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- 1.) Propose the biosynthesis of 5-methylorsellinic acid: CH3 НО. CH3 `CO,H OHConsidering the general structure of penicillins, how are they rendered ineffective? Select one: O a B-Lactamase performs nucleophilic attack of the amide in the penicillin side chain Ob. B-Lactamase performs nucleophilic attack of the amide in the B-lactam ring and subsequently hydrolyzes this intermediate OC. B-Lactamase performs nucleophilic attack of the thiazolidone ring on the carbon next to the electronegative sulfur leading to a covalently inhibited B-Lactamase o d. All of these O e. None of theseOutline the key strategy used to reduce the sensitivity of the beta-lactam ring of a penicillin to hydrolysis, illustrating your answer by describing three examples of structural modification.
- Draw a stepwise mechanism for the following reaction. The fourmemberedring in the starting material and product is called a β-lactam.This functional group confers biological activity on penicillin and many related antibiotics. (Hint: The mechanism begins with β elimination and involves only two steps.)Show how you would accomplish the following synthetic transformations. Show all intermediates.(a) 2,2@dibromobutane ¡ but@1@yne (b) 2,2@dibromobutane ¡ but@2@yne(c) but@1@yne ¡ oct@3@yne (d) trans@hex@2@ene ¡ hex@2@yne(e) 2,2@dibromohexane ¡ hex@1@yne (f) cyclodecyne ¡ cis@cyclodecene(g) cyclodecyne ¡ trans@cyclodecene (h) hex@1@yne ¡ hexan@2@one, CH3COCH2CH2CH2CH3(i) hex@1@yne ¡ hexanal, CH3(CH2)4CHO (j) trans@hex@2@ene ¡ cis@hex@2@enePropose a reasonable synthetic route for the preparation of the substituted benzene derivative shown below. You may use whatever reagents are necessary to transform the starting molecule into the desired product. CH(CH3)2 step 1 step 2 step 3 čOH Step 1 reagent/reagents %3D Step 2 reagent/reagents %3D Step 3 reagent/reagents
- Define the following: 1. Cofactor 2. Coenzyme 3. "-ase" ending1 ).Which of the following accurately describes substrate specificity for serine proteases? A.The binding cleft B.Mg2+ metal activated enzyme C.The catalytic triad D.Facilitates redox chemistry E.Stabilizes the transition state 2). Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? select all that apply leucine aspartic acid histidine lysine Please answer both correct i will give u upvote.Given the active site diagram below, which circled component coordinates the cofactor? 1 5 NH+ Mn²+ 3 4 2 5 1 *H3N. N H₂ HN O NH₂+ Mn²+ -3
- One of the main sources of sphingosine in the body is in the cell membrane. What complication could arise from the biological synthesis of ceramide?Lysosyme catalyzes the hydrolysis of the carbohydrate linkage in part of the bacterial cell wall (peptidoglycan layer). 1. Propose a mechanism using general acid/base catalysis 2. Propose a mechanism using covalent catalysis. (An intermediate has been observed that indicates a glycosidic bond to the aspartate).A decapeptide which could resist burns was isolated from an endemic plant from Mt. Mayon. Deduce the amino acid sequence of the decapeptide given the following informations. Mercaptoethanol gave two pentapeptides F1 and F2. Chymotrypsin treatment of F1 releases S and a tetrapeptide (C,K,F,M) while F2 gave a dipeptide (M,S) and a tripeptide (C,F,K) F1 when treated with CNBr released a free homoserine lactone and a tetrapeptide. Trypsin treatment of F1 gave a tripeptide and a dipeptide. F2 treated with carboxypeptidase released free M while with trypsin gave free K and a tetrapeptide.