. The first two steps of ovothiol C biosynthesis are shown below. Propose the rest of the pathway, indicating the potential involve- ment of cofactors. co- coo H NH,* Histidine Fo*, 02 reductant .coo- *H,N° coo- *H,N° COO HS* NH,* 5-Histidylcysteine sulfoxide conjugate 5-Histidylcysteine thioether conjugate Cysteine
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- Shown below is a substrate for a Trypsin. Draw the mechanism for this serine protease using the artificial substrate. Be sure to draw the catalytic triad, and show the role of the oxyanion hole. Draw the complete structure of every intermediate and product and PUSH ARROWS!!!!! Do not abbreviate structures using R and R' H₂N _N_CH. сно CH₂ CH₂ CH₂ NH d=19H₂ NH₂ O CH- H₂C HN O CHThe diagram below shows the substrate binding cleft for a protease, providing the substrate structure, and indicating the residues (using one-letter code) that line the four specificity pockets. 1 M F H₂N K R IZ 2 3 P F S W оо E 4 The protease is known to cleave the amide linkage between W and E residues for substrates containing the WEFD sequence. Using 3-letter code with amino acids linked by a "dash" (ex. GLY-ALA), the N-terminal product is A and the C-terminal product is AWhich of the following statements about ribozyme catalytic residues is INCORRECT? General acid catalysis requires the standarde nucleotide exchangeable proton acidities (represented by pKa values). Ribozymes work by lowering the AG‡ through transition state stabilization without changing the overall AG of the reaction. Some ribozymes cleave phosphodiester bonds, and like proteases, can be autocatalytic. There are fewer known classes of mammalian ribozymes than mammalian enzyles.
- In this step of purine biosynthesis, which functional group gets activated by ATP Pribose NH, ATP Carboxyaminolmidazole ribonedeotide Asp AD Fumarate Pribose NH, S-Aminolmidazole- 4(N-succinylcarboxamide) ribonucleotide O Carboxyaminoimidazole ribonucleotide COOH O Carboxyaminoimidazole ribonucleotide NH2 O Asp side chain COOH O Asp main chain NH2 O Asp main chain COOHLysozyme catalyzes a "bi-bi" reaction, which means there are (how many) reactants and (how many) products. List, in order, the reactants that bind and the products that are released during a lysozyme-catalyzed reaction cycle -- be succinct but be specific. 1. First reactant = 2. First product = 3. Second reactant = 4. Second product %3DIn serine protease catalytic triad mechanism, the first and second products that leaves the active site are Carboxylic acid and amide respectively Amide and carboxylic acid respectively Ester and amide respectively Carboxylic acid and ester respectively
- Shown below is a substrate for a Elastase. CH, HN NH NH, Draw the mechanism for this serine protease using the artificial substrate. Be sure to draw the catalytic triad, and show the role of the oxyanion hole. Draw the complete structure of every intermediate and product and PUSH ARROWS!Consider 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.Which substrate is the best substrate for chymotrypsin? O N-acetylphenylalanine ethyl ester with Km of 8.2 x 102 M and keat of 2.1 x 102 sec 1. O N-acetylmethionine ethyl ester with Km of 12.3 x 102 M and keat of 2.1 x 1o sec1. O N-acetylleucine ethyl ester with Km of 8.2 x 10o2 M and kcat of 4.1 x 102 sec1. O N-acetylalanine ethyl ester with Km of 4.1 x 101 M and kcat of 4.1 x 101 sec.
- . The mechanism for lysozyme cleavage of its polysaccharide substrate requires Glu35 in its nonionized form, whereas the nearby Asp52 must be ionized (see the figure below). The pK values for the side-chain carboxyl groups on the two amino acids in solution are virtually identical. a) How can one carboxyl group be charged and the other uncharged in the active site of lysozyme? b) The pH optimum for lysozyme is about 5. Why do you suppose that the activity decreases above and below this optimum? Glu3s NAG Asp52 0-H Glu35 -C Asp52 tri-NAG NAGRefer to the figure. Portions of three biosynthetic pathways regulated through feedback inhibition and activation are shown. Two of these pathways intersect at carbamoyl phosphate. The third pathway generates a product that activates production of carbamoyl phosphate through allosteric modification of the enzyme carbamoyl phosphate synthetase. Arginine pathway Pyrimidine pathway Glutamate СТР Purine pathway N-acetylglutamate synthetase N-acetylglutamate UMP UMP ATCase Ornithine СР CO, + ATP Carbamoyl phosphate synthetase + Gin t-Arginine In this set of pathways, arginine biosynthesis is shut down through feedback inhibition when and arginine reach high levels of concentration. О СТР O ornithine O UMP O carbamoyl phosphate O glutamate.Propose a mechanism for the conversion of 5- formamidoimidazole-4- carboxamide ribonucleotide into inosinate.