In biochemistry laboratories, phenylmethylsulfonyl fluoride (PMSF) is a serine proteaseinhibitor commonly added to cell homogenates to protect proteins from digestion formserine proteases that are released when cell membranes and cell organelles arebroken.=S-FPMSF: phenylmethylsulfonyl fluoride1. Based on our discussion of covalent inhibition of acetylcoline, esterase bydiisopropylfluorophosphate, predict the effect of PMSF on chymotrypsin and predict howPMSF will modify the chymotrypsin active site. Justify your answer based on thepropertied of the active sites of the enzymes.

In order to understand how PMSF (Phenylmethylsufonyl fluoride) inhibits chymotrypsin, we need to…

Answered: In biochemistry laboratories,…

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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What step ends the first-half of the chymotrypsin mechanism? Attack of water on the acyl-enzyme intermediate. Selected Collapse of the first tetrahedral intermediate, releasing of the C-terminal peptide fragment and formation of the acyl-enzyme intermediate. Deprotonation of serine by the histidine. Collapse of the second tetrahedral intermediate leading to the final products. REVIEW QUESTION 1/1 CONTINUE MacBook Pro https://virginiacommonwealth.instructure.com/courses/42082/assignments/271397 esc OT
the structures of chymotrypsin and other serine proteases revealed that the active sites of these enzymes shared a particular sterochemical arrangement of residues crucial to their activity. This came to be known as the catalytic triad, as it consisted of the oponyomous serine (Ser) residue, along with a histidine (His) and an aspartate (Asp) residue. Which of the following would result in the greatest decrease in function of the catalytic triad found in serine proteases? O Mutation to Ser, Cys, Asp O Mutation to Ser, His, Asp O Mutation to Cys, His, Asp O Mutation to Ser, His, Glu
Can you please order the following steps involving the regeneration of ribonucleotide reductase that occurs in most animals so that it may carry out the formation of deoxyribonucleotides. (Note that not all steps are shown.) 1. Reduction of thioredoxin 2. Reduction of ribonucleotide reductase 3. Oxidation of thioredoxin reductase 4. Reduction of thioredoxin reductase
Describe the mechanism of action of 1 cycle of the ubiquitin (Ub) ligase system. Describe how the E1, E2 and E3 ligases work to covalently link Ub to the target protein, including which uses an energy source (and how), and the operative amino acids on the enzymes, Ub and target protein
A lipase enzyme has been isolated from a bacterium with a strong red color, found in industrial waste from a fishing company. This enzyme has great potential for elaboration of degreasers for industrial use as it can work at a wide range of temperature (between 4 ° and 80 ° C). However, it is estimated that its purity for industrial purposes is only 35% since it is contaminated with a low molecular weight protein that binds the smallest red pigment peptides and salts product of the purification process 1- Propose a methodology to increase the degree of purity of this enzyme, eliminatingsmall proteins and color.2- How it is ensured that the degree of purity of the enzyme has increased.
Azathioprine is an immunosuppressant drug used in kidney transplants. In vivo, azathioprine is metabolized to the hypoxanthine analog 6- mercaptopurine, which is then converted into 6-mercaptopurine ribose monophosphate, the active form of the drug. 6- Mercaptopurine ribose monophosphate also inhibits de novo purine synthesis, reducing uric acid levels in the blood and urine. However, when administered to Lesch – Nyhan patients, there was no effect on uric acid levels. Explain why this is the case.
Which of the following statements are descriptions of metal ion catalysis or examples of metal ion catalysis? Choose all correct answers a Zn²+ cofactor may properly orient the substrate in the active site through ionic interactions. a covalent bond forms between enzyme and substrate lowers the energy or stabilizes the transition state or intermediate catalyst retains its original form after reaction occurs catalysts may participate in oxidation-reduction reactions by changes in the oxidation state
Consider the metabolic pathway show below that converts substrate A to B with the enzyme A-ase, B to C with B-ase(I), and so forth. Acety/A-ase Acetate - A-ase Deacetylase A-ase Protease & C-ase B-ase ABCD What is the mechanism of regulation of B-ase? Positive allostery Reversible Covalent modification Isoenzymes Proteolytic Activation Feedback Inhibition 1
ATP synthase is a protein that catalyzes the formation of the energy storage molecule adenosine triphosphate using adenosine diphosphate and inorganic phosphate. Which of the following are true for the protein, ATP synthase? Select all apply A mutation of Asp61 to glutamic acid would have less of a deleterious effect on its ability to synthesize ATP than a mutation of Asp61 to alanine A mutation of Asp61 to alanine would have less of a deleterious effect on its ability to synthesize ATP than a mutation of Asp61 to glutamic acid The F1 subunit is primarily responsible for translocating H+ ions across the inner mitochondrial membrane during ATP synthesis The FO subunit is primarily responsible for translocating H+ ions across the inner mitochondrial membrane during ATP synthesis
The purified OXA-M290 enzyme can now be tested to determine which β-lactamase inhibitor is most effective. This inhibitor could be prescribed in combination with a β-lactam antibiotic to treat the infection caused by the E. coli KGH1 strain. Before testing inhibitors against OXA-M290, the kinetic activity of this enzyme must first be measured. The activity of OXA-M290 is measured using nitrocefin, a chromogenic β-lactam antibiotic. When nitrocefin is hydrolyzed by a β-lactamase, it changes from yellow to red in colour. The nitrocefin hydrolysis product has an extinction coefficient of 20,500 M-1 cm-1 at 486 nm. The hydrolysis of 60 μM nitrocefin by 1 nM OXA-M290 is monitored using a microplate reader. The absorbance of the wells in the plate is measured at 486 nm every 30 seconds. This experiment is carried out with three replicates, generating the following data: Time (min) Absorbance of Replicate 1 Absorbance of Replicate 2 Absorbance of Replicate 3 0.5 0.0984…
Failure of anti-oxidant function results in the hydroxylation of an aromatic acid of Enzyme Z and its activation, so that it degrades protoporphyrin to porphyrin, an unstable product. When hit by light, this product further degrades to form a compound responsible for the lesions and excruciating pain the man suffers. The mutation also affected an amino acid at the N-terminal of Enzyme X. Sequencing of the first seven (7) amino acids at the N-terminal of the normal enzyme gave the following sequence: trp-arg-asp-leu-ser-gly-his When the cDNA was sequenced by the Sanger method utilizing ddCTP, the following products were obtained: Tetranucleotide Hexanucleotide Nonanucleotide Decanucleotide Dodenucleotide Octadecanucleotide Nonadecanucleotide 21-nucleotide The mutation involved the 19th bases of the template strand of the peptide. A comparison of the electrophoretic profile of the normal peptide (N) and mutant peptide (M) is shown below. The (+) electrode is situated at the bottom. pH…
The enzyme mutase which is important for the synthetic of tyrosine and phenylalanine in saccharomyces cerevisiae has been studied as an example of an allosteric enzyme. Tyrosine acts as a negative effector for this enzyme. What effects would you see on the action of the enzyme were you to increase the concentration of tyrosine? The chorismate mutase would shift to its R conformation The curve showing the kinetics or chorismate mutase would shift to the right The curve showing the kinetics of chorismate mutase would shift to the left The chorismate mutase would become saturated more rapidly

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