Cysteine nitrosylation inactivates the HIV-1 protease

Biochem Biophys Res Commun. 1998 Sep 29;250(3):575-6. doi: 10.1006/bbrc.1998.9350.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzyme Activation
  • HIV Protease / metabolism*
  • Nitric Oxide / antagonists & inhibitors
  • Nitric Oxide / metabolism*
  • Nitric Oxide Donors / pharmacology
  • Nitro Compounds / pharmacology
  • Oxidation-Reduction

Substances

  • Nitric Oxide Donors
  • Nitro Compounds
  • Nitric Oxide
  • FK 409
  • HIV Protease