1. Alkaline phosphatase has a key serine residue in the active site that is critical for biological activity. Suggest a plausible four-step arrow-pushing mechanism for hydrolysis of phosphate Ser 0-00 Ser oo 0 0 0) phosphoserine intermediate
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- Bradykinin is a linear nonapeptide released by blood plasma globulin in response to a wasp sting. It is a very potent pain-causing agent. Its constituent amino acids are 2R, G, 2F, 3P, S. The sue of 2,4-dinitrofluorobenzene and carboxypeptidase shows that both terminal residues are arginine. Partial hydrolysis of bradykinin gives the following di- and tripeptides: FS + PGF +PP + SPF + FR + RPSerine esterase contains a catalytic triad at its active site. Which amino acid in serine esterase is responsible for mediating general acid catalysis for the breakdown of tetrahedral intermediate to the carboxyl product? Explain.A nonapeptide released by globulins in the blood in response to a waspsting. Hydrolysis gives the following amino acids: 2 Arg, Gly, 2 Phe, 3 Pro, and Ser.Edman degradation gives phenylthiohydantoin of Arg. Cleavage with carboxypeptidase gives Arg. Partial hydrolysis gives the following di- and tripeptides: Phe-Ser, Pro-GlyPhe, Pro-Pro, Ser-Pro-Phe, Phe-Arg, and Arg-Pro. What is the amino acid sequence of this peptide?
- 4b) Canavanine is closely related to arginine, and like arginine its side group has a +1 charge when protonated. If you dissolved canavanine in an aqueous solution at pH 10, what would the net charge on a molecule of canavanine be? Please show your work or make it clear how you determined the charge contribution from each ionizable group.suggest a plausible arrow-pushing mechanism for the formation of a covalent adduct between the suicide inhibitor 5-trifluoromethyluridylic acid and thymidylate synthase that involves the active_site thiolate.Given the following peptide SEPIMAPVEYPK(a) Estimate the net charge at pH 7 and at pH 12. Assume the pKa valuesgiven in as shown. (b) How many peptides would result if this peptide were treated with(1) cyanogen bromide, (2) trypsin, or (3) chymotrypsin?(c) Suggest a method for separating the peptides produced by chymotrypsintreatment.
- Given the following peptideSEPIMAPVEYPK(a) Estimate the net charge at pH 7 and at pH 12. Assume the pKa valuesgiven in Table (b) How many peptides would result if this peptide were treated with(1) cyanogen bromide, (2) trypsin, or (3) chymotrypsin?(c) Suggest a method for separating the peptides produced by chymotrypsintreatment.The conversion of methionine to homocysteine requires folate (N5-methyl THF) while the remethylation of homocysteine to methionine requires Vitamin B12. Describe at least two different ways in which these enzymatic reactions could be positively influenced to help reduce this individual's homocysteine levels.Show the steps and intermediates in the synthesis of Leu-Ala-Phe by the solid-phase process.2
- 1. Taking the structure of the amino acids into account, give a comparative discussion pK values where histidine=2 and alanine=2.The overall adenylate kinase reaction (2 ADP = AMP + ATP) is a combination of 3 reactions: ATP hydrolysis, pyrophosphate hydrolysis, and ATP formation. Show each step and provide the standard free energy (ΔG°′) for each and the overall reaction. If the adenylate kinase reaction is at equilibrium and intracellular [ATP] = 5 mM and [ADP] = 0.5 mM, calculate the concentration of AMP at pH 7 and 25 °C. Show all work. ATP (ADP+P) = -30.5 kj/mol; ATP (AMP+PP) = -45.6 kj/mol; PP = -19.2 kj/molMatch the following methods of Analysis Fractional analysis, methylation, and periodate oxidation Use of endo- and exoglycosidases Polarimetry, mass spectrometry, & NMR Chromatographic separations of hydrolyzed fragments A. Chemical Method B. Enzymatic Method C. No Match D. Spectroscopic