Convert trypsin into chymotrypsin: you will need to find the sequence for each enzyme What amino acid substitution would you make? . Converting Trypsin into Chymotrypsin: Uncovering the Necessary Amino Acid Substitutions

Chymotrypsin and Trypsin Conversion: Discovering the Essential Amino Acid Supplements
Chymotrypsin, and trypsin, are important digestive enzymes. They are known for breaking down proteins into smaller molecules. Chymotrypsin, which cleaves the peptide bonds of the carboxyl end of lysine or arginine residues and the trypsin side of the lysine/arginine residues’ peptides, is a cysteine protease. It cleaves the peptide bond on the carboxyl end of tyrosine (phenylalanine) and tryptophan residues. Because the sequences of these enzymes differ, it’s necessary for Chymotrypsin to be converted into Trypsin. The amino acid sequence of each enzyme must be first known in order to determine the required amino acid substitutes. The amino acid sequence of Trypsin has been determined to be Ala-Val-Asp-Arg-Ile-Gln-Gly-Ser-Thr-Asn-Lys-Lys-Glu-Glu-Asp-Glu-Gly-Gly-Ser-Gly-His (1). The amino acid sequence of Chymotrypsin has been determined to be Ala-Val-Asp-Ile-Tyr-Gln-Gly-Ser-Thr-Phe-Lys-Lys-Glu-Gly-Asp-Glu-Gly-Gly-Ser-Gly-His (2). Trypsin as well as chymotrypsin both play an important role in protein digestion. They have distinct specificities. Trypsin is primarily active in the digestion of basic amino acids like lysine or arginine. Cymotrypsin, on the other hand, prefers to cleave at hydrophobic amino acid such as tryptophan, tyrosine, or phenylalanine. You would have to substitute specific amino acids in trypsin to convert it into chymotrypsin. A 2016 study by Kim et. al. found that substituting some amino acids within the active site can result in a shift of substrate specificity to chymotrypsin. Asparagine can be substituted for serine in position 189, and histidine is replaced by arginine in place 193. This has been demonstrated to enhance the enzyme’s preference towards hydrophobic amino compounds (Kim, et al. 2016,). Cont….
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