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Where is endopeptidase made?

Updated: 12/5/2022
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Q: Where is endopeptidase made?
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The protein-based digestive enzyme endopeptidase is produced?

during interphase


What is the difference between endopeptidase and ectopeptidase?

Endopeptidase targets peptide links between amino acids in the middle of the protein chain whereas exopeptidases (or ectopeptidases) target the available "ends" of the amino acid chain. This is explains why in the Human body proteins are subject to endopeptidase action before exopeptidase to ensure the maximum amount of "ends" (larger surface area) is possible, increasing efficiency.


Is trypsin a protein?

No, trypsinogen is a zymogen, an enzyme precursor, an inactive chemical produced by the pancreas. In the intestine, trypsinogen is activated by the mucosal enzyme enteropeptidease to produce the enzyme trypsin which is critical to digestion.


Why is it important that trypsin cuts only specific peptide bonds?

Trypsin is considered an endopeptidase, i.e., the cleavage occurs within the polypeptide chain rather than at the terminal amino acids located at the ends of polypeptides. By breaking bonds in the middle of the protein chain, it serves to stabilize the developing negative charge on the carbonyl oxygen atom of the cleaved amides. Only a small amount of enteropeptidase is necessary to start the reaction. This activation mechanism is common for most serine proteases, and serves to prevent autodigestion of the pancreas.


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