Cysteine nitrosylation inactivates the HIV-1 protease
T Persichini, M Colasanti, GM Lauro… - … and Biophysical Research …, 1998 - Elsevier
T Persichini, M Colasanti, GM Lauro, P Ascenzi
Biochemical and Biophysical Research Communications, 1998•ElsevierNitric 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 …
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 …
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.
Elsevier
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