Pyruvate dehydrogenase kinase (PDH kinase) catalyzes the phosphorylation of a specific Ser residue on the E1 subunit of the enzyme,rendering it inactive. One strategy to treat a pyruvate dehydrogenase deficiency disease involves administering dichloroacetate, acompound that inhibits pyruvate dehydrogenase kinase. How might this strategy be effective?The activity of the pyruvate dehydrogenase complex can be enhanced by inhibiting the kinase.O The activity of the pyruvate dehydrogenase complex can be enhanced by phosphorylation.O The activity of the pyruvate dehydrogenase complex can be enhanced by increasing concentrations of PDH kinase.O None of the above.

Pyruvate dehydrogenase catalyzes the link reaction between glycolysis and the TCA cycle. Pyruvate…

Answered: Pyruvate dehydrogenase kinase (PDH…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

See similar textbooks

Similar questions

Regulation of the pyruvate dehydrogenase complex (PDH) is dependent on indicators of energy charge (i.e. ATP/ADP ratio) and redox status (i.e. NADH/NAD* ratio). Answer the following questions about regulation of the PDH. a. The PDH is subject to regulation by a kinase and a phosphatase. Upon phosphorylation by the kinase, activity of PDH is reduced. Removal of the phosphoryl by the phosphatase increases activity of PDH. For the following metabolites, select whether the kinase that acts upon PDH is likely to be allosterically activated or inhibited by the molecule. ATP: [Select] NADH: [Select] b. When oxygen is depleted, the electron transport chain does not flow. What effect would these conditions have on activity of the PDH and why? (note, superscript does not work in the dropdown menu so NAD+ = NAD*) What effect?: [Select] Why?: [Select]
Which of the following is true about comparing the α-ketoglutarate dehydrogenase complex and the pyruvate dehydrogenase complex? Group of answer choices They catalyze reactions that produce the exact same set of products They are both dehydrogenase complexes, but have very different structures They both catalyze reactions that oxidize NADH to NAD+ They both use the same E3 enzyme component Which of the following best describes stage 2 of the citric acid cycle? Group of answer choices ATP production by the electron transport chain production of acetyl CoA regeneration of oxaloacetate release of 2 carbons as carbon dioxide
Enzyme 1 is Aconitase and the starting material goes through both the hydration and dehydration mechanism. I just need help with enzyme 2 and intermediate B, thank you
A patient exhibiting all the symptoms of beriberi is placed on a thiamine-enriched diet; however, the symptoms do not disappear. Genetic screening suggests a defect in pyruvate dehydrogenase phosphatase. Briefly explain why the genetic defect caused beriberi symptoms andy why thiamine supplementation had no effect.
Order the cofactors based on their use in the mechanism of the a-etogluterate dehydrogenase complex. 1. Stabilizes a carbanion due to decarboxylation 2. Allows for the splitting of the carbon skeleton from the electron pair generated in a redox reaction 3. Enzyme bond electron carrier that is part of dihydrolipoyl dehydrogenase 4. Final electron acceptor in the overall reaction catalyzed by this complex 1 2 3 4 answer choices: lipoamide, biotin, 2 Fe - 2S cluster, TPP, NAD+, FAD
Draw a plausible mechanism for the oxidation of dihydrolipoamide to lipoamide by the E3 subunit (dihydrolipoamide dehydrogenase) of pyruvate dehydrogenase complex.
Fatty acid oxidation for energy yield occurs in the mitochondrial matrix, and for palmitate as one example, generates [FADN2, NADH, and Acetyle-CoA or FADH, GTP, and NADPH] , all of which can be converted to ATP (108 of them to be exact) via oxidative phosphorylation. This is a [greater or smaller] yield of ATP per carbon atom compared to glucose. Ketogenesis is a process where acetyl-CoA (including that from breakdown of fatty acids) is converted to ketone bodies under conditions where carbohydrates are [in excess or liminting] . Acetoacetate and D-beta-hydroxybutyrate are delivered from liver to the blood stream where they provide energy for [cardiac and skeletal muscle as well as brain or synthesis of glycogen] . [Insulin or glucagon] promotes ketogenesis by stimulating fatty acid export from adipose tissue.
Pyruvate dehydrogenase kinase-4 (PDK-4) is a widely expressed isoform of PDK and is responsible for inhibiting pyruvate dehydrogenase (PDH) complex activity via phosphorylation. When PDK-4 is active, the PDH complex is in its phosphorylated state and pyruvate cannot be converted into acetyl-CoA for entry into the citric acid cycle. Instead, in gluconeogenic tissues like liver and kidney, pyruvate is channeled to support gluconeogenesis. Conversely, when PDK-4 is inactive, the PDH complex readily converts pyruvate into acetyl-CoA. A researcher wants to determine the role of PDK-4 on blood glucose homeostasis. To accomplish this, she proposes to generate a PDK-4 knockout mouse using CRISPR technology. To create the knockout mouse, she must first generate PDK-4 knockout embryos to implant into pseudopregnant female mice. Arrange the steps to outline the process by which she will generate the PDK-4 knockout embryos. First step Last step Answer Bank Generate Cas9 mRNA and sgRNA specific to…
Given 1 molecule of maltose considering the malate-aspartate shuttle. Identify the following:1. Total number of glucose molecules entering glycolysis2. Total number of pyruvate molecules produces at the end of glycolysis3. Total number of mitochondrial NADH produced after pyruvate is acted upon pyruvate dehydrogenase complex4.Total number of CO2 released right after the pyruvate dehydrogenase complex reaction5. Total number of acetyl coA molecules entering the citric acid cycle6. Total number of net cytosolic ATP molecules produced right after glycolysis7. Total number of all NADH molecules produced after complete oxidation8.Total number of all FADH2 molecules produced after complete oxidation9. Total number of all mitochondrial GTP molecules produced10. Total number of net ATP molecules produced after complete oxidation
The pyruvate dehydrogenase (PDH) complex catalyzes the oxidative decarboxylation of pyruvate to acetyl‑CoA and CO2.CO2. Multiple copies of pyruvate dehydrogenase (E1), dihydrolipoyl transacetylase (E2), and dihydrolipoyl dehydrogenase (E3) along with five cofactors form the PDH complex. Biochemists have studied the PDH complex for decades, in part due to its interesting use of substrate channeling during catalysis. What is the molecular mechanism of substrate channeling in the PDH complex? A. The swinging lipoyllysyl arm of E2 carries electrons and an acetyl group from E1 to E2. B.The active sites of E1, E2, and E3 undergo conformational changes that move products of one reaction to their next position without solvent exposure. C.Electrons and an acetyl group travel between E1 and E2 through a tunnel in E2. D. Metal ions coordinated with thiamine pyrophosphate (TPP) in E1 shield the electrons and acetyl group from scavenging by other enzymes until they reach E3.
ATP, like ADP and AMP, is a competitive inhibitor of NADH binding to malate dehydrogenase. Provide a structural explanation for this inhibition.
During Krebs cycle, the conversion of isocitrate to alpha-keto glutarate involves all of the following reactions/mechanisms except Reduction of isocitrate Reduction of NAD+ Decarboxylation of isocitrate Oxidation of isocitrate

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS