metabolism assignment
Short Answer Question 1 (5 points). Below are two structural formulas showing the substrate and inhibitor for an enzyme. Based on these structures, determine the most likely mechanism of inhibition for this enzyme, and explain why you have chosen this mechanism.
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Homework # 16: Enzymes Late assignment will be given a grade of "0. Due Date 1. An enzyme is primarily made out of a (hint what food group). catechol+ oxygen (0a) Catecholasepolyphenol 2. Loo...
Homework # 16: Enzymes Late assignment will be given a grade of "0. Due Date 1. An enzyme is primarily made out of a (hint what food group). catechol+ oxygen (0a) Catecholasepolyphenol 2. Looking at the equation above, the enzyme in this reaction is: 2. A. Catechol B. Oxygen C. Catecholase D. Polyphenol 3. Looking at the same equation as question 2, what is the substrate? A. Catechol B. Oxygen C. Catecholase D. Polyphenol What is the name of the...
Compare competitive and noncompetitive inhibition Question Suppose that glycerol (CH,OHCH(OH)CH,OH) is a substrate in a...
Compare competitive and noncompetitive inhibition Question Suppose that glycerol (CH,OHCH(OH)CH,OH) is a substrate in an enzyme-catalyzed biochemical reaction and propylene glycol (CH OHCH(OH)CHZ) is an inhibitor of the reaction. Would you expect propylene glycol to be a competitive or noncompetitive inhibitor? Why? Select the correct answer below: O It is likely that propylene glycol would be a competitive inhibitor because it easily binds to glycerol. O It is likely that propylene glycol would be a competitive inhibitor because it has...
i need help answering questions EXTRA CREDIT 1. A pharmaceutical company has developed a new chemotherapy...
i need help answering questions
EXTRA CREDIT 1. A pharmaceutical company has developed a new chemotherapy drug (STOP2D) which functions as an inhibitor of the enzyme Split2. This enzyme is part of a pathway that promotes cell division. Suppose that in clinical trials, some of the patients become resistant to the drug. In order to determine the mechanism of resistance, the proteome of the patients is examined and it is found that the expression of Split2 is normal; however, the...
b) (10 points) Acetylcholinesterase is a hydrolase that hydrolyzes the neurotransmitter acetylcholine. Caffeine inhibits the action...
b) (10 points) Acetylcholinesterase is a hydrolase that
hydrolyzes the neurotransmitter acetylcholine. Caffeine inhibits
the action of Acetylcholinesterase and clinical studies have
indicated that it can be involved in the slowing of Alzheimer
disease pathology. P11149 is a galanthamine analogue that has also
been studied as a potential drug for treating Alzheimer
disease.
The initial reaction rate for acetylcholine hydrolysis was measured
at an enzyme concentration of 5×10-8 M with no inhibitor present,
and in the presence of caffeine or...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. T...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
Compare competitive and noncompetitive inhibition Question An enzyme is placed in the presence of an unknown...
Compare competitive and noncompetitive inhibition Question An enzyme is placed in the presence of an unknown substance to determine whether the substance is an inhibitor. As the substrate concentration is increased, the rate of reaction is compared to the normal rate of reaction. Initially, the rate is equal to normal, and as the substrate concentration is increased more and more, the rate of reaction remains the same as the normal rate. What can be concluded about the unknown substance? Select...
Compare competitive and noncompetitive inhibition Question An enzyme is placed in the presence of an unknown...
Compare competitive and noncompetitive inhibition Question An enzyme is placed in the presence of an unknown substance to determine whether the substance is an inhibitor. As the substrate concentration is increased, the rate of reaction is compared to the normal rate of reaction. Initially, the rate is slower than normal, but as the substrate concentration is increased more and more, the rate of reaction approaches normal. What can be concluded about the unknown substance? Select the correct answer below: O...
1. Graphic depictions of enzyme kinetic data can aid in evaluation of reversible enzyme inhibition. Please...
1. Graphic depictions of enzyme kinetic data can aid in evaluation of reversible enzyme inhibition. Please use the data below to determine type of inhibition for using two different concentrations (in blue and purple). Be sure to include graphical representation (Michaelis-Menton, Lineweaver-Burk plots), type of inhibition, appropriate kinetic schemes and rate equations. The enzyme concentration at its initial state E, was kept constant. All data points are given in arbitrary units. Completely justify your answer. Use Excel or graphing paper...
Consider the trypsin binding-pocket specificity structure scenario and critical AAs interactions ...
Consider the trypsin binding-pocket specificity structure scenario and critical AAs interactions within: G226-D189-G216 (see L3, slide 26): a single nucleotide polymorphism within the D189 codon resulted in a first nucleotide Guanine replacement by Cytosine. What is the consequence of this mutation relative to binding pocket- substrate specificity? (3 pts) 5. You work at the infamous enzymology lab; a colleague asks you to evaluate her enzyme activity data test based on the efficacy of two inhibitors, each at the [10 mM]...
2. The reaction below is catalyzed by the CK enzyme: NH2 OP H2N H₂N N Ń...
2. The reaction below is catalyzed by the CK enzyme: NH2 OP H2N H₂N N Ń cooK COO - INN CO + ATP + ADP Below is a picture of the active site for this enzyme. The red atoms are the amino acids in the CK protein. The blue structure is the substrate, the orange is the phosphate end of ATP. All dashed lines are showing interactions and the curved arrows are showing the mechanism. The wavy lines indicate that...
Homework # 16: Enzymes Late assignment will be given a grade of "0. Due Date 1. An enzyme is primarily made out of a (hint what food group). catechol+ oxygen (0a) Catecholasepolyphenol 2. Looking at the equation above, the enzyme in this reaction is: 2. A. Catechol B. Oxygen C. Catecholase D. Polyphenol 3. Looking at the same equation as question 2, what is the substrate? A. Catechol B. Oxygen C. Catecholase D. Polyphenol What is the name of the...
Compare competitive and noncompetitive inhibition Question Suppose that glycerol (CH,OHCH(OH)CH,OH) is a substrate in an enzyme-catalyzed biochemical reaction and propylene glycol (CH OHCH(OH)CHZ) is an inhibitor of the reaction. Would you expect propylene glycol to be a competitive or noncompetitive inhibitor? Why? Select the correct answer below: O It is likely that propylene glycol would be a competitive inhibitor because it easily binds to glycerol. O It is likely that propylene glycol would be a competitive inhibitor because it has...
i need help answering questions
EXTRA CREDIT 1. A pharmaceutical company has developed a new chemotherapy drug (STOP2D) which functions as an inhibitor of the enzyme Split2. This enzyme is part of a pathway that promotes cell division. Suppose that in clinical trials, some of the patients become resistant to the drug. In order to determine the mechanism of resistance, the proteome of the patients is examined and it is found that the expression of Split2 is normal; however, the...
b) (10 points) Acetylcholinesterase is a hydrolase that
hydrolyzes the neurotransmitter acetylcholine. Caffeine inhibits
the action of Acetylcholinesterase and clinical studies have
indicated that it can be involved in the slowing of Alzheimer
disease pathology. P11149 is a galanthamine analogue that has also
been studied as a potential drug for treating Alzheimer
disease.
The initial reaction rate for acetylcholine hydrolysis was measured
at an enzyme concentration of 5×10-8 M with no inhibitor present,
and in the presence of caffeine or...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
Compare competitive and noncompetitive inhibition Question An enzyme is placed in the presence of an unknown substance to determine whether the substance is an inhibitor. As the substrate concentration is increased, the rate of reaction is compared to the normal rate of reaction. Initially, the rate is equal to normal, and as the substrate concentration is increased more and more, the rate of reaction remains the same as the normal rate. What can be concluded about the unknown substance? Select...
Compare competitive and noncompetitive inhibition Question An enzyme is placed in the presence of an unknown substance to determine whether the substance is an inhibitor. As the substrate concentration is increased, the rate of reaction is compared to the normal rate of reaction. Initially, the rate is slower than normal, but as the substrate concentration is increased more and more, the rate of reaction approaches normal. What can be concluded about the unknown substance? Select the correct answer below: O...
1. Graphic depictions of enzyme kinetic data can aid in evaluation of reversible enzyme inhibition. Please use the data below to determine type of inhibition for using two different concentrations (in blue and purple). Be sure to include graphical representation (Michaelis-Menton, Lineweaver-Burk plots), type of inhibition, appropriate kinetic schemes and rate equations. The enzyme concentration at its initial state E, was kept constant. All data points are given in arbitrary units. Completely justify your answer. Use Excel or graphing paper...
Consider the trypsin binding-pocket specificity structure scenario and critical AAs interactions within: G226-D189-G216 (see L3, slide 26): a single nucleotide polymorphism within the D189 codon resulted in a first nucleotide Guanine replacement by Cytosine. What is the consequence of this mutation relative to binding pocket- substrate specificity? (3 pts) 5. You work at the infamous enzymology lab; a colleague asks you to evaluate her enzyme activity data test based on the efficacy of two inhibitors, each at the [10 mM]...
2. The reaction below is catalyzed by the CK enzyme: NH2 OP H2N H₂N N Ń cooK COO - INN CO + ATP + ADP Below is a picture of the active site for this enzyme. The red atoms are the amino acids in the CK protein. The blue structure is the substrate, the orange is the phosphate end of ATP. All dashed lines are showing interactions and the curved arrows are showing the mechanism. The wavy lines indicate that...
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