pH dependence of bovine mast cell tryptase catalytic activity and of its inhibition by 4',6-diamidino-2-phenylindole

FEBS Letters
L FiorucciF Ascoli

Abstract

Tryptases are oligomeric enzymes localized in the secretory granules of mast cells. Their role(s) in vivo has yet to be clarified and the lack of powerful and specific inhibitors has hampered the comprehension of the biological functions of these enzymes. In this paper, we identify 4',6-diamidino-2-phenylindole as a potent inhibitor for bovine tryptase. This inhibitory effect and the enzyme catalyzed hydrolysis of the synthetic substrate Boc-Phe-Ser-Arg-methyl-coumarin were investigated in the pH range of 6.0-9.0. On the basis of the pK shifts occurring upon formation of the inhibitor(substrate)/enzyme complexes, some aminoacidic groups are proposed to play a role in such interactions.

References

Oct 1, 1992·Biological Chemistry Hoppe-Seyler·J StürzebecherC P Sommerhoff
Jul 1, 1992·Biological Chemistry Hoppe-Seyler·L FiorucciF Ascoli
May 21, 1991·Biochemistry·V J Braganza, W H Simmons
Nov 1, 1987·Archives of Biochemistry and Biophysics·G H CaugheyJ A Nadel
Jun 1, 1985·Archives of Biochemistry and Biophysics·H KidoN Katunuma
Apr 17, 1995·FEBS Letters·L FiorucciF Ascoli
Jan 1, 1964·Advances in Protein Chemistry·J WYMAN

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Citations

Dec 29, 2005·Bioorganic & Medicinal Chemistry·Olga N BurchakMaxim Y Balakirev
Dec 25, 2008·Chemical Reviews·M Sameiro T Gonçalves

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