Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Chapter 26, Problem 36P
Interpretation Introduction
Interpretation:
The mechanism for the production of methylamine from dimethylamine that is catalyzed by cytochrome P450 should be determined.
Concept introduction:
Enzymes that are produced from the cytochrome P450 genes usually facilitate the synthesis and
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Chapter 26 Solutions
Biochemistry
Ch. 26 - Prob. 1PCh. 26 - Prob. 2PCh. 26 - Prob. 3PCh. 26 - Prob. 4PCh. 26 - Prob. 5PCh. 26 - Prob. 6PCh. 26 - Prob. 7PCh. 26 - Prob. 8PCh. 26 - Prob. 9PCh. 26 - Prob. 10P
Ch. 26 - Prob. 11PCh. 26 - Prob. 12PCh. 26 - Prob. 13PCh. 26 - Prob. 14PCh. 26 - Prob. 15PCh. 26 - Prob. 16PCh. 26 - Prob. 17PCh. 26 - Prob. 18PCh. 26 - Prob. 19PCh. 26 - Prob. 20PCh. 26 - Prob. 21PCh. 26 - Prob. 22PCh. 26 - Prob. 23PCh. 26 - Prob. 24PCh. 26 - Prob. 25PCh. 26 - Prob. 26PCh. 26 - Prob. 27PCh. 26 - Prob. 28PCh. 26 - Prob. 29PCh. 26 - Prob. 30PCh. 26 - Prob. 31PCh. 26 - Prob. 32PCh. 26 - Prob. 33PCh. 26 - Prob. 34PCh. 26 - Prob. 35PCh. 26 - Prob. 36PCh. 26 - Prob. 37PCh. 26 - Prob. 38PCh. 26 - Prob. 39PCh. 26 - Prob. 40PCh. 26 - Prob. 41PCh. 26 - Prob. 42PCh. 26 - Prob. 43PCh. 26 - Prob. 44PCh. 26 - Prob. 45PCh. 26 - Prob. 46PCh. 26 - Prob. 47P
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- B- Vitamins are converted readily into important metabolic cofactors. Deficiency in any one of them has serious side effects. a. The disease beriberi results from a vitamin B 1 (Thiamine) deficiency and is characterized by cardiac and neurological symptoms. One key diagnostic for this disease is an increased level of pyruvate and α-ketoglutarate in the bloodstream. How does this vitamin deficiency lead to increased serumlevels of these factors? b. What would you expect the effect on the TCA intermediates for a patient suffering from vitamin B 5 deficiency? c. What would you expect the effect on the TCA intermediates for a patientsuffering from vitamin B 2 /B 3 deficiency?arrow_forwardPyruvate is accepted into the TCA cycle by a “feeder” reaction using the pyruvate dehydrogenase complex, resulting in acetyl-CoA and CO2. Provide a full mechanism for this reaction utilizing the TPP cofactor. Include the roles of all cofactors.arrow_forwardMap out all of the metabolic pathways in the liver cell. Draw out the structures and names of all compounds neatly by hand and the pathways responsible for metabolizing them. Some examples are: Glycolysis/gluconeogenesis, PPP, Glycogenesis/glycogenolysis, Krebs, ETC, selectamino acid pathways (Ala, Glu, Asp) Lipogenesis/lipolysis. Citrate/MAS/glycerol phosphate shuttlesystems, and the Cori/Glc-Ala cycles. Rules:-Draw both a mitochondrial area of metabolism and a cytoplasmic area of metabolism.-Draw the liver and its roles in glucose recycling (Cori cycle/Glc-Alanine recycling)-Avoid drawing the same molecule twice (except for separate mitochondrial/cytoplasmic populations. i.e. Design the PPP/Glycolysis so that GAP is only drawn once)-Label Carbon 4 of glucose and highlight where you would expect to find it in EVERY compound in whichit is present.-Have one or two locations for NADH/NADPH/ATP/GTP/CoQH2 – many arrows will come to/from thesespots.arrow_forward
- a. Draw the Krebs Cycle and show the entry points for the amino acids Alanine,Glutamic Acid, Asparagine, and Valine into the Krebs Cycle. (Include name of Enzymes involved) b. How many rounds of Krebs will be required to waste all Carbons of Glutamic Acid as CO2? (Show by drawing out the mechanism that occurs)arrow_forwardThe malate-aspartate shuttle allows malate to be exchanged for aspartate acrossthe inner mitochondrial membrane. (a) Describe the role of the malate-aspartate shuttle in liver cells under HIGHblood glucose conditions. Be sure to explain your answer. (b) Describe the role of the malate-aspartate shuttle in liver cells under LOW blood + glucose conditions.arrow_forward(a) Write out the net reaction, calculate ∆E ̊' for the reaction, and calculate the standard free-energy change (∆G°') for the overall oxidation/reduction reaction. (h) How many moles of ATP could theoretically be generated per mole of FADH2 oxidized by this reaction, given a ∆G ̊' of ATP synthesis of + 31 kJ/mol? How many moles of ATP could be generated per mole of FADH2 oxidized by this reaction under more typical cellular conditions (where ∆G' of ATP hydrolysis is ~ -50 kJ/mol)? Be sure to show your work and explain your answer.arrow_forward
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