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-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.
Department of Biology, University of Rome 'Roma Tre,&rsquo, Viale Marconi 446, I-00146, Rome, Italy.
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D004789:Enzyme Activation; D016333:HIV Protease / Q000378:metabolism*; D009569:Nitric Oxide / Q000037:antagonists & inhibitors / Q000378:metabolism*; D020030:Nitric Oxide Donors / Q000494:pharmacology; D009574:Nitro Compounds / Q000494:pharmacology; D010084:Oxidation-Reduction
D020030:Nitric Oxide Donors; D009574:Nitro Compounds; D009569:Nitric Oxide; C061872:FK 409; D016333:HIV Protease