reaction using the same substrate. Inst 10 nanomoles/ml of the in 40. Sudentase
ID: 147648 • Letter: R
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reaction using the same substrate. Inst 10 nanomoles/ml of the in 40. Sudentase and Instructoras cataligstte whercasesng to esusubstt for thesubstrate whereas studentase resulted in identical Vma values of 100 has a K- value of 10 uM for the substrate containing dividual enzymes concentrations, assays containing statements is true. sing this data determine which of the following a. The Ka of studentase greater b. The K.c of instructorase is grebut the Kus of the encorase is greater than the K.u. of studentase. d. The Kat of the enzymes is oe is greater than the Kor of instructorase. d. STudentasezymeseater than the Kon of studentase. but instructorase has a greater Specificity Constant than of the enzymes is instructorase. None of t studentase entical, but studentase has a greater Specificity Constant than e. he above statements is true. 41. Proteins that aid in the correct and timely folding of other pro correct and timely folding of other proteins e prosthetic g a. motifs. b. chaperones. c. liposomes. d. cooperative. 42. The lock and key model of enzyme activity proposes that eadh a. Enzyme can react with only a single substrate b. Enzyme has a cofactor that promotes the cataly c. Substrate has a specific cofactor that binds it to the enzytnd substrate ha d. Enzyme binds a specific substrate because the active site tes the catalytic activity structures Substrate binding causes the enzyme to undergo co the substrate. e. conformational changes to accommodate 43. An abnormal variant of hemoglobi in was found to contain two additional positive charges in the central cavity of the molecule. How will, if at all, will this change effect hemoglobin function a. This hemoglobin will demonstrate a higher affinity for O b. This hemoglobin will be no different from "normal" hemoglobin. c. This hemoglobin will demonstrate a lower affinity for On d. All of the above e. None of the above 44. Competitive inhibitors have this effect: a. b. c. Increase the KM value. Decreasing the value for Vmax. Compete with substrate binding. e. All of these are correct. Which statement about intrinsically disordered proteins is true? a. They contain many large hydrophobic amino acids. b. They represent pathologically misfolded conformations of cellular proteins c. They have no stable d. They are responsible for proteostasis. e. They can interact with multiple protein-binding partners and are central to 45. structure and therefore have no cellular function. protein interaction networks. 6. All catalysts work by lowering the activation energy for a reaction. b. Nope! a.Explanation / Answer
40. a. Kcat of studentase is greater than Kcat of instructorase
Kcat / Km gives a measure of enzyme efficiency. The enzyme efficiency is increased with high turnover number (high Kcat) and low Km.
41. b. chaperones
Chaperones are proteins help in the folding and unfolding of macromolecular structures.
42. a. Enzyme can react with only a single substrate
According to lock and key model, the enzyme structure is predetermined and as a key fits into the lock, only one substrate can fit with the enzyme.
43. b. The hemoglobin will be no different from normal hemoglobin
The two extra charges don't affect the oxygen affinity, as O2 binds with the heme part.
44. d. a and c
Competitive inhibitor competes with the substrate and increases the Km value.
45. e.They can interact with multiple protein binding partners and are central to protein interaction networks. Disordered proteins called linear motifs make interactions with other proteins and other macromolecules like DNA and RNA.
They are rich in polar (hydrophilic) aminoacids and with various biologic roles.
46. a. Yup
Catalyst reduces the activation energy of the reaction. Enzyems act as catalysts lowering the activation energy needed.
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