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…

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter4: Cells

Section: Chapter Questions

Problem 1ITD

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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
1. Consider the three-dimensional model of the tertiary structure of an enzyme below. Amino acids involved in binding are shaded blue, and amino acids involved in catalysis are shaded red. A. Suppose research has shown that amino acid 82 in the red shaded region is lysine, an amino acid with a positively-charged side chain. This lysine is critical for catalysis. Other studies have found that amino acids 12 and 62 in the blue region are both phenylalanine, an amino acid with a nonpolar side chain, and are critical for substrate binding. These amino acids are relatively close in the active site but are separated by 20-70 amino acids in the primary structure. Using what you know about protein structure, explain how amino acids separated in the primary structure can come close together in the active site. B. Use this information and figure 4.2 in your book to answer the following questions: Do you think changing amino acid 82, lysine, an amino acid with a positively-charged side…
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• 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
1. Give TWO (2) examples of sterols responsible for the synthesis of Vitamin D. How these sterols can be converted into Vitamin D? 2. Geranylgeranyl pyrophosphate (GGPP) is a universal precursor for all diterpene/diterpenoids. How GGPP is converted to linear, monocyclic, bicyclic and tricyclic diterpene/diterpenoids? Explain.
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.
3. Below is an image of sucrose. HO OH OH HO- HO OH OH НО (a) Using sucrose as a substrate, draw a schematic reaction for a general glycosidase. Explain whether your mechanism corresponds to an inverting or a retaining type enzyme. C :) (b) The two products can occur in a range of forms in solution. How many forms might you expect in this case, and explain how these interconvert. C 2
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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