4 - The restriction enzyme EcoRV is not active if it has not bound to its...
4 - The restriction enzyme EcoRV is not active if it has not bound to its target site. Describe how the enzyme is activated upon binding to its correct target site, and describe the biological importance of this activation mechanism.
Homework Answers
upon binding to its target site enzyme undergo confirmatiol changes to activate ,this activation mechanism important for product formation and maintenance of biological system.
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4 - The restriction enzyme EcoRV is not active if it has not
bound to its...
QUESTION A drug binds to the active site of an enzyme. If atis bound to the...
QUESTION A drug binds to the active site of an enzyme. If atis bound to the active site of the enzyme, it prevents substrate binding This drug 10
A noncompetitive inhibitor O sits on the active site of an enzyme blocking the subtrate inactivates...
A noncompetitive inhibitor O sits on the active site of an enzyme blocking the subtrate inactivates an enzyme by binding to the allosteric site on an enzyme and changing the shape of the active site. lowers the activation energy of the chemical reaction its involved in All of the above npu Reset Selection
The enzyme catalase has a ferric ion tightly bound to the active site. The ferric ion...
The enzyme catalase has a ferric ion tightly bound to the active site. The ferric ion is called a(n) O enzyme. O side chain. substrate. cofactor.
Which statement about enzyme catalysis is false? All of the active site amino acids are next...
Which statement about enzyme catalysis is false? All of the active site amino acids are next to each other in the primary sequence. Enzymes speed up reactions by forming specific non-covalent bonds between the enzyme amino acids and the transition state molecule. Some enzymes require other molecules, called cofactors, to carry out chemical reactions. Generally, the most important amino acids for an enzyme's function are those in the active site. Question 6 1 pt When [S] is much more than...
The effect of pH on the activity of an enzyme was examined. At its active site,...
The effect of pH on the activity of an enzyme was examined. At its active site, the enzyme has an Ionizable group that must be positively charged for substrate binding and catalysis to take place. The Ionizable group has a pk of 6.0. The substrate is negatively charged throughout the pH range of the experiment At what pH=9. the enzyme will be operating at answer is either Vmax, 1/2 Vmax or less than 1/2 Vmax (type in one of the...
1. Protein kinases phosphorylate target enzymes and as a result enzymes become activated or inactivated. Which...
1. Protein kinases phosphorylate target enzymes and as a result enzymes become activated or inactivated. Which of the statements are TRUE? (Multiple answers: You can select more than one option) A. Phosphorylated enzymes behave like competitive inhibitors B The presence of a phosphate acts as a non-competitive inhibitor/activator. No change in Km but significant change in Vmax C. The presence of a phosphate group induces a conformational change that modifies the affinity and catalytic ability of a target enzyme D....
Question 4 C. Cloning and restriction enzyme digest Video aid 1: Plasmid cloning Video aid 2:...
Question 4
C. Cloning and restriction enzyme digest Video aid 1: Plasmid cloning Video aid 2: Restriction enzyme digest analysis The PCR was a success and your target region of 440 bp in length has been amplified. You igate a short linker containing an Apal restriction enzyme site onto both ends of the PCR product, digest it with Apal, and clone it into the Apal site of the 5 kb plasmid diagrammed below Bamll 300 EcoRI 3400 1000 2000 5...
PT1. Which of the following does not describe a mechanism that cells use to regulate enzyme...
PT1. Which of the following does not describe a mechanism that cells use to regulate enzyme activity? Explain. (5 points) Cells control enzyme activity by the binding of small molecules Cells control enzyme activity by phosphorylation and dephosphorylation Cells control the diffusion rates of substrate to enzymes Cells control the rate of enzyme degradation Cells control the rate of enzyme synthesis Cells control the targeting of enzymes to specific organelles PT2. Which of the following properties of an enzyme is...
please help thanks VI You are studying the mechanism of catalysis for an enzyme and find...
please help thanks
VI You are studying the mechanism of catalysis for an enzyme and find that mutating an active site lysine to glutamate has no effect on initial binding, but it significantly decreases the rate at which the enzyme catalyzes its reaction. Predict how this mutation (Lys Glu) is affecting catalytic rate in three sentences or fewer. (Hint, what might the lysine be doing to facilitate catalysis?) LMS stabilizes transition State
Part A - Overview of enzyme structure and enzymatic reactions Enzymes are large globular proteins. Much...
Part A - Overview of enzyme structure and enzymatic reactions Enzymes are large globular proteins. Much of their three dimensional shape is the result of interactions between the R (variable) groups of their amino acids. The active site is the portion of the enzyme that will interact with the substrate the molecule that the enzyme acts upon. The nature and arrangement of amino acids in the active site make each enzyme specific to a substrate and to the reaction it...
QUESTION A drug binds to the active site of an enzyme. If atis bound to the active site of the enzyme, it prevents substrate binding This drug 10
A noncompetitive inhibitor O sits on the active site of an enzyme blocking the subtrate inactivates an enzyme by binding to the allosteric site on an enzyme and changing the shape of the active site. lowers the activation energy of the chemical reaction its involved in All of the above npu Reset Selection
The enzyme catalase has a ferric ion tightly bound to the active site. The ferric ion is called a(n) O enzyme. O side chain. substrate. cofactor.
Which statement about enzyme catalysis is false? All of the active site amino acids are next to each other in the primary sequence. Enzymes speed up reactions by forming specific non-covalent bonds between the enzyme amino acids and the transition state molecule. Some enzymes require other molecules, called cofactors, to carry out chemical reactions. Generally, the most important amino acids for an enzyme's function are those in the active site. Question 6 1 pt When [S] is much more than...
The effect of pH on the activity of an enzyme was examined. At its active site, the enzyme has an Ionizable group that must be positively charged for substrate binding and catalysis to take place. The Ionizable group has a pk of 6.0. The substrate is negatively charged throughout the pH range of the experiment At what pH=9. the enzyme will be operating at answer is either Vmax, 1/2 Vmax or less than 1/2 Vmax (type in one of the...
Question 4
C. Cloning and restriction enzyme digest Video aid 1: Plasmid cloning Video aid 2: Restriction enzyme digest analysis The PCR was a success and your target region of 440 bp in length has been amplified. You igate a short linker containing an Apal restriction enzyme site onto both ends of the PCR product, digest it with Apal, and clone it into the Apal site of the 5 kb plasmid diagrammed below Bamll 300 EcoRI 3400 1000 2000 5...
please help thanks
VI You are studying the mechanism of catalysis for an enzyme and find that mutating an active site lysine to glutamate has no effect on initial binding, but it significantly decreases the rate at which the enzyme catalyzes its reaction. Predict how this mutation (Lys Glu) is affecting catalytic rate in three sentences or fewer. (Hint, what might the lysine be doing to facilitate catalysis?) LMS stabilizes transition State
Part A - Overview of enzyme structure and enzymatic reactions Enzymes are large globular proteins. Much of their three dimensional shape is the result of interactions between the R (variable) groups of their amino acids. The active site is the portion of the enzyme that will interact with the substrate the molecule that the enzyme acts upon. The nature and arrangement of amino acids in the active site make each enzyme specific to a substrate and to the reaction it...
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