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4. Three different enzymes (A, B, C) have been found to catalyze the same reaction using...
yule grapn below comparing two different enzymes with different enzyme kinetics. a. Do the graphs have...
yule grapn below comparing two different enzymes with different enzyme kinetics. a. Do the graphs have any of the same values for their Vmax, Vmax/2 or Km? If so which are the affinity for substrate same which are different? Enzyme with high Enzyme with low affinity for substrate Difference in reaction rate at low [5] Reaction rater Low (S] Substrate concentration [5] b. READ THIS: Enzyme-substrate affinity is the tendency for enzyme and substrate to bind together and form the...
vo " No effect or a slight increase B. A decrease in the an C. An...
vo " No effect or a slight increase B. A decrease in the an C. An increase in the rate D. An increase in the rate of E. A complete loss of enzyme crease in the affinity for substrate coup e in the rate of mentide hond cleavage are ne rate of peptide-bond cleavage due to an incre of enzyme activity due to the inability to bind substrate rmation below. of test tubes, es the enzyme in each In questions...
Question 4 Multi-Part Questions. Make sure to answer ALL parts (a-c)! You have isolated two versions...
Question 4 Multi-Part Questions. Make sure to answer ALL parts (a-c)! You have isolated two versions of the same enzyme, a wild type and mutant. The marteses You have determined the following kinetic characteristics for each of the enzymes. Vmax Wild Type Km 200 umol / min 0.2mm Mutant 2 umol / min 20mm and the reaction is a two-step reaction where k.1 is much larger than k3, which enzyme has the higher affinity for substrate to you You determine...
6. You have been working with the jarase enzyme which is not well understood. The jarase...
6. You have been working with the jarase enzyme which is not well understood. The jarase enzyme catalyzes the reaction shown below between B-hydroxy-2-butanone (B-H2b) and NAD'. You have noticed that jarase cannot catalyze the reverse reaction: OH + NAD NADH + H You generated the following kinetic data for the jarase enzyme, all reactions are carried out under the same reaction conditions, which are: pH 7.0, 1 mM NAD' varying amounts of B-H2b (from 0.002 - 2 mm) and...
1. The following kinetic data was generated for the Hst enzyme. The overall reaction for this...
1. The following kinetic data was generated for the Hst enzyme. The overall reaction for this enzyme is: OH ОН + NH3 NH2 All reactions are carried out in a final reaction volume of 2 mL with 0.1ug of purified Hst protein present at pH 7.8. The Hst protein has a molecular weight of 90 kDa based on estimates from gel filtration column chromatography and a molecular weight of 45 kDa based on estimates from denaturing SDS PAGE gel electrophoresis....
NAD+ -dependent Glyceraldehyde-3-phosphate + Dehydrogenase from Thermoproteus tenax. 1. Name the three enzymes that catalyze irreversible,...
NAD+ -dependent Glyceraldehyde-3-phosphate + Dehydrogenase from Thermoproteus tenax. 1. Name the three enzymes that catalyze irreversible, regulated reactions in glycolysis as studied in class. 2. What is the significance of the GAPDH reaction in E. coli to glycolysis? 3. How does the reaction catalyzed by GAPDH from T. tenax presented here differ from the reaction carried out in E. coli? 4. The activity of the GAPDH enzyme was assayed in the presence of a constant amount of glyceraldehyde-3-phosphate and an...
You have an enzyme that uses two substrates in a random reaction (the order of binding of the substrates is random). And the reaction A + B à P is catalyzed by the enzyme bringtogetherase You have car...
You have an enzyme that uses two substrates in a random reaction (the order of binding of the substrates is random). And the reaction A + B à P is catalyzed by the enzyme bringtogetherase You have carried out five sets of reaction rates Keeping B constant and varying A and then increasing B and Vary ing A again until all combinations of A and B are measured. In the reaction you used 0.02 mg of bringtogetherase which is a...
Applying the Michaelis-Menten Equation II Another enzyme is found that catalyzes the reaction A <===> B...
Applying the Michaelis-Menten Equation II Another enzyme is found that catalyzes the reaction A <===> B Researchers find that the K for the substrate A is 4 uM, and the kcat is 20 min^-1 (a) In an experiment, [A] = 6 mM, and the initial velocity, Vo was 480 nM min^-1 What was the [Et] used in the experiment? (b) In another experiment, [Et] 0.5uM, and the measured Vo=5uM min^-1 What was the [A] used in the experiment? ( c)...
Rodrigo is an enzyme engineer. He wants to know which of four peptide substrates is bound...
Rodrigo is an enzyme engineer. He wants to know which of four peptide substrates is bound most tightly by his engineered enzyme. Which value should he measure and pay attention to? Km KCAT Vo Both A and B kcat, [S], and [E]t Rodrigo's enzyme was assayed with three substrates (A, B, and C). The SAME enzyme concentration used was for each of the three reactions. The results of the three experiments are plotted as Lineweaver-Burke plots below. Considering what you...
You have an enzyme that uses two substrates in a random reaction (the order of binding...
You have an enzyme that uses two substrates in a random reaction (the order of binding of the substrates is random). And the reaction A + B à P is catalyzed by the enzyme bringtogetherase You have carried out five sets of reaction rates Keeping B constant and varying A and then increasing B and Vary ing A again until all combinations of A and B are measured. In the reaction you used 0.02 mg of bringtogetherase which is a...
yule grapn below comparing two different enzymes with different enzyme kinetics. a. Do the graphs have any of the same values for their Vmax, Vmax/2 or Km? If so which are the affinity for substrate same which are different? Enzyme with high Enzyme with low affinity for substrate Difference in reaction rate at low [5] Reaction rater Low (S] Substrate concentration [5] b. READ THIS: Enzyme-substrate affinity is the tendency for enzyme and substrate to bind together and form the...
vo " No effect or a slight increase B. A decrease in the an C. An increase in the rate D. An increase in the rate of E. A complete loss of enzyme crease in the affinity for substrate coup e in the rate of mentide hond cleavage are ne rate of peptide-bond cleavage due to an incre of enzyme activity due to the inability to bind substrate rmation below. of test tubes, es the enzyme in each In questions...
Question 4 Multi-Part Questions. Make sure to answer ALL parts (a-c)! You have isolated two versions of the same enzyme, a wild type and mutant. The marteses You have determined the following kinetic characteristics for each of the enzymes. Vmax Wild Type Km 200 umol / min 0.2mm Mutant 2 umol / min 20mm and the reaction is a two-step reaction where k.1 is much larger than k3, which enzyme has the higher affinity for substrate to you You determine...
6. You have been working with the jarase enzyme which is not well understood. The jarase enzyme catalyzes the reaction shown below between B-hydroxy-2-butanone (B-H2b) and NAD'. You have noticed that jarase cannot catalyze the reverse reaction: OH + NAD NADH + H You generated the following kinetic data for the jarase enzyme, all reactions are carried out under the same reaction conditions, which are: pH 7.0, 1 mM NAD' varying amounts of B-H2b (from 0.002 - 2 mm) and...
1. The following kinetic data was generated for the Hst enzyme. The overall reaction for this enzyme is: OH ОН + NH3 NH2 All reactions are carried out in a final reaction volume of 2 mL with 0.1ug of purified Hst protein present at pH 7.8. The Hst protein has a molecular weight of 90 kDa based on estimates from gel filtration column chromatography and a molecular weight of 45 kDa based on estimates from denaturing SDS PAGE gel electrophoresis....
Rodrigo is an enzyme engineer. He wants to know which of four peptide substrates is bound most tightly by his engineered enzyme. Which value should he measure and pay attention to? Km KCAT Vo Both A and B kcat, [S], and [E]t Rodrigo's enzyme was assayed with three substrates (A, B, and C). The SAME enzyme concentration used was for each of the three reactions. The results of the three experiments are plotted as Lineweaver-Burke plots below. Considering what you...
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