Chapter

Acid Proteases:Structure, Function, and Biology

Volume 92 of the series Advances in Experimental Medicine and Biology pp 199-210

Pepstatin Inhibition Mechanism

  • Joseph MarciniszynJr.Affiliated withLaboratory of Protein Studies Oklahoma Medical Research Foundation, and the Department of Biochemistry and Molecular Biology, University of Oklahoma School of Medicine
  • , Jean A. HartsuckAffiliated withLaboratory of Protein Studies Oklahoma Medical Research Foundation, and the Department of Biochemistry and Molecular Biology, University of Oklahoma School of Medicine
  • , Jordan TangAffiliated withLaboratory of Protein Studies Oklahoma Medical Research Foundation, and the Department of Biochemistry and Molecular Biology, University of Oklahoma School of Medicine

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Abstract

Pepstatin is a strong inhibitor for all acid proteases. It does not inhibit other groups of proteases, such as the neutral and alkaline proteases (1). The unusual potency of pepstatin toward acid proteases is indicated by its Ki which was reported by Kunimoto et al. (2) to be about 1 × 10−10 M for porcine pepsin. Although its chemical structure has been shown (3) to be a hexapeptide which contains two residues of an unusual amino acid, 4-amino-3-hydroxy-6-methylhepatanoic acid (statine), the mode of inhibition by pepstatin is unknown.