Abstract
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.
Keywords: nitric oxide, cysteine protease, enzyme inhibition, cys-nitrosylation, cysno-denitrosylation, acid-base catalysis, structural consensus rules
Current Enzyme Inhibition
Title: Structural Consensus Rules for Cysteine Protease Inhibition by NO(-Donors)
Volume: 1 Issue: 3
Author(s): Paolo Ascenzi, Alessio Bocedi, Fabio Polticelli and Martino Bolognesi
Affiliation:
Keywords: nitric oxide, cysteine protease, enzyme inhibition, cys-nitrosylation, cysno-denitrosylation, acid-base catalysis, structural consensus rules
Abstract: 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.
Export Options
About this article
Cite this article as:
Ascenzi Paolo, Bocedi Alessio, Polticelli Fabio and Bolognesi Martino, Structural Consensus Rules for Cysteine Protease Inhibition by NO(-Donors), Current Enzyme Inhibition 2005; 1 (3) . https://dx.doi.org/10.2174/157340805774580448
DOI https://dx.doi.org/10.2174/157340805774580448 |
Print ISSN 1573-4080 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-6662 |
![](/images/wayfinder.jpg)
- Author Guidelines
- Bentham Author Support Services (BASS)
- Graphical Abstracts
- Fabricating and Stating False Information
- Research Misconduct
- Post Publication Discussions and Corrections
- Publishing Ethics and Rectitude
- Increase Visibility of Your Article
- Archiving Policies
- Peer Review Workflow
- Order Your Article Before Print
- Promote Your Article
- Manuscript Transfer Facility
- Editorial Policies
- Allegations from Whistleblowers
- Announcements