Cysteine nitrosylation inactivates the HIV-1 protease.
作者信息
Persichini T, Colasanti M, Lauro G M, Ascenzi P
机构信息
Department of Biology, University of Rome 'Roma Tre,&rsquo, Viale Marconi 446, I-00146, Rome, Italy.
出版信息
Biochem Biophys Res Commun. 1998 Sep 29;250(3):575-6. doi: 10.1006/bbrc.1998.9350.
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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