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- what is meant by S195? D102? H57?
- What do you figure would happen to the enzymes catalytic activity if the amino acids above were mutated?
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- What features distinguish enzymes that undergo allosteric control from those that obey the Michaelis– Menten equation?How can you recognize an enzyme that does not display Michaelis–Menten kinetics?1. A) Explain this statement, “Most enzymes are gene-encoded proteins, but most enzymes are not only protein". B) You recently isolated a new enzyme in your lab, and you named it "lipidase 1120". As a temporary name, this is fine. Who is responsible for assigning a formal name, and on what criteria will that name be assigned?
- The objective is to study a novel protease P isolated from the digestive tract of an Amazonian insect. This protease can exist into two forms Pi and Pa which have identical amino acid sequences (both of 80 kDa). However, only Pa shows proteolytic activity. To better understand the activation mode of Pi (inactive form) in Pa (active form), the following experiment was done using DIPF. DIPF (diisopropylphosphofluoridate) is a well-known irreversible inhibitor of serine proteases. It reacts with the catalytic serine residue of the active site of proteases as shown below: Enzyme -CH₂OH + CH(CH3)2 O F-P=0 O CH(CH3)2 Diisopropylphospho- fluoridate (DIPF) Enzyme -CH,—O CH(CH3)2 O <=0 O CH(CH3)2 DIP-Enzyme Both proteases Pa and P₁ were incubated with 32P-DIPF for 30 min at 37°C, and then dialysed to remove excess of unreacted radiolabelled reagent. The two proteases were then analyzed in Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE), with and without 2-mercaptoethanol.…Using the appropriate graph and table above, explain what the N426S mutation appears to be doing to the enzyme’s function. Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.B-lactamase is an enzyme found in many antibiotic-resistant bacteria that hydrolyzes and inactivates antibiotics like penicillin and cephalosporin. The amount of antibiotic hydrolyzed in 1 minute in a 10-ml solution containing purified ß-lactamase was measured as a function of antibiotic concentration. The kinetics of hydrolysis was performed for two antibiotic substrates (A and B). Assume that the concentration of ß-lactamase was kept constant during the assay. 12 Initial Velocity (nanomole/min) 10 8 2 0 10 20 | 30 [Antibiotic] (µm) 40 50 Antibiotic A Antibiotic B a) Based on the enzyme description, what type of enzyme is ß-lactamase? Lyase Isomerase Ligase Hydrolase Oxidoreductase Transferase b) Based on your answer in (a), what other reactant, in addition to the antibiotic substrate, needs to be in the active site of ß-lactamase for the hydrolysis reaction to proceed? c) From the reaction curves above, what is the approximate value of Vmax for the enzyme reaction? (Do not forget the…
- You have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new enzyme uses the same catalytic triad and the same reaction mechanism as chymotrypsin. Your new enzyme differs from chymotrypsin because it cuts peptides at the C terminus of polar, non-ionizable R groups. a) Beginning with the first tetrahedral intermediate, draw the mechanism of catalysis that occurs to cleave the tripeptide Asn-Phe-Lys substrate ending your answer with product and free enzyme. b) From the list below, which of the components would most likely be found in the area of the enzyme that substitutes the hydrophobic pocket of chymotrypsin? Very briefly explain your choice(s)., Ser lle Zn Val c) You've constructed a molecule that is able to bind to the 1 tetrahedral intermediate of your new.enzyme, preventing catalysis. From experimental results, you can see that this molecule is only able to bind to the tetrahedral intermediate. Assuming that this enzyme follows…You have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new enzyme uses the same catalytic triad and the same reaction mechanism as chymotrypsin. Your new enzyme differs from chymotrypsin because it cuts peptides at the C terminus of polar, non- ionizable R groups.A) Beginning with the first tetrahedral intermediate, draw the mechanism of catalysis that occurs to cleave the tripeptide Asn- Phe- Lys substrate ending your answer with the product and free enzyme.You have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new enzyme uses the same catalytic triad and the same reaction mechanism as chymotrypsin. Your new enzyme differs from chymotrypsin because it cuts peptides at the C terminus of polar, non- ionizable R groups. A) Beginning with the first tetrahedral intermediate, draw the mechanism of catalysis that occurs to cleave the tripeptide Asn- Phe- Lys substrate ending your answer with the product and free enzyme. B) From the list below, which of the components would most likely be found in the area of the enzyme that substitutes the hydrophobic pocket of chymotrypsin? Very briefly explain your choice(s): Ser ile Zn+ Val C) You've constructed a molecule that is able to bind to the 1st tetrahedral intermediate of your new enzyme, preventing catalysis. From experimental results, you can see that this molecule is only able to bind to the tetrahedral intermediate. Assuming that this enzyme follows…
- In the Avery experiment, mice were killed if they injected with S strain cells. Furthermore, incubation with extract from dead S strain cells could transform non pathogenic cells into pathogenic cells. This effect of S strain extract was eliminated if S strain extract is treated with what enzyme before incubation with non-pathogenic cells? protease DNAse RNAse LipaseWhat is the mechanism of an enzyme reaction involving a coenzyme for Nucleophilic Addition Rxns? GiveLysozyme is an antibacterial enzyme found in animals. Residues Asp 101 and Arg 114 are required for efficient catalysis, although they are located at some distance from the active site Glu 35 and Asp 52. Substituting Ala for either Asp 101 or Arg 114 does not significantly alter the enzyme's tertiary structure, but significantly reduces its catalytic activity. Explain.