In the chemical mechanism of chymotrypsin, the group that acts as a general base in the deacylation half reaction is O an O of a Ser hydroxyl the unprotonated carboxylate of an Asp the unprotonated imidazole of a His residue an OH from H2O the unprotonated a-amino group
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- Draw the tripeptide val-glu-his as it exists under physiological pH. Write the reaction for the hydrolysis of this tripeptide into the individual amino acids. Be sure to show the reaction conditions and the final products that result under these conditions.Name and draw the structure of the a-keto acid resulting when each of the following amino acids undergoes transamination with a-ketoglutarate: (a) aspartate, (b) glutamate, (c) alanine, (d) phenylalanine.The amln0 acid histldine ls usually found in actlve sltes 0f enzymes. What structural feature does the R group of hlstidine have that may be important for the activity of enzymes? Explain
- the following peptide is incubated as chymotrypsin: Gly-Val-Phe-Lys-Ala. Present the detailed chemical mechanism by which chymotrypsin hydrolyzes this peptide. Briefly explain each step. Include only the structure of the final products of the reaction.Why double bonds of fatty acids in our body are generally in cis for?Ala Leu Glu Glu Asn Ala represent the following amino acid in its predominant form at pH= 7
- If D-glyceraldehyde-3-phosphate (DGAP) is dissolved in water, 96% of it will form dihydroxy- acetonephosphate (DHAP). Which of the following will triose phosphate isomerase do? a)Shift the balance to 100% DHAP b)Shift the balance to 0% DHAP c)Catalyze the peptide bond breaking d)Make the reaction fasterDescribe the structures of glutamine and alanine. What are the characteristics of the R-groups? What other features of these amino acids make them important as they relate to metabolism?. A nervous polecat. Pyrrolysine (Pyl, O) and Selenocysteine (Sec, U) are two uncommon amino acids. Knowing that these amino acids exists, translate the following amino acid sequence into one – letter code: Thr – Trp – Ile – Thr – Cys – His – Tyr – Leu – Ile – Thr – Thr – Ile – Glu – Phe – Glu – Arg – Arg – Glu – Thr – Ala – Arg – Glu – Asn – Thr – Tyr – Pyl – Sec – Met – Ala – Leu – Phe – Pyl – Tyr.
- With regards to arganine illustrate the pH-dependent transitions on a titration graph from most to least protonated. Indicate also the relevant part of the amino acid which is associated with the transition on that part of the graph.Over time, the glutamine residues of polypeptides are susceptible to deamidation, a reaction in which the amide group is replaced by a carboxylate group. What amino acid is produced when glutamine is deamidated?Some amino acids are synthesized by replacing the keto group (CO) of an organic acid known as an α-keto acid with an amino group (CNH+3). Identify the amino acids that can be produced this way from the following α-keto acids: