Cysteine nitrosylation inactivates the HIV-1 protease

Tiziana Persichini; Marco Colasanti; Giuliana M. Lauro; Paolo Ascenzi

doi:10.1006/bbrc.1998.9350

Cysteine nitrosylation inactivates the HIV-1 protease

Tiziana Persichini, Marco Colasanti, Giuliana M. Lauro, Paolo Ascenzi

Istituto Nazionale per le Malattie Infettive Lazzaro Spallanzani

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	575-576
Number of pages	2
Journal	Biochemical and Biophysical Research Communications
Volume	250
Issue number	3
DOIs	https://doi.org/10.1006/bbrc.1998.9350
Publication status	Published - Sep 29 1998

Keywords

Cysteine nitrosylation
Enzyme inhibition
HIV-1 protease
Nitric oxide

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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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.",

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AU - Persichini, Tiziana

AU - Colasanti, Marco

AU - Lauro, Giuliana M.

AU - Ascenzi, Paolo

PY - 1998/9/29

Y1 - 1998/9/29

N2 - 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.

AB - 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.

KW - Cysteine nitrosylation

KW - Enzyme inhibition

KW - HIV-1 protease

KW - Nitric oxide

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Cysteine nitrosylation inactivates the HIV-1 protease

Abstract

Keywords

ASJC Scopus subject areas

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