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Protein (Hydrolysis (Protease specficity is determined by adjacent amino…

- - - - trypsin
        
        secreted by the pancreas to hydrolyse polypeptides and chymotrypsinogen in the small intestine.
        
        derived from trypsinogen
        and activated by membrane-
        bound enterokinase.
      - chymotrypsin
        
        secreted by the pancreas and
        hydrolyses polypeptides in
        the small intestine.
        
        derived from chymotrypsinogen
        and activated by active trypsin.
      - pepsin
        
        secreted in the stomach to hydrolyse proteins and inactive pepsinogen in the stomach.
        
        protein interaction w/in pepsinogen
        covers the catalytic domain.
        
        the masking peptide chain unbinds
        due to a change in polarity at low pH
        levels in the stomach (protonation)
        
        protease cleaves itself to release a
        fragment of peptide off the chain,
        leading to the formation of pepsin
  - - - such as lysine
        and arginine
    - - such as tyrosine
        and phenylalanine
  - - - attack peptide bonds w/in the peptide / protein chain
        
        include pepsin, trypsin, and chymotrypsin.
    - - attack paptide bonds at the
        end of the peptide chain.
        
        two types: aminopeptidase and carboxypeptidase
        
        both active in the small intestine, and gives rise to amino acids and di/tri-peptides.
- - - - at least six different types.
      - almost identical to the SLGT-1
        transporter mechanism w/ glucose.