Inhibitors of human neutrophil cathepsin G: structural and biochemical studies

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Issue Date
1992-04-01
Authors
Groutas, William C.
Brubaker, Michael J.
Venkataraman, Radhika
Epp, Jeffrey B.
Stanga, Michael A.
McClenahan, Jerald J.
Advisor
Citation

Archives of biochemistry and biophysics. 1992 Apr; 294(1): 144-6.

Abstract

The interaction of a series of sulfonate and phosphate esters derived from N-hydroxysuccinimide with human leukocyte cathepsin G was investigated. The synthesized compounds were found to be time-dependent inhibitors of the enzyme. The composite interplay of steric and electronic effects leads to the formation of acyl enzymes of variable stability, ultimately resulting in partial or full recovery of enzymatic activity. Compounds acting via phosphorylation of the active site serine inactivated the enzyme rapidly and irreversibly.

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