carbons?6. Delineate the steps in the production by a human of a C20:3 45, 8, 11 fatty acid. Make sure yourscheme is metabolically plausible. For each step, list the enzymes, cofactors, and product(s).You may start from palmitate, if that is useful. If you require an alternate starting material,identify the material and explain why you chose that material.

Fatty acid metabolism includes Fatty acid biosynthesis (an anabolic process) and β- oxidation…

Answered: 6. Delineate the steps in the…

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

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ymes change their conformation after each reaction, therefore they can only be used once. OEnzymes can be proteins that can be denatured by changes in pH or temperature. D Question 37 A major difference between purine and pyrimidine biosynthesis is that pyrimidine: O are attached to the ribose sugar while being synthesized O are completely synthesized prior to attaching to the ribose sugar O are partially synthesized, the sugar is added, then synthesis is completed O do not have a sugar moiety Question 38 Which of the following is produced in largest numbers by the TCA cycle?
7
Please give the both answer.
Number 8
Amino acids are linked through peptide bonds to form proteins. This linkage of amino acids in the formation of proteins accomplished by [ Select ] reaction V [ Select ] Hydrolysis Fission Condensation Fusion
With one mole each of sucrose, and arginine: 1) rank these molecules in order of increasing energy production, 2) describe the metabolic pathways involved in producing ATP for each molecule, 3) approximate (and explain) and the number of Acetyl-Co A molecules that would be generated from each molecule.
Number 6
4. a. Calculate the KM (Michaelis constant) and the vmax (the maximum initial rate) for both substrates (sphingosine and ATP). Show your work, and be careful about units. b. threo-dihydrosphingosine, a stereoisomer of sphingosine, is an inhibitor of sphingosine kinase. What kind of inhibitor (competitive, uncompetitive, noncompetitive) is threo-dihydrosphingosine? Citing information from the Lineweaver-Burke plots, explain how you can tell.
8.Choose the False statement about enzyme binding sites Binding at an allosteric site ca affect binding and catalysis at the Ortho steric site. In addition to ortho steric sites , some enzymes have other sites where catalysis can be conducted. They are called , allosteric sites, from “allo,” the other. In principle, allosteric ligands can have structures that do not resemble those of substrates. Ligand binding at an allosteric site can cause a conformational change of an enzyme. Enzyme can be inhibited by an allosteric ligand that does not complete with substrate.
Two enzymes are being studied: the first enzyme E1, uses 2-tert-butyl-3- methylpentanopic acid as a substrate whereas the second enzyme E2, uses 2,3,4,5-tetraaminooctanoic acid as a substrate. Based on the lock-and-key model hypothesis, the active site of E, would be more * x with predominantly + x side chains and the active site of E2 would be more + x side chains
4. a. Use the data in the graph above to estimate a KM value for the enzyme in the presence of these metabolites, and enter them into the table below. b. Classify these metabolites as either activators or inhibitors, and explain your rationale below.
explain the correct and wrong choices

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