Cysteine nitrosylation inactivates the HIV-1 protease.

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.

Cite this paper

@article{Persichini1998CysteineNI, title={Cysteine nitrosylation inactivates the HIV-1 protease.}, author={Tiziana Persichini and Marco Colasanti and Giuliana Maria Lauro and Paolo Ascenzi}, journal={Biochemical and biophysical research communications}, year={1998}, volume={250 3}, pages={575-6} }