9. Devise a reaction path for the following synthesis. Indicate any required reagent(s) and show the structures of the major product after each step. Do not give mechanism/arrow pushing. Br OH CH2CH3
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- . 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 Cysteine12 Determine the type of biochemical reaction that occurs in the reaction shown below. O O O O O redox isomerization group C-C bond formation/cleavage transfer hydrolysis/condensation Previous Ex-xx-xx OH (ATP) OH OH OH OH + AMP OH OPO₂² OH OH +AMP1 OH (ADP)Please don't provide handwritten solution...
- Can the target compound at right be efficiently synthesized from the starting material at left? Br starting material Br ? Br target If so, draw a synthesis below. If no synthesis using reagents ALEKS recognizes is possible, check the box under the drawing area. Be sure you follow the standard ALEKS rules for submitting syntheses. More... Br : ☐ T Add/Remove step X Br G Br ос E ol Ar5Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
- Could you please assist as to what would be the correct reaction?1. Please fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysis exemplified by the serine protease: Chymotrypsin. In your answer discuss employing the illustration whenever possible: the overall reaction mechanism, stability of the reaction transition state, proximity and orientation effects, acid-base catalysis, and covalent catalysis. (c) (0) Ap Asp Toe His Asp 10 C-N bond cleavage HN Ho Ser Ger Binding of substi 196 Ser Gly alto video LBHB NH Sere HAR Proton donation by H (h) Fel of amino product yest OHN Hig Ser Ap (0) Formation of covalent (ES) Alp Me complex Serios2
- Associate the biochemical reaction in TSI agar to certain genera or species. Reaction Possible Organism(s) K/K K/A K/A, H2S* A/A A/A A/A, H2S*VII. Analysis of a peptide antibiotic purified from a strain of Bacillus brevii resulted in the following significant information: Complete hydrolysis of the peptide yielded equimolar amounts of Leu, Orn, Phe, Pro, and Val Molecular weight of the peptide was estimated to be aroung 1,200 Da The peptide failed to undergo hydrolysis when treated with carboxypeptidase Partial hydrolysis and then chromatographic separation of products yielded the following di- and tripeptides: Leu-Phe, Phe-Pro, Orn-Leu, Val-Orn, Val-Orn-Leu, Phe-Pro-Val, Pro-Val-Orn Treament with dinitrofluorobenzene (DNFB) followed by complete hydrolysis yielded only free amino acids and the DNFB-derivatized ornithine at its side chain Using this set of information available to you, deduce the amino acid sequence of this peptide antibiotic. Write your final peptide sequence only using 3-letter abbreviations.8.1
