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 18.4, Problem 5P
Which of the following amino acid side chains can help remove a proton from the α-Carbon of an
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Which of the following amino acid side chains can aid the departure of a leaving group?
Which of the following amino acid's side chains will become protonated and carry a +1 charge when the pH of its environment is decreased from pH 11.5 to pH 7.5?
Glutamate
Lysine
Arginine
Histidine
Aminotransferases require Mg2+ ion as a cofactor.True or False?
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
- 22-71 Which amino acid side chain is most frequently involved in denaturation by reduction?arrow_forwardAn amino acid residue side chain is deprontonated at pH9.5. What is the pKa of this residue if it is fully deprotonated at this pH?arrow_forwardTyrosine is an amino acid whose side chain has a pKa of 10.1. At pH 7, what protonation form would you expect to find it in?arrow_forward
- Carboxypeptidase requires a Zn²+ cofactor for the hydrolysis of the peptide bond of a C-terminal aromatic amino acid. T/F?arrow_forwardExplain why, when the guanidino group of arginine is protonated, the double-bonded nitrogen is thenitrogen that accepts the proton. 2 H+ + NH2NHCH2CH2CH2CHNH +NH3CO−O CO−O H2NC NHCH2CH2CH2CHarrow_forwardDraw the structure of the amino acid L-leucine at each pH: (a) 6; (b) 10; (c) 2. Which form predominates at L-leucine's isoelectric point?arrow_forward
- What is the predominant form of the following amino acids at pH= 1? What is the overall charge on the amino acid at this pH? threoninearrow_forwardWhat is the predominant form of the following amino acids at pH= 1? What is the overall charge on the amino acid at this pH? argininearrow_forwardwould chymotrypsin to be most active at a pH of 4.5, 7.8, or 10.0?arrow_forward
- Although tryptophan contains a heterocyclic amine, it is considered a neutral aminoacid. Explain why the indole nitrogen of tryptophan is more weakly basic than one ofthe imidazole nitrogens of histidine.arrow_forwardsuggest a plausible arrow-pushing mechanism for the formation of a covalent adduct between the suicide inhibitor 5-trifluoromethyluridylic acid and thymidylate synthase that involves the active_site thiolate.arrow_forwardShow how the following amino acids might be formed in the laboratory by reductiveamination of the appropriate a@ketoacid.(a) alanine (b) leucine (c) serine (d) glutaminearrow_forward
arrow_back_ios
SEE MORE QUESTIONS
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 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
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY