NH, N. NH NH NH2 Benzamidine and Leupeptin are competitive trypsin inhibitors. They are shown in their deprotonated forms at high pH. Modify the above drawings to show the protonation and charge at pH 7.0 Draw competitive inhibitors for chymotrypsin based on these structures ZI
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- 22) answer the following question.. Refer to the kinetic scheme for competitive inhibition and the structures shown below to E+S ES E +P -co- CO- 1 2 EI Compound 1 was determined to act as a competitive inhibitor through standard inhibition studies. Structural studies did not show any resemblance to the transition state. Compound 2 was also determined to act as a competitive inhibitor. Structural studies showed that it does resemble the transition-state. The K, constant is used to assess relative affinity of inhibitors for enzymes. That is, each compound has its own K, value. We can interpret K, the same way we do with Ka values. True or False: K, > Kµ2. Briefly explain your answer.Paraphrasing Tool . medicinal meet Mniversity of Nizwa pKa of flurazepam is 8.71. Ifthe pH of the stomach is 3.5 and that of intestine is 6.0 then oral flurazepam will be t of Flurazepam Select one: a. ionized in the stomach and neutral in the intestine O b. neutral in the stomach and ionized in the intestine O c. ionized in both the stomach and the intestine O d. neutral in both the stomach and the intestine Which of the following molecules is neutral?About 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
- Which of these heterocyclic drugs is likely to be the least soluble in water? Use the Fsp³ parameter to decide. OH Tramadol Chemical Formula: C16H25NO2 YOUR OW Pantoprazole Torasemide Chemical Formula: C16H15F2N3O4S Chemical Formula: C16H20N4O3S Temazepam -OH Chemical Formula: C16H13CIN₂O2 Tioconazole Chemical Formula: C16H13C3N₂OS A. Tramadol B. Pantoprazole C. Torasemide D. Temazepam E. ToconazoleHEPES, 4-(2-hydro)-1-piperazine ethane sulfonic acid, shown below. fully protonated, has pKa’s of 3.00 and 7.55. It is a commonly used buffer for tissue culture and organ storage during transplantation due in part to its effectiveness over a wide temperature range. One-way oxalic acid can be produced in fungi by hydrolysis of oxaloacetate, an intermediate in the Kreb’s citric acid cycle, to produce oxalic acid and acetic acid. This reaction, shown below, is catalyzed by oxaloacetase. [O2CC(O)CH2CO2] 2− + H2O → C2O44−+ CH3COO− + H+ oxaloacetate oxalic acid acetate In a 1-ml reaction mixture containing 50 mM NaCl, 50 mM HEPES, pH 7.8, 5 mM oxaloacetate and 5 pmol oxaloacetase, complete hydrolysis of the oxaloacetate was achieved in 10 minutes of incubation at 30°C. What was the pH of the reaction mixture at the end of the reaction?Think about what part of chymotrypsin, according to our coverage, most contributes to stabilization of the transition state. This contributor is best identified as: Othe acid/base catalyst
- enzyme-inhibitor complex requires 450 kJ.mol-1 to dissociate and that it displays kinetics somehow similar to non-competitive inhibition, this enzyme is good to use to inhibit toxanthine oxidase in the case of hyperuricemia and gout?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.H. OH co co2 но H co, 1-isopropylmalate 2-isopropylmalate Biosynthesis of leucine involves conversion of 1-isopropyimalate to 2-isopropylmalate (see above). This proceeds in four steps under basic enzymic catalysis via an isolable compound produced in step 2. Write a detailed mechanism for this conversion. Then, draw the intermediate compound) produced in step 2. • You do not have to consider stereochemistry. • Draw uninvolved carboxyl groups in the anionic state, and enolates as carbanions. When needed, abbreviate CoenzymeA-S- as CH3S- In your drawing. aale
- Chymotrypsin has the highest affinity for which of the following substrates: Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Chymotrypsin Ки (М) 4.4 x 10-1 8.8 x 10-2 6.6 x 104 Kcat (S-1) 5.1 x 10-2 1.7 x 10-1 1.9 x 102 Substrate N-acetylglycine ethyl ester N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 OA. N-acetylglycine ethyl ester OB. N-acetylvaline ethyl ester OC. N-acetyltyrosine ethyl ester D. UreaDraw the Fischer projection for L-glucose. Drag the appropriate labels to their respective targets. H as OH H =0 C CH₂OH Reset HelpGiven the active site and reaction mechanism below, what is the mechanism of irreversible inhibition of the inhibitor provided? Active Site Reaction Mechanism Inhibitor `NH2. н Он SH OH- OH OH HO- NH „NH OH OH OH -Mg²+ Uncompetitive Affinity-based Transition state analog Non-specific Mechanism-based