| MadSci Network: General Biology |
Dear CP:
Thanks for your interesting question.
Pepsin, as you know, is an enzyme secreted in the stomach which digests
proteins by cleaving peptide bonds, which link the amino acids that
comprise a protein. Most enzymes, including pepsin, are proteins.
The answer to you question is that pepsin does indeed digest other pepsin
molecules. However, during a meal, pepsin molecules will be far outnumbered
by other proteins, thus a pepsin molecule will run into many other peptide
bonds to cleave before it runs into another pepsin molecule. Also, pepsin
will be continually secreted by the stomach during a meal.
Side point: it is possible that pepsin digests itself less readily than
other proteins. This is because pepsin is most active at cleaving the
peptide bond between two hydrophobic amino acids. The amino acids in
pepsin are arranged such most of the amino acids on the surface are
hydrophilic.
Ray Hsu
hsurm@medicine.wustl.edu
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