation for how the two aspartic acid residue of the enzyme reacts with the hydroxyl group which increases the binding efficiency of inhibitor is to be stated.
Concept introduction:
The amino acid is made of two
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
The activity of an enzyme requires a glutamic acid to display its -COOH
functional group in the protonated state. Suppose the pK, of the -COOH
group is 4.07.
(a) Will the enzyme be more active at pH 3.5 or 4.5? Explain.
(b) What fraction of the enzymes will be active at pH = 4.07? Explain.
(c) At what pH will the enzyme show 78% of maximal activity?
How can the Michaelis constant (Km) be identified and used to represent the affinity between the enzyme and the substrate?
An enzyme catalyzes the hydrolysis of an ester with a
certain activity, but this activity is lost in a 3 M urea
solution. What is the most likely explanation for the loss
of activity?
(A) Urea binds to the active site of the enzyme
competitively with the substrate.
(B) Urea causes the cleavage of the peptide bonds in the
enzyme.
(C) Urea causes the enzyme to denature and lose its
specific three-dimensional shape.
(D) Urea reacts with disulfide bonds in the enzyme.
Chapter 27 Solutions
EBK ORGANIC CHEMISTRY STUDY GUIDE AND S
Ch. 27 - Prob. 27.1PCh. 27 - Prob. 27.2PCh. 27 - Prob. 27.3PCh. 27 - Prob. 27.4PCh. 27 - Prob. 27.5PCh. 27 - Prob. 27.6PCh. 27 - Prob. 27.8PCh. 27 - Prob. 27.9PCh. 27 - Prob. 27.10PCh. 27 - Prob. 27.11P
Ch. 27 - Prob. 27.12PCh. 27 - Prob. 27.13PCh. 27 - Prob. 27.14PCh. 27 - Prob. 27.15PCh. 27 - Prob. 27.16PCh. 27 - Prob. 27.17PCh. 27 - Prob. 27.18PCh. 27 - Prob. 27.19PCh. 27 - Prob. 27.20PCh. 27 - Prob. 27.21PCh. 27 - Prob. 27.22PCh. 27 - Prob. 27.23PCh. 27 - Prob. 27.24PCh. 27 - Prob. 27.25PCh. 27 - Prob. 27.26PCh. 27 - Prob. 27.27PCh. 27 - Prob. 27.28PCh. 27 - Prob. 27.29PCh. 27 - Prob. 27.30PCh. 27 - Prob. 27.31PCh. 27 - Prob. 27.32PCh. 27 - Prob. 27.33PCh. 27 - Prob. 27.34PCh. 27 - Prob. 27.35PCh. 27 - Prob. 27.36PCh. 27 - Prob. 27.37PCh. 27 - Prob. 27.38PCh. 27 - Prob. 27.39PCh. 27 - Prob. 27.40PCh. 27 - Prob. 27.41PCh. 27 - Prob. 27.42PCh. 27 - Prob. 27.43APCh. 27 - Prob. 27.44APCh. 27 - Prob. 27.45APCh. 27 - Prob. 27.46APCh. 27 - Prob. 27.47APCh. 27 - Prob. 27.48APCh. 27 - Prob. 27.49APCh. 27 - Prob. 27.50APCh. 27 - Prob. 27.51APCh. 27 - Prob. 27.52APCh. 27 - Prob. 27.53APCh. 27 - Prob. 27.54APCh. 27 - Prob. 27.55APCh. 27 - Prob. 27.56APCh. 27 - Prob. 27.57APCh. 27 - Prob. 27.58APCh. 27 - Prob. 27.59APCh. 27 - Prob. 27.60APCh. 27 - Prob. 27.61APCh. 27 - Prob. 27.62APCh. 27 - Prob. 27.63APCh. 27 - Prob. 27.64APCh. 27 - Prob. 27.65APCh. 27 - Prob. 27.66APCh. 27 - Prob. 27.67APCh. 27 - Prob. 27.68APCh. 27 - Prob. 27.69APCh. 27 - Prob. 27.70APCh. 27 - Prob. 27.71APCh. 27 - Prob. 27.72APCh. 27 - Prob. 27.73APCh. 27 - Prob. 27.74APCh. 27 - Prob. 27.75APCh. 27 - Prob. 27.76APCh. 27 - Prob. 27.77APCh. 27 - Prob. 27.78APCh. 27 - Prob. 27.79APCh. 27 - Prob. 27.80APCh. 27 - Prob. 27.81APCh. 27 - Prob. 27.82APCh. 27 - Prob. 27.83AP
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
- Ethyleneimine reacts with cysteine side chains in proteins to form S - aminoethyl derivatives. The peptide bonds on the carboxyl side of these modified cysteine residues are susceptible to hydrolysis by trypsin . Why?arrow_forwardAlthough the bond energy for the hydrogen bond in a vacuum is estimated to be about 20 kJ/mol, we find that each hydrogen bond in a folded protein contributes much less--probably less that 5 kJ/mol--to the enthalpy of protein stabilization. Suggest an explanation for this difference. Explain briefly.arrow_forwardOutline the four general stages in an enzyme-catalyzedreaction.arrow_forward
- Hemoglobin A has a pI value of 5.6 whereas the variant hemoglobin M has an aspartate residue in place of the normal valine at position 85 of the alpha chain. What effect will this substitution have on the electrophoretic behavior of the protein at pH 7.0. (explain clearly the reason for your answer)arrow_forwardResearchers analysed a glycopeptide (a peptide carrying one or several oligosaccharide groups) and determined both the sequence of the peptide and the sequence of the sugar molecule. The latter was identified as a diholoside coupled to the peptide by an osidic bond. The systematic name of this sugar is: B-D-glucopyranosyl-(1→4)-ß-D-galactopyranose. : Represent the chemical formula of this diholoside in a way that all oses are Question 1 represented according to the Haworth convention. Apart from the furane and/or pyrane cycles all atoms of this molecule must be given.arrow_forwardSome proteases are cysteine proteases and threonine proteases as opposed to serine proteases. What properties of these amino acids residues allow them to be in a similar catalytic process? Cysteine: R=-CH2SH Threonine: R= -CH(CH3)OHarrow_forward
- A tripeptide contains lysine (R= -(CH₂)4NH₂), phenylalanine (R= -CH₂C6H5) and glycine (R= -H). It was found that the tripeptide reacts with 2 moles of DNFB to give compound A. When compound A was treated with SOCI2, glycine was activated. When hydrolyzed, both NH₂ groups of lysine were found to be DNP-labelled. What is the structure of the tripeptide? Select one: H (CH₂)2NH2 CH NH CH H₂N O O H₂N H₂N H₂N C (CH2)4NH2 CH 010 (CH2)4NH2 CH C=O CH,Ph CH NH NH NH CH CH,Ph CH H 010 CH CH,Ph CH (CH2)4NH2 ΝΗ NH NH NH CH,Ph CH H CH COOH H CH COOH COOH COOHarrow_forwardThe shown image is a reaction diagram for the hydrolysis of peptide bonds. Appropriately substituted phosphonates (structure shown above) were successfully designed as strong inhibitors for proteolytic enzymes. Explain why this strategy was successful. Note that the lengths of P–O bonds in phosphonates are significantly longer than the corresponding C–O bonds.arrow_forwardThe activity of sulphonamides is decreased if they are taken at the same time as procaine. Suggest why this might be the case. Explain, please.arrow_forward
- Glycine is a diprotic acid, which can potentially undergo two dissociation reactions, one for the a-amino group (-NH3), and the other for the carboxyl (-COOH) group. Therefore, it has two pKą values. The carboxyl group has a pK₁ of 2.34 and the a-amino group has a pK₂ of 9.60. Glycine can exist in fully deprotonated (NH₂-CH₂-COO-), fully protonated (NH3-CH₂-COOH), or zwitterionic form (NH3-CH₂-COO-). Match the pH values with the corresponding form of glycine that would be present in the highest concentration in a solution of th pH. fully deprotonated form NH,−CH,−COO- pH 11.9 pH 6.0 pH 8.0 fully protonated form NH3-CH₂-COOH pH 1.0 Answer Bank pH 7.0 zwitterionic form NH3-CH₂-COO-arrow_forwardplease explain What percentage of a side-chain sulfhydryl group of cysteine is protonated at pH 7.9?arrow_forwardThe pKaa of the conjugate acid of guanidine is 13.6, making it one of the strongest neutral organic bases. Offer an explanation.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
ChemistryChemistryISBN:9781305957404Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCostePublisher:Cengage Learning
ChemistryChemistryISBN:9781259911156Author:Raymond Chang Dr., Jason Overby ProfessorPublisher:McGraw-Hill Education
Principles of Instrumental AnalysisChemistryISBN:9781305577213Author:Douglas A. Skoog, F. James Holler, Stanley R. CrouchPublisher:Cengage Learning
Organic ChemistryChemistryISBN:9780078021558Author:Janice Gorzynski Smith Dr.Publisher:McGraw-Hill Education
Chemistry: Principles and ReactionsChemistryISBN:9781305079373Author:William L. Masterton, Cecile N. HurleyPublisher:Cengage Learning
Elementary Principles of Chemical Processes, Bind...ChemistryISBN:9781118431221Author:Richard M. Felder, Ronald W. Rousseau, Lisa G. BullardPublisher:WILEY
Chemistry
Chemistry
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Cengage Learning
Chemistry
Chemistry
ISBN:9781259911156
Author:Raymond Chang Dr., Jason Overby Professor
Publisher:McGraw-Hill Education
Principles of Instrumental Analysis
Chemistry
ISBN:9781305577213
Author:Douglas A. Skoog, F. James Holler, Stanley R. Crouch
Publisher:Cengage Learning
Organic Chemistry
Chemistry
ISBN:9780078021558
Author:Janice Gorzynski Smith Dr.
Publisher:McGraw-Hill Education
Chemistry: Principles and Reactions
Chemistry
ISBN:9781305079373
Author:William L. Masterton, Cecile N. Hurley
Publisher:Cengage Learning
Elementary Principles of Chemical Processes, Bind...
Chemistry
ISBN:9781118431221
Author:Richard M. Felder, Ronald W. Rousseau, Lisa G. Bullard
Publisher:WILEY