A common feature of all serine proteases

A common feature of all serine proteases is

    1. Autocatalytic activation of zymogen precursor
    1. Tight binding of pancreatic trypsin inhibitor
    1. Cleavage of protein on the carboxyl site of serine residues
    1. Presence of Ser-His-Asp catalytic triad at the active site

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EXP:

  • The active site of serine proteases contain three critical amino acids Serine. Histidine and Aspartate. These residues are often referred to as the catalytic triad.

  • They are activated by proteolytic activation and not autocatalytic activation.

  • Pancreatic trypsin inhibitor is serine protease inhibitor only for trypsin and not for other serine protease enzymes such as chymotrypsin or elastase. Serine proteases enzymes tightly bind the respective protease inhibitors instead of normal substrates.

  • Serine proteases attack the carbonyl group (not carboxyl group) of peptide bond.