Inhibitors of human neutrophil cathepsin G: structural and biochemical studies
Groutas, William C. Brubaker, Michael J. Venkataraman, Radhika Epp, Jeffrey B. Stanga, Michael A. McClenahan, Jerald J.
Groutas, William C.
Brubaker, Michael J.
Venkataraman, Radhika
Epp, Jeffrey B.
Stanga, Michael A.
McClenahan, Jerald J.
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1992-04-01
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Article
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Research Support, U.S. Gov't, P.H.S.
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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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Full text of this article is not available in SOAR.
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Elsevier
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Archives of Biochemistry and Biophysics
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NLM
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0003-9861