Which of the following is incorrect about the drugs called statins? O a. None; all the other choices are correct O b. They are competitive inhibitors of the regulatory enzyme of cholesterol synthesis O c. They have a bulky group that mimics CoA Od. They have an HMG-like group
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- The following structure is more active than morphine as an analgesic. H3C CH3 H. H3C' O Il.. What is the principal reason for this? The extra acetyl group binds to cell surface receptors improving active internalization. The acetyl groups mask a polar group allowing the structure to cross the blood brain barrier more efficiently. The extra acetyl group masks an alcohol group which would otherwise undergo a phase Il metabolic conjugation reaction leading to rapid excretion of the drug. The acetyl groups increase the stability of the drug in the cellular environment. O Il..Which of the following statements is not true about the catalytic triad in chymotrypsin? Group of answer choices the side chain of the serine 195 is hydrogen bonded to the imidazole ring of histidine the -NH group of the imidazole ring of histidine is hydrogen bonded to the carboxylate group of aspartate 102 the histidine residue serves to position the aspartate 102 side chain and to polarize its carboxylate group so that it is poised for deprotonation histidine acts as a general base catalyst none of theseThe following structure is more active than morphine as an analgesic. H3C N. CH3 H. H3C O .. What is the principal reason for this? O The extra acetyl group binds to cell surface receptors improving active internalization. O The acetyl groups mask a polar group allowing the structure to cross the blood brain barrier more efficiently. O The extra acetyl group masks an alcohol group which would otherwise undergo a phase Il metabolic conjugation reaction leading to rapid excretion of the drug. O The acetyl groups increase the stability of the drug in the cellular environment. O ..
- A schematic representation of the enzyme IspD complexed to inhibitor 3, and a series of inhibitors 3-5 are shown below. Ala202 lle240 mwww NH NH Val263 ОН www HN N- lle177 HN 'N' CI 3 X = N 4 X = C-CN 5 X = C-COO IC50 274 µM IC50 140 nM IC50 35 nM NH2 HN Val266 N -N O-H---- N HN %3D Arg157 HN wwww lle265 Explain why structure 4 is a more potent inhibitor (lower IC50 value) than inhibitor 3 and why structure 5 is a much weaker inhibitor (higher IC50 value) than 3 and 4.Figure 1 shows the catalytic triad of a-chymotrypsin. Identify A, B and C. Describe the subsequent steps of stage 1 and stage 2 of a- chymotrypsin mechanism. Illustrate with diagrams. A B CH2 H-N N: H-O Figure 1About defroxamine (all are correct except Select one: 1- its a tridentate chelating agent of great water solubility as well as stability forming a hexagonal complex 2- due to its poor GIT absorption administered as I.M and I.V injection 3- the precursor is a ferric ion natural product obtained from the bacteria Streptomuces pilosis modified through removal of iron III then converted as mesylate salt 4- it is a water instable compound produced as injectable powder for instant reconstitution used to treat hemochromatosis
- One mechanism by which lead exerts its poisonous effect on enzymes can be stopped by chelation therapy with EDTA. Describe this type of lead poisoning and explain why it is reversible.Which of the following statements is true about the chymotrypsin reaction? 1. The catalytic triad at the active site is formed by three residues: His, Gly, and Ser 2. When the substrate is p-Nitrophenylacetate, the rate-limiting step is the release of p-Nitrophenolate. 3. During the reaction, LBHB forms when the proton is donated to His from Ser or water. 4. The chymotrypsin reaction involves “only” specific acid-base catalysis 5. The “oxyanion hole” is formed by the amide nitrogens of Ser and GluConsider the mechanism of enolase, as indicated below. Which of the following correctly describes the roles of the Mg2+ as illustrated in the figure? (This is a multi- select question). Mg2+ Mg2 Enolase PO3- OH -C-C-H H OH HO H-N-H Lys 345 Glu211 2-Phosphoglycerate bound to enzyme Mg2+ Mg2 PO3- OH C-C-H OH HO H H-N*-H Lys 345 O Glu211 Enolic intermediate HOH PO3- H Phosphoenolpyruvate The metal ion (Mg2+) is helping to stabilize the extra negative charge that developed on the carboxyl group in the enolic intermediate. The metal ion (Mg2+) is serving as a general base, removing a proton in order to improve the quality of the nucleophile. The metal ion (Mg2+) is assisting in the oxidation of the carboxyl carbon through metal ion catalysis. The metal ion (Mg2+) is helping to orient the substrate properly in the active site. The metal ion (Mg2+) is accepting a proton in order to improve the quality of the leaving group.
- Trypsin uses a nearly identical mechanism as chymotrypsin (including the catalytic triad his57-ser195-asp102. beginning with the enzyme substrate complex draw the complete steps in the trypsin mechanism that occur to release the first product and create the acyl enzyme intermediate in the trypsin active site. The substrate for trypsin to be used is gly-lys-gly-alaWhich of the following is false about chymotrypsin? A Hydrolytic cleavage of a peptide bond by chymotrypsin involves two nucleophilic attacks to the substrate B It is activated in the presence of trypsin C It is synthesized in the thyroid gland D Polypeptide chains in chymotrypsin are linked by S-S bondsPMSF is a molecule used in biochemical research. It inactivates serine proteases by binding covalently to the catalytic serine residue at the active site. Which kind of inhibition does PMSF do? Suicide Mixed O Competitive O Non-competitive