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 | |
| 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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Cite this
Persichini, T., Colasanti, M., Lauro, G. M., & Ascenzi, P. (1998). Cysteine nitrosylation inactivates the HIV-1 protease. Biochemical and Biophysical Research Communications, 250(3), 575-576. https://doi.org/10.1006/bbrc.1998.9350