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limetrout654Lv1
28 Sep 2019
A change in the primary sequence of a protein will never change how a protein is allosteric regulated.a.) Trueb.) FalseWhich of the following is NOT a mechanism of enzyme regulation?a.) Feedback inhibition by a product.b.) Addition or removal of phosphate groups to amino acids with alcohol groups.c.) Stimulation by a substrate or product.d.) Proteolytic cleavage.e.) Removal of a methyl group from the side chain of alanine.Which of these is NOT true about the active site of an enzyme?a.) It is composed of distinct amino acids that perform catalytic activitiesb.) It often has a prosthetic group depending on the enzymec.) It is formed by the folding of the proteind.) It is the site of binding of a competitive inhibitore.) It will never be affected by changes in the primary structure of the pWhich is NOT true about the Km of an enzyme:a.) is calculated as half of the maximal velocity of an enzymeb.) is a hypothetical number that cannot be achieved experimentallyc.) is negatively affected by a competitive inhibitord.) is a measure of how tightly an enzyme binds to its substratee.) all of the above are trueWhich is true about Vmax:a.) is the maximal velocity at which an enzyme can functionb.) is reduced by a non-competitive inhibitorc.) is determined on a Lineweaver-Burke plot by taking the reciprocal of the y-interceptd.) is low for an enzyme with a low Km and high substrate affinitye.) all of the above
A change in the primary sequence of a protein will never change how a protein is allosteric regulated.a.) Trueb.) FalseWhich of the following is NOT a mechanism of enzyme regulation?a.) Feedback inhibition by a product.b.) Addition or removal of phosphate groups to amino acids with alcohol groups.c.) Stimulation by a substrate or product.d.) Proteolytic cleavage.e.) Removal of a methyl group from the side chain of alanine.Which of these is NOT true about the active site of an enzyme?a.) It is composed of distinct amino acids that perform catalytic activitiesb.) It often has a prosthetic group depending on the enzymec.) It is formed by the folding of the proteind.) It is the site of binding of a competitive inhibitore.) It will never be affected by changes in the primary structure of the pWhich is NOT true about the Km of an enzyme:a.) is calculated as half of the maximal velocity of an enzymeb.) is a hypothetical number that cannot be achieved experimentallyc.) is negatively affected by a competitive inhibitord.) is a measure of how tightly an enzyme binds to its substratee.) all of the above are trueWhich is true about Vmax:a.) is the maximal velocity at which an enzyme can functionb.) is reduced by a non-competitive inhibitorc.) is determined on a Lineweaver-Burke plot by taking the reciprocal of the y-interceptd.) is low for an enzyme with a low Km and high substrate affinitye.) all of the above
Casey DurganLv2
28 Sep 2019