In the first cycle of fatty acid synthesis via the acyl carrier protein system, the acetyl group on fatty acid synthase condenses withthe malonyl-ACP complex. Draw the structure of the products of this reaction.·Represent ACP by R1. Do not include the free synthase in your drawing.• Be sure to include charges on atoms at pH = 7.• Draw one structure per sketcher. Add additional sketchers using the drop-down menu in the bottom right corner.·Separate multiple products using the + sign from the drop-down menu.?n []

In this reaction:The acetyl group is denoted as CH3-C(=O)-S-R1.The malonyl-ACP is represented as…

Answered: In the first cycle of fatty acid…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter26: Synthesis And Degradation Of Nucleotides

Section: Chapter Questions

Problem 18P

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Protease enzymes cleave proteins by hydrolyzing peptide bonds. The strategy for each type of metalloprotease begins with generating a nucleophile that attacks the peptide bond that attacks the peptide carbonyl group. O Macmillan Learning On the basis of the information provided in the figure, show the next step in the mechanism for peptide-bond cleavage by a metalloprotease. Metalloproteases H R₁ HN Zn Enz 2+ R₂ Draw curved arrows on the pre-drawn structures to show the metalloprotease mechanism. If you need to reset the structures, click More followed by Reset Drawing. Select Draw Templates Groups More B - H Enz H H с R1 | : HN O | Zn 2+ B R2 N Zn Erase
Shown below is a substrate for a Trypsin. Draw the mechanism for this serine protease using the artificial substrate. Be sure to draw the catalytic triad, and show the role of the oxyanion hole. Draw the complete structure of every intermediate and product and PUSH ARROWS!!!!! Do not abbreviate structures using R and R' H₂N _N_CH. сно CH₂ CH₂ CH₂ NH d=19H₂ NH₂ O CH- H₂C HN O CH
complete the following mechanism showing the cleavge of the peptide bond for the following cysteine protease reaction. you only need a catalytic dyad for cystein proteases because the pKa of cysteine is low enough (8) and close enough to the pH of 7.4 that is can easily be deprotonated by histidine.
Image
• Draw the 2 anomeric ring structures for D-glucose, using CHO the information in the straight- н-с -он Но -с —н chain structure provided. In your Н-с -он figure, number each of the C Н-с -он 1. ČH,OH atoms, and show the position of every OH group.
Malonyl-ACP is a precursor in fatty acid synthesis in the acyl carrier protein pathway. Draw the structure of malonyl-ACP No stereochemistry required Represent ACP by R1 and be sure to include charges on atoms at ph=7
Consider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number (1, 2, 3, etc) represents an enzyme. Draw arrows indicating all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway.
Use the given experimental data to deduce the sequence of anoctapeptide that contains the following amino acids: Ala, Gly (2 equiv),His (2 equiv), Ile, Leu, and Phe. Edman degradation cleaves Gly from theoctapeptide, and carboxypeptidase forms Leu and a heptapeptide. Partialhydrolysis forms the following fragments: Ile–His–Leu, Gly, Gly–Ala–Phe–His, and Phe–His–Ile.
Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?
5) Consider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number over an arrow (1, 2, 3, etc) represents an enzyme that catalyzes that reaction (so enzyme 2 catalyzes the conversion of B to C). Indicate all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway. please indicate each interaction in the format example: "X will inhibit enzyme 27".
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