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Structural Consensus Rules for Cysteine Protease Inhibition by NO(-Donors)

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Nitric oxide (NO) exerts its action in several physiological and pathological events. The great propensity for Cys(NO)-(de)nitrosylation represents a mechanism which modulates cysteine protease action. Cys(NO)-(de)nitrosylation is assisted by basic and acid residues, within the environment of the Cys catalytic residue. In particular, Cys-nitrosylation is catalyzed by amino acid residues which stabilize the reactive deprotonated form of the Cys Sγ atom. By contrast, CysNO-denitrosylation is assisted by amino acid residues which facilitate the protonation of the Cys Sγ atom with the concomitant NO release. Note that Cysnitrosylated residues may undergo oxidation giving rise to sulfenic, sulfinic or sulfonic acid and lead to the formation of disulfide bridges. These structural consensus rules apply not only to cysteine proteases, but represent a generally accepted mechanism for (macro)molecular Cys(NO)-(de)nitrosylation.
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Keywords: acid-base catalysis; cys-nitrosylation; cysno-denitrosylation; cysteine protease; enzyme inhibition; nitric oxide; structural consensus rules

Document Type: Review Article

Affiliations: Department of Biology and Interdepartmental Laboratory for Electron Microscopy, University 'Roma Tre', Viale Guglielmo Marconi 446, I-00146 Rome, Italy.

Publication date: 2005-11-01

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  • Current Enzyme Inhibition aims to publish all the latest and outstanding developments in enzyme inhibition studies with regards to the mechanisms of inhibitory processes of enzymes, recognition of active sites, and the discovery of agonists and antagonists, leading to the design and development of new drugs of significant therapeutic value. Each issue contains a series of timely, in-depth reviews written by leaders in the field, covering a range of enzymes that can be exploited for drug development. Current Enzyme Inhibition is an essential journal for every pharmaceutical and medicinal chemist who wishes to have up-to-date knowledge about each and every development in the study of enzyme inhibition.
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