Essential Organic Chemistry, Global Edition
3rd Edition
ISBN: 9781292089034
Author: Paula Yurkanis Bruice
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
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.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
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
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.
Chapter 18 Solutions
Essential Organic Chemistry, Global 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
- What type of specificity (absolute, group, linkage, or stereochemical) is associated with each of the following enzymes? a. Sucrase b. A lipase c. A decarboxylase d. L-glutamate oxidasearrow_forwardThe enzyme that catalyzes reaction below can be classified as: NAD* NADH + H* Но- H-Ć- Н—с—н H- malate dehydrogenase Oxaloacetate Malatearrow_forwardAll inhibitors of eicosanoids act by inhibiting the cyclooxygenases * True Falsearrow_forward
- Oxaloacetate 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_forwardWhich class of enzymes trypsin belongs to?arrow_forwardTPP is a coenzyme for transketolase, the enzyme that catalyzes the conversion of a ketopentose (xylulose5-phosphate) and an aldopentose (ribose-5-phosphate) to an aldotriose (glyceraldehyde-3-phosphate) and a ketoheptose (sedoheptulose-7-phosphate). Notice that the total number of carbons in the reactants and products is the same (5 + 5 = 3 + 7). Propose a mechanism for this reaction.arrow_forward
- Chemistry Many drugs are competitive inhibitors of specific enzymes. For drugs that act as competitive inhibitors, the enzymes must be allosterically regulated. the substrate must be bound to the enzyme before the drug can bind. O the amount of drug needed to achieve the same effect is increased as the substrate concentration increases. the amount of drug needed to achieve the same effect is increased as the substrate concentration decreases.arrow_forwardMatch each enzyme with the correct substrate. Enzyme Substrate lactose maltose fumarate lactate pyruvate Answer Bank lactate dehydrogenase pyruvate carboxylase lactase maltase fumarasearrow_forwardWhy do we say the two enzyme-catalyzed reactions taking place in your test tube are "coupled"? O peroxidase and glucose oxidase utilize hydrogen peroxide as a substrate O peroxidase utilizes the lactone produced by glucose oxidase as a substrate O because there is a dye in solution O peroxidase and glucose oxidase utilize glucose as a substrate Operoxidase utilizes the hydrogen peroxide produced by glucose oxidase as a substrate Evaluatearrow_forward
- GR Methanol and ethanol bind to the same active site on the enzyme alcohol dehydrogenase (ADH) to undergo oxidation, as shown in the equations below. In methanol poisoning, ethanol is given intravenously to prevent the formation of formaldehyde that has toxic effects. In this scenario, what type of inhibitor is ethanol with regard to alcohol dehydrogenase catalyzing the oxidation of methanol? budy CH3-OH + NAD+ HCHO+NADH + H+ CH3-CH2-OH + NAD+ CH3-CHO + NADH + H* O a competitive inhibitor ADH O an irreversible inhibitor ADH O a noncompetitive inhibitor O both a noncompetitive and an irreversible inhibitor O Sea hparrow_forwardTPP is a coenzyme for transketolase, the enzyme that catalyzes the conversion of a ketopentose (xylulose- 5-phosphate) and an aldopentose (ribose-5-phosphate) to an aldotriose (glyceraldehyde-3-phosphate) anda ketoheptose (sedoheptulose-7-phosphate). Notice that the total number of carbons in the reactants and products is the same (5 + 5 = 3 + 7). Propose a mechanism for this reaction.arrow_forwardWhich coenzyme is responsible for the following reaction? ОН B12 one of the THF (tetrahydrofolate) coenzymes O FADH2 O TPP (thiamine pyrophosphate) NADH (or NADPH) O NAD+ (or NADP*) O KH2 O FAD O PLP (pyridoxal phosphate) hiotinarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
General, Organic, and Biological ChemistryChemistryISBN:9781285853918Author:H. Stephen StokerPublisher:Cengage Learning
Organic And Biological ChemistryChemistryISBN:9781305081079Author:STOKER, H. Stephen (howard Stephen)Publisher:Cengage Learning,
General, Organic, and Biological Chemistry
Chemistry
ISBN:9781285853918
Author:H. Stephen Stoker
Publisher:Cengage Learning
Organic And Biological Chemistry
Chemistry
ISBN:9781305081079
Author:STOKER, H. Stephen (howard Stephen)
Publisher:Cengage Learning,
Enzymes - Effect of cofactors on enzyme; Author: Tutorials Point (India) Ltd;https://www.youtube.com/watch?v=AkAbIwxyUs4;License: Standard YouTube License, CC-BY
Enzyme Catalysis Part-I; Author: NPTEL-NOC IITM;https://www.youtube.com/watch?v=aZE740JWZuQ;License: Standard Youtube License