Essential Organic Chemistry (3rd Edition)
3rd Edition
ISBN: 9780321937711
Author: Paula Yurkanis Bruice
Publisher: PEARSON
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Chapter 18.12, Problem 27P
What groups are interchanged in the following enzyme-catalyzed reaction that requires coenzyme B12?
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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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- Please solve it asaparrow_forwardIdentify the class and sub-class of the enzyme on the given enzyme-catalyzed reactionarrow_forwardConsider the following reaction: H-C-O-P-O CH2 0- OH C-O-P-0- Leaving Group CH2 0- • What is the leaving group? • What is the enzyme classification for the enzyme that catalyzes this reaction? ptsarrow_forward
- Identify the modes of catalysis and when / why they occur• Acid-base • Covalent• Transition state stabilization• Catalysis by proximity • Catalysis by strain• Lock & key is better seen as describing substrate binding to active sitearrow_forwardMatch each enzyme class to the type of reactions catalyzed. Enzyme Class [11][ Type of Reactions Catalyzed reactions involving the transfer of a functional group from one molecule to another energetically unfavorable reactions that require ATP to form new bonds oxidation-reduction reactions reactions that eliminate or form a double bond hydrolysis reactions isomerization reactions hydrolase Answer Bank transferase ligase lyase isomerase oxidoreductasearrow_forwardThe image at right shows which of the following aspects of enzymatic catalysis? the lock and key model of catalysis the induced fit model of catalysis allosteric activation of the enzyme the formation of the catalytically competent ES complex a favorable interaction of the substrate with the enzyme active site Substrate Enzyme E-S complexarrow_forward
- What are the products for the chemical reaction of C2H5OH+O2—->arrow_forwardAcetylcholine esterase is an important enzyme in neural synaptic signal transmission. It breaks down the neurotransmitter acetylcholine after it binds the acetylcholine receptor. Its active site has the same features used by serine proteases. Here is the reaction catalyzed by Acetylcholine esterase: Acetylcholine Choline OH Acetate + H Acetylcholine is an ester, while peptide bonds cleaved by proteases are amides. How should acetylcholine estease's mechanism accommodate this? This cannot be determined from the information presented in class and in this question. For amides, the amide nitrogen is deprotonate to make it more like an ester. The same mechanism cleaves deprotonated amides and esters. No changes are needed. The mechanism same works for esters and amides. Prior to cleavage, a transamination converts the ester to an amide. The esterase will make a covalent intermediate to an amine to create the amide to be cleaved.arrow_forwardEnzymes are categorized by the types of reactions that they catalyze. An enzyme that catalyzes the reaction shown below would be a HO HO CH3 مصر A) isomerase B) ligase C) hydrolase CH3 D) oxidoreductase E) transferase CH3 CH3 CH3 CH3 CH3 CH3arrow_forward
- 13. A specific enzyme will usually only catalyze one particular reacton. True Falsearrow_forwardOxaloacetate is an inhibitor of succinate dehydrogenase because it is structurally very similar to succinate as shown below. Also, its binding to the enzyme does not involve any covalent bond formation. What type of inhibitor is oxaloacetate? COO | CH₂ 1 CH₂ 1 COO Succinate COO | CH₂ C=O COO Oxaloacetate O a noncompetitive inhibitor both a noncompetitive and an irreversible inhibitor O an irreversible inhibitor O a competitive inhibitorarrow_forwardA flavin-dependent enzyme catalyzes the transformation shown below. NH₂ FAD NH₂ a) Circle the specific class of enzymes below to which this flavin-dependent enzyme most likely belongs. oxidase monooxygenase (FMO) b) Circle the co-substrate this enzyme requires for activity. NAD(P)+ NAD(P)H c) Circle the co-product this enzyme produces. H₂O H₂O2 Baeyer-Villiger monooxygenase (BVMO) reductase no co-substrate required Neither d) Provide a complete curved-arrow mechanism for the transformation shown above. You should draw all reaction intermediates in their most stable resonance form wherever possible. Be sure your mechanism shows the formation of all co-products. You may continue your mechanism onto the next page if necessary.arrow_forward
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DIGESTER-35 | VITAMINS AND THEIR RELATED COENZYMES| GPAT | NIPER | PHARMACIST| DI; Author: GPAT DISCUSSION CENTER;https://www.youtube.com/watch?v=CGrdNYmho0s;License: Standard YouTube License, CC-BY