EBK ORGANIC CHEMISTRY STUDY GUIDE AND S
6th Edition
ISBN: 9781319385415
Author: PARISE
Publisher: VST
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Chapter 27, Problem 27.64AP
Interpretation Introduction
Interpretation:
The explanation as to how trypsin-catalyzed hydrolysis with the chymotrypsin-trypsin mixture is avoided without separation of the two enzymes is to be stated.
Concept introduction:
Trypsin is an enzyme that is found in the
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The following data were recorded from an experiment to measure the activity of a peptidase
enzyme. A number of solutions of different concentrations of a dipeptide were prepared then the
same small amount of the enzyme was added to each of them. The rate of cleavage of the peptide
bond was measured and the initial rate of the reaction was recorded
Peptide conc
(mmol L-¹)
0.334
0.450
0.667
1.00
1.33
1.67
Initial rate
0.152
0.201
0.269
0.417
0.505
0.667
(mmol L¹ s¹)
For the peptidase enzyme find the maximum velocity and the Michaelis constant.
What are the three forms of regulation that follow the Michaelis Menten kinetics? What are the mechanisms by which
these inhibitors can regulate the enzyme?
Chorismate mutase is an enzyme that promotes a pericyclic reaction by forcing the substrate to assume the conformation needed for the reaction. The product of the pericyclic reaction is prephenate that is subsequently converted into the amino acids phenylalanine and tyrosine. What kind of a pericyclic reaction does chorismate mutase catalyze?
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
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- Which one will make the largest contribution to hydrophobic interactions via LDFs within the active site of an enzyme?arrow_forwardOutline the four general stages in an enzyme-catalyzedreaction.arrow_forwardThe hydrolysis of an ester can be sped up by both acidic and basic conditions. Aminolysis of an ester can be sped up by acidic conditions, but not by basic conditions. Explain why.arrow_forward
- Some 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_forwardMany peptides react further after synthesis (process is called post-translational modification). In this example a cysteine cyclizes to form a thiazole ring in Sanguinamide A. O= HN HN" SH -H₂O o= HN" 0= 0= N₂ S HN Sanguinamide Aarrow_forwardHow can the Michaelis constant (Km) be identified and used to represent the affinity between the enzyme and the substrate?arrow_forward
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