enzyme that convert inactive chymotrypsinogen into its active form
Answers
Answer:
Chymotrypsinogen must be inactive until it gets to the digestive tract. This prevents damage to the pancreas or any other organs. It is activated into its active form by another enzyme called trypsin.
Explanation:
Trypsin is an enzyme that aids with digestion. An enzyme is a protein that speeds up a certain biochemical reaction. Trypsin is found in the small intestine. It can also be made from fungus, plants, and bacteria.
Trypsin breaks peptides down into amino acids. Lipase breaks fats down into fatty acids and glycerol.
Various proteolytic enzymes are used to detach cells from the adherent substrate, of which the trypsin a member of serine protease family is most frequently used. ... Long term incubation with high trypsin concentration damage cells by striping cell surface proteins and kill the cells.
Trypsin cleaves the peptide bond between the carboxyl group of arginine or the carboxyl group of lysine and the amino group of the adjacent amino acid. The rate of cleavage occurs more slowly when the lysine and arginine residues are adjacent to acidic amino acids in the sequence or cystine.
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