A particular protein-cased enzyme is always produced in the cell. What types of regulation do you...
A particular protein-cased enzyme is always produced in the cell. What types of regulation do you have to consider? The regulations that are considered are phosphorylation, zymogenic, competitive and noncompetitive inhibition, positive allosteric regulation, and irreversible inhibition.
Homework Answers
The regulations that are considered are phosphorylation, zymogenic, competitive and non-competitive inhibition, positive allosteric regulation and irreversible inhibition.
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A particular protein-cased enzyme is always produced in the
cell. What types of regulation do you...
How you would determine an enzyme regulation? Below is a series of results from tests of...
How you would determine an enzyme regulation? Below is a series of results from tests of one particular enzyme. List all the potential methods of regulation still possible after each test. The options are: "genetic" control, zymogenic, phosphorylation, competitive inhibition, noncompetitive inhibition, positive allosteric regulation, and irreversible inhibition. 1. The enzyme is always present in the cell. 2. All tests only slow enzyme activity. 3. Adding more substrate does not increase reaction rate. 4. There seems to be a form...
Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric...
Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric b) irreversible c) reversible d) suicide 2. DIFP is: a) a competitive inhibitor b) an allosteric inhibitor c) a noncompetitive inhibitor d) a suicide inhibitor 3. Competitive inhibitors: a) bind to the active site b) bind to the enzyme-substrate complex c) bind outside the active site and decrease substrate binding d) bind outside the active site and decrease rate of catalysis.
For each of the following enzyme regulation mechanisms/situations below, list whether it will: A. Always decrease activity V B. Always increase activity V C. May increase or decrease activity V D. May...
For each of the following enzyme regulation mechanisms/situations below, list whether it will: A. Always decrease activity V B. Always increase activity V C. May increase or decrease activity V D. May decrease or possibly have minimal effect on activity V E. Will definitely have no significant effect on activity V 1. Competitive Inhibitor with [I] > Ki and [S] < Km 2. Noncompetitive inhibitor with [I] > Ki and [S] < Km 3. Phosphorylation of Enzyme 4. Product Inhibition...
CILI ULIULIS. Question 2 The reason enzyme catalyzed reaction rates have a maximum velocity at high...
CILI ULIULIS. Question 2 The reason enzyme catalyzed reaction rates have a maximum velocity at high substrate concentrations is: Enzymes denature at high substrate concentrations. O None of the answers are correct. The enzyme active sites are saturated. O If enzymes go too fast they make mistakes. O The build-up of product limits the rate of the reaction. Question 3 TILS LICTULUGTCAICONI Question 3 4 pts For a plot of velocity vs. [S] where the maximal velocity of the uninhibited...
PLease answer all... Thank you! 53) An enzyme is (1 pts) an organic catalyst able to...
PLease answer all... Thank you!
53) An enzyme is (1 pts) an organic catalyst able to change the rate of reaction a protein All of the above are correct. 54) Cyanide is a strong inhibitor of iron-containing enzymes because it binds with iron and deprives the enzyme of its cofactor. This is called O noncompetitive ihibition denaturation O competitive inhibition O constitutive enzymes 55) Enzymes which are produced by the cell only in response to a particular substrate are called...
12) Which of the following types of enzyme carries out phosphorylation of a protein? (a) isomerase...
12) Which of the following types of enzyme carries out phosphorylation of a protein? (a) isomerase (b) kinase (c) phosphodiesterase (d) lyase (e) hydrolase 13) Flavin adenine nucleotide is a coenzyme for which of the following? (a) monoamine oxidase (b) trypsin (c) chymotrypsin (d) Na+ K+ ATPase (e) all of the above 14) A noncompetitive inhibitor (a) binds only to [ES] (b) binds either [E] or [ES] (c) binds only to [E] (d) binds only to [S] (15) Which of...
eurtansmitteenzyme found in the synaptic cleft and required for degrading a. glycosyltransferase c hemoglobin b. PDH...
eurtansmitteenzyme found in the synaptic cleft and required for degrading a. glycosyltransferase c hemoglobin b. PDH complex e.catalase d. acetylcholinesterase 44. Which of the following is a tenet of the endosymbiotic theory? a autophagolysosomes are the source of substantial protein production viruses at some time i incorporated into the mitochondrial genome engulfed bacteria may be the original source of m more than one of the above pped in vesicles in the cytoplasm contribute to the cell's ATP supply e. the...
QUESTION 1 Imagine you want to get rich by genetically engineering tobacco plants to produce acai...
QUESTION 1 Imagine you want to get rich by genetically engineering tobacco plants to produce acai berry juice. To do so, you insert the genes for each of the enzymes in the hypothetical acai synthesis pathway, the first step of which is (hypothetically) conversion of glucose to fructose. The challenge is that glucose must be maintained at or above a minimum concentration or the plant will die because it can no longer make ATP. For the reaction pathway shown below,...
When running enzyme assays, why do you need to normalize enzyme activity to total protein concentration?...
When running enzyme assays, why do you need to normalize enzyme activity to total protein concentration? What does the specific activity mean in the research lab where enzymes are used? (Hint: are enzymes always pure?)
6. What does a buffer do? Why are bicarbonate and phosph Henderson Hasselbalch equation to calculate...
6. What does a buffer do? Why are bicarbonate and phosph Henderson Hasselbalch equation to calculate pH if pKa i ate really good biological buffers? Use the s 4.0, [A-1-10μΜ, and [HA-1000μΜ 7. In what eukaryotic cell structure (cytosol, nucleus, mitochondrion, inner mitochondrial membrane, rough ER, smooth ER, plasma membrane etc.) do the following functions take place? Transcription Translation (2 sites) Glycolysis Kreb's Cycle Electron transport chain AG, of a reaction is +11,600 The standard J/mol. What is K at...
How you would determine an enzyme regulation? Below is a series of results from tests of one particular enzyme. List all the potential methods of regulation still possible after each test. The options are: "genetic" control, zymogenic, phosphorylation, competitive inhibition, noncompetitive inhibition, positive allosteric regulation, and irreversible inhibition. 1. The enzyme is always present in the cell. 2. All tests only slow enzyme activity. 3. Adding more substrate does not increase reaction rate. 4. There seems to be a form...
Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric b) irreversible c) reversible d) suicide 2. DIFP is: a) a competitive inhibitor b) an allosteric inhibitor c) a noncompetitive inhibitor d) a suicide inhibitor 3. Competitive inhibitors: a) bind to the active site b) bind to the enzyme-substrate complex c) bind outside the active site and decrease substrate binding d) bind outside the active site and decrease rate of catalysis.
CILI ULIULIS. Question 2 The reason enzyme catalyzed reaction rates have a maximum velocity at high substrate concentrations is: Enzymes denature at high substrate concentrations. O None of the answers are correct. The enzyme active sites are saturated. O If enzymes go too fast they make mistakes. O The build-up of product limits the rate of the reaction. Question 3 TILS LICTULUGTCAICONI Question 3 4 pts For a plot of velocity vs. [S] where the maximal velocity of the uninhibited...
PLease answer all... Thank you!
53) An enzyme is (1 pts) an organic catalyst able to change the rate of reaction a protein All of the above are correct. 54) Cyanide is a strong inhibitor of iron-containing enzymes because it binds with iron and deprives the enzyme of its cofactor. This is called O noncompetitive ihibition denaturation O competitive inhibition O constitutive enzymes 55) Enzymes which are produced by the cell only in response to a particular substrate are called...
eurtansmitteenzyme found in the synaptic cleft and required for degrading a. glycosyltransferase c hemoglobin b. PDH complex e.catalase d. acetylcholinesterase 44. Which of the following is a tenet of the endosymbiotic theory? a autophagolysosomes are the source of substantial protein production viruses at some time i incorporated into the mitochondrial genome engulfed bacteria may be the original source of m more than one of the above pped in vesicles in the cytoplasm contribute to the cell's ATP supply e. the...
QUESTION 1 Imagine you want to get rich by genetically engineering tobacco plants to produce acai berry juice. To do so, you insert the genes for each of the enzymes in the hypothetical acai synthesis pathway, the first step of which is (hypothetically) conversion of glucose to fructose. The challenge is that glucose must be maintained at or above a minimum concentration or the plant will die because it can no longer make ATP. For the reaction pathway shown below,...
6. What does a buffer do? Why are bicarbonate and phosph Henderson Hasselbalch equation to calculate pH if pKa i ate really good biological buffers? Use the s 4.0, [A-1-10μΜ, and [HA-1000μΜ 7. In what eukaryotic cell structure (cytosol, nucleus, mitochondrion, inner mitochondrial membrane, rough ER, smooth ER, plasma membrane etc.) do the following functions take place? Transcription Translation (2 sites) Glycolysis Kreb's Cycle Electron transport chain AG, of a reaction is +11,600 The standard J/mol. What is K at...
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