Cysteine Nitrosylation Inactivates the HIV-1 Protease

descriptionPublicationkeyboard_double_arrow_right Article 01 Sep 1998 Italy English Publisher:Elsevier BVJournal:Biochemical and Biophysical Research Communications, volume 250, pages 575-576 (issn: 0006-291X,

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Authors: PERSICHINI T; COLASANTI M; LAURO GM; ASCENZI, Paolo;

doi: 10.1006/bbrc.1998.9350

pmid: 9784385

handle: 11590/115763 , 11590/136221 , 11590/151859

Cysteine Nitrosylation Inactivates the HIV-1 Protease

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Abstract

Nitric oxide (NO) may modulate the catalytic activity of cysteine-containing enzymes. HIV-1 protease action is modulated by the redox equilibrium of Cys67 and Cys95 regulatory residues. In the present study, the inhibitory effect of NO, released by the NO-donor (+/-)-(E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide (NOR-3), on the aspartyl HIV-1 protease action is reported. HIV-1 protease inactivation via NO-mediated nitrosylation of Cys regulatory residue(s) may represent a possible mechanism for inhibition of HIV-1 replication.

Country

Italy

Related Organizations

Roma Tre University
Italy

Keywords

Enzyme Activation, HIV Protease, Nitric Oxide Donors, Nitric Oxide, Nitro Compounds, Oxidation-Reduction

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