Essential Organic Chemistry (3rd Edition)
3rd Edition
ISBN: 9780321937711
Author: Paula Yurkanis Bruice
Publisher: PEARSON
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Textbook Question
Chapter 18.8, Problem 14P
In succinate dehydrogenase, FAD is covalently bound to its enzyme as a result of a base removing a proton from the C-8 methyl group and an acid donating a proton to N-1. Then a hitstidine side chain of the enzyme adds to the methylene carbon at C-8 as a proton adds to N-5.Draw the mechanism for these two steps that lead to enzyme-bound FADH2.
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FAD is covalently bound to succinate dehydrogenase (the enzyme whose mechanism was shown on the previous page) as a result of a base removing a proton from the C-8 methyl group and an acid donating a proton to N-1. Then a histidine side chain of the enzyme adds to the methylene carbon at C-8 and a proton adds to N-5. Draw the mechanism for these two steps using B: _ and HB for the base and acid, respectively.
The enzyme 6-phosphogluconate dehydrogenase is part of the pentose pathway
for glucose oxidation. What enzyme that is involved in glucose oxidation by the
citric acid cycle has a very similar reaction mechanism to 6-phosphogluconate
dehydrogenase?
A) isocitrate dehydrogenase
B) alpha-ketoglutarate dehydrogenase
C) succinate dehydrogenase
D) malate dehydrogenase
E) pyruvate dehydrogenase
(99+
RATI
a
Which of the following reactions would best describe that catalytic activity of a dehydrogenase enzyme?
O The transfer of a hydronium ion from a substrate to NAD+ to generate NADH and an oxidized product
O The removal of an OH group from a substrate through the formation of water and a dehydrated product
O General acid-base chemistry
O An hydrolytic attack by an hydroxide bound Zn++ molecule
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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