Homework Answers
6d.u41 is an inhibitor of jarase enzyme and it reduces kcat or catalytic efficiency of enzyme. since km is also reduced it is competetive inhibition
6e. km is reduced much and kcat is reduced to a lesser extent means it is competetive inhibition
6f. jarase is dehydrogenase enzyme and u42 is inhibitor
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6d. Fully explain what effect U41 is having on the jarase
enzyme. If it...
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...
included proper units when HLLL 1. The following kinetic data were generated for the enzyme SpB1,...
included proper units when HLLL 1. The following kinetic data were generated for the enzyme SpB1, this enzyme has an unknown biological function. Using the information provided below answer questions la-le. All reactions had 0.1 mg/mL SPBT which based on amino acid sequence and gel filtration column chromatography has a molecular weight of 42,500 Daltons. S002- Substrate 1 Substrate 2 KM (MM) kcat (sec) glucose >50 <0.01 glucose NADP 4+1 0.5+0.07 glucose NAD 2718 2 +0.05 galactose >50 <0.01 galactose...
10.What type of inhibitor is this? How do you know? (2) 11.For your assigned inhibitor 1,...
10.What type of inhibitor is this? How do you know? (2)
11.For your assigned inhibitor 1, what are the apparent Km &
Vmax? (NOTE: apparent Km& Vmax are just the Km & Vmax in
presence of inhibitor, at a given concentration.) (2)
Kinetics experiments were performed on PGI. Enzyme activity
(initial velocity, Vo) was measured at varying concentrations of
Glucose-6-phosphate (G6P). The enzyme concentration used in all
experiments was 1.5 μM.
12.What will be the reaction rate with 0.500 mM...
You are still interested in the enzyme happyase, which catalyzes the following reaction: HAPPY = SAD...
You are still interested in the enzyme happyase, which catalyzes the following reaction: HAPPY = SAD Previously, you determined that kcat = 400 s and Km = 10 M for your sample of happyase. Further research shows that this happyase sample was actually contaminated with a reversible inhibitor called ANGER. When ANGER is fully removed from the happyase preparation and [Eltotalis 4 nM, the measured Vmax is increased to 4.8 umes-1 and the measured Km is now 15 MM. Use...
(7 pts) What is the sequence of the following HEXAPEPTIDE? *PROVIDE WORK/ANSWER for B-F! (Use deductive...
(7 pts) What is the sequence of the following HEXAPEPTIDE? *PROVIDE WORK/ANSWER for B-F! (Use deductive reasoning) Observations from Sequencing Experiments: A. The Sequence contains the following amino acids: Y, R, M, K, G, D B. Reaction with 1-fluoro-2,4-dinitrobenzene yielded DNP-G. ___ ___ ___ ____ ___ ___ y = 0.058x + 0.0081 y = 0.2711x + 0.0105 -0.02 0 0.02 0.04 0.06 0.08 0.1 0.12 0.14 -0.2 -0.1 0 0.1 0.2 0.3 0.4 0.5 Velocity ( mM/min) -1 [S] mM-1...
Enzyme kinetics: You recently joined a new research group, and in your first week you successfully...
Enzyme kinetics: You recently joined a new research group, and in your first week you successfully discover a new version of an enzyme called happyase, which you name happyase*, that catalyzes the chemical reaction: HAPPY ↔ SAD You begin devising ways to characterize the enzyme. (5 points total, 2 each for A, B and 1 for C). In the first experiment, with [Et] at 4 nM, you find that the Vmax is 1.6 mM/s. Based on this experiment, what is...
Can someone please help with questions ii-vi? 6. Many types of cancerous tumors have cells with...
Can someone please help with questions ii-vi?
6. Many types of cancerous tumors have cells with a high dependence on glycolysis for generating the ATP needed for growth. Even in the presence of oxygen, these cells use glycolysis and lactate fermentation as their main source of ATP. i.) Give a balanced reaction for the reaction catalyzed by the enzyme lactate dehydrogenase (LDH). Give the structures of pyruvate and lactate, and add the names of any additional reactants or products needed...
Interpret the data above 1. What is the aporoximate Km and Vmax (units matter) 2.Briefly explain...
Interpret the data above
1. What is the aporoximate Km and Vmax (units matter)
2.Briefly explain how you found each
3.if you used 0.020 microM enzyme in your studies, what is
kcat in units of s^-1? Show your work units matter
4. Does this enzyme appear to display cooperativity? Explain
how you came up to that conclusion.
Directions: Below are data from 4 separate experiments that you must analyze/evaluate. Using the information from all 4 experiments, you must then propose...
Biochemistry. Please answer all completely. 13. Identify the electrophilic center and nucleophile in the below image...
Biochemistry. Please answer all completely.
13. Identify the electrophilic center and nucleophile in the below image : R 14. Give an example of amino acids with R group shown below which can function as nucleophile during enzyme catalysis. Nucleophiles Negatively charged oxygen (as in an unprotonated hydroxyl group or an ionized carboxylic acid) Negatively charged sulfhydryl Uncharged amine group HN Imidazole 15. Identify the amino acids with the following side chains and also define if they will work as acid...
2. hypothesize the best conditions (pH and temperature) under which the enzyme chymotrypsin functions with an...
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...
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...
included proper units when HLLL 1. The following kinetic data were generated for the enzyme SpB1, this enzyme has an unknown biological function. Using the information provided below answer questions la-le. All reactions had 0.1 mg/mL SPBT which based on amino acid sequence and gel filtration column chromatography has a molecular weight of 42,500 Daltons. S002- Substrate 1 Substrate 2 KM (MM) kcat (sec) glucose >50 <0.01 glucose NADP 4+1 0.5+0.07 glucose NAD 2718 2 +0.05 galactose >50 <0.01 galactose...
10.What type of inhibitor is this? How do you know? (2)
11.For your assigned inhibitor 1, what are the apparent Km &
Vmax? (NOTE: apparent Km& Vmax are just the Km & Vmax in
presence of inhibitor, at a given concentration.) (2)
Kinetics experiments were performed on PGI. Enzyme activity
(initial velocity, Vo) was measured at varying concentrations of
Glucose-6-phosphate (G6P). The enzyme concentration used in all
experiments was 1.5 μM.
12.What will be the reaction rate with 0.500 mM...
You are still interested in the enzyme happyase, which catalyzes the following reaction: HAPPY = SAD Previously, you determined that kcat = 400 s and Km = 10 M for your sample of happyase. Further research shows that this happyase sample was actually contaminated with a reversible inhibitor called ANGER. When ANGER is fully removed from the happyase preparation and [Eltotalis 4 nM, the measured Vmax is increased to 4.8 umes-1 and the measured Km is now 15 MM. Use...
Can someone please help with questions ii-vi?
6. Many types of cancerous tumors have cells with a high dependence on glycolysis for generating the ATP needed for growth. Even in the presence of oxygen, these cells use glycolysis and lactate fermentation as their main source of ATP. i.) Give a balanced reaction for the reaction catalyzed by the enzyme lactate dehydrogenase (LDH). Give the structures of pyruvate and lactate, and add the names of any additional reactants or products needed...
Interpret the data above
1. What is the aporoximate Km and Vmax (units matter)
2.Briefly explain how you found each
3.if you used 0.020 microM enzyme in your studies, what is
kcat in units of s^-1? Show your work units matter
4. Does this enzyme appear to display cooperativity? Explain
how you came up to that conclusion.
Directions: Below are data from 4 separate experiments that you must analyze/evaluate. Using the information from all 4 experiments, you must then propose...
Biochemistry. Please answer all completely.
13. Identify the electrophilic center and nucleophile in the below image : R 14. Give an example of amino acids with R group shown below which can function as nucleophile during enzyme catalysis. Nucleophiles Negatively charged oxygen (as in an unprotonated hydroxyl group or an ionized carboxylic acid) Negatively charged sulfhydryl Uncharged amine group HN Imidazole 15. Identify the amino acids with the following side chains and also define if they will work as acid...
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...
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