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An aspartic protease analogue: intermolecular catalysis of peptide hydrolysis by carboxyl groups
1School of Chemistry and Molecular Engineering and Center for Molecular Catalysis, Seoul National University, 151-747, Seoul, Republic of Korea.
Bioorganic & Medicinal Chemistry Letters
|May 30, 2001
Abstract:
Two aspartic carboxyl groups act as key catalytic groups in the active site of an aspartic protease. We synthesized an aspartic protease analogue by positioning three salicylate residues in close proximity on a cross-linked polystyrene. The immobile artificial protease effectively hydrolyzed albumin into many small fragments by the catalytic action of carboxyl groups contained in the active site. The artificial protease manifested optimum activity at pH 3 just as aspartic proteases.