Converting Trypsin and Chymotrypsin: A Comparison of Amino Acid Substitutions
The activity of trypsin and chymotrypsin are essential components of the digestive system and are present in the human body, as well as in other animals. These proteins are digestive enzymes that hydrolyze proteins into smaller peptides and amino acids, allowing for the absorption of nutrients in the body. Trypsin and chymotrypsin are both serine proteases, meaning they use the non-ionic serine residue to hydrolyze target proteins (Kang et al., 2019). The two enzymes have different enzymatic activities, with trypsin being more active than chymotrypsin (Kang et al., 2019). Trypsin and Chymotrypsin are two important enzymes found in the digestive system of many animals. Both enzymes play an important role in the digestion of proteins by breaking down the protein into smaller peptide fragments. However, the two enzymes have different amino acid sequences and therefore, in order to convert one enzyme into the other, it is necessary to make specific amino acid substitutions. The amino acid sequence of Trypsin, according to a study published in 2019, is composed of Arg-Ile-Asp-Gly-Ser-Phe-Pro-Arg-Ala-Gly-Gly-Thr-Gly-His-Gly-Asn (1). Similarly, the amino acid sequence of Chymotrypsin is composed of Tyr-Ile-Asp-Gly-Ser-Phe-Ser-Lys-Ala-Gly-Gly-Thr-Gly-His-Gly-Asn (2). To convert Trypsin into Chymotrypsin, it is necessary to make two amino acid substitutions, namely substituting a Lysine for the Proline at position 7 and a Tyrosine for the Arginine at position 1. Cont…..
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