Cysteine Nitrosylation Inactivates the HIV-1 Protease

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...

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Veröffentlicht in:	Biochemical and biophysical research communications 1998-09, Vol.250 (3), p.575-576
Hauptverfasser:	Persichini, Tiziana, Colasanti, Marco, Lauro, Giuliana M., Ascenzi, Paolo
Format:	Artikel
Sprache:	eng
Schlagworte:	AIDS/HIV cysteine nitrosylation Enzyme Activation enzyme inhibition HIV Protease - metabolism HIV-1 protease Human immunodeficiency virus 1 nitric oxide Nitric Oxide - antagonists & inhibitors Nitric Oxide - metabolism Nitric Oxide Donors - pharmacology Nitro Compounds - pharmacology Oxidation-Reduction
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Beschreibung
Zusammenfassung:	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.
ISSN:	0006-291X 1090-2104
DOI:	10.1006/bbrc.1998.9350