Examination of N-hydroxylation as a prerequisite mechanism of nitric oxide synthase inactivation

Bioorg Med Chem Lett. 2000 May 15;10(10):1077-80. doi: 10.1016/s0960-894x(00)00171-2.

Abstract

L-N5-(1-Hydroxyiminoethyl)-ornithine (L-NHIO) and L-N6-(1-hydroxyiminoethyl)-lysine (L-NHIL) were synthesized and tested as potential intermediates in the mechanism-based inactivation of nitric oxide synthase (NOS) by L-N5-iminoethylornithine (L-NIO) and L-N6-iminoethyllysine (L-NIL). Although these compounds were determined to be competitive inhibitors, mechanism-based inactivation was not observed.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding, Competitive
  • Enzyme Activation
  • Enzyme Inhibitors / pharmacology
  • Hydroxylation
  • Lysine / analogs & derivatives*
  • Lysine / pharmacology
  • Nitric Oxide Synthase / antagonists & inhibitors
  • Nitric Oxide Synthase / chemistry
  • Nitric Oxide Synthase / metabolism*
  • Ornithine / analogs & derivatives*
  • Ornithine / pharmacology

Substances

  • Enzyme Inhibitors
  • N(6)-(1-iminoethyl)lysine
  • N(G)-iminoethylornithine
  • Ornithine
  • Nitric Oxide Synthase
  • Lysine