Essential Organic Chemistry (3rd Edition)
3rd Edition
ISBN: 9780321937711
Author: Paula Yurkanis Bruice
Publisher: PEARSON
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Question
Chapter 18.5, Problem 7P
Interpretation Introduction
Interpretation:
Side chain of amino acid that can form an imine with the substrate has to be identified.
Concept introduction:
Amino acids are the molecules which containing an
Amino acids are the basic structural building units of protein and other
An imine is a compound having
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Which of the following amino acid side chains can form an imine with a substrate?
In a typical amino acid zwitterion, the carboxylate end is
O neutral
O attached to an amine
O positively charged
soluble in a nonpolar solvent
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Which of the attached amines can be used to resolve a racemic mixture of amino acids?
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...
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Similar questions
- The 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 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_forwardLysine and tryptophan are two amino acids that contain an additional Natom in the R group bonded to the a carbon. While lysine is classified asa basic amino acid because it contains an additional basic N atom,tryptophan is classified as a neutral amino acid. Explain why thisdifference in classification occurs.arrow_forward
- 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_forward9. How do you know if a malenimide based reagent will conjugate to nitrogen or sulphur in an amino acid? но protein -protein SH NH2arrow_forwardWhich of the following amines can be used to resolve a racemic mixture of amino acids?arrow_forward
- Net charge and isoelectric point of an amino acid with an ionizable side group.Consider the net charge and isoelectric point of an amino acid with ionizable side (R-) group.(a) Identify the acidic amino acid(s) capable of having a negatively charged carboxyl side group.(b) Identify the basic amino acid(s) capable of having a positively charged amino side group.(c) For an amino acid with a side (R-) chain that can ionize to a negative charge, derive a general expression in terms of measured pH and known pKa values of α-carboxyla-amino (pKca), α-amino(pKaa),and side group (pKRa), respectively, for the net charge of an amino acid Consider the net charge and isoelectric point of an amino acid with ionizable side (R-) group.(d) For an amino acid with a side (R-) chain that can ionize to a positive charge, derive a general expression in terms of measured pH and known pKa values ofα-carboxyl (pKca), α-amino (pKaa), and side group (pKRa), respectively, for the net charge of the amino acid.(e)…arrow_forwardDraw the structure for each of the following peptides in their fully protonated forms. Indicate which protons are dissociable in the structure. a) Gly-Lys-Arg-Phe b) Y-D-S-C-Qarrow_forwardThe aminolysis of acetic anhydride will produce aniline and ammonia as major products. True or Falsearrow_forward
- Which of the following substituent is an ortho/para-directing activator and an ortho/para-directing deactivator? a amino group b halogen group c nitro group d carboxyl grouparrow_forwardThe reaction of an ester with an amine is not as slow as the reaction of an ester with water or an alcohol. Explain with reason. Explain why the rate of aminolysis of an ester cannot be increased by H+, OH- or OR-. How can you activate the carboxylic acid? Is acid catalyzed hydrolysis of acetamide a reversible or an irreversible reaction. Explain.arrow_forwardThe stability of our genetic code depends on the stability of DNA. We are fortunate that the aminoacetal linkages ofDNA are not easily cleaved. Show why your mechanism for part (a) does not work so well with deoxycytidine anddeoxyadenosine.arrow_forward
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