Examination of N-hydroxylation as a prerequisite mechanism of nitric oxide synthase inactivation.
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.
Maurer
T S
TS
Department of Pharmaceutics, School of Pharmacy, University at Buffalo, State University of New York, 14260-1200, USA.
Pan
J
J
Booth
B P
BP
Kalman
T I
TI
Fung
H L
HL
D001667:Binding, Competitive; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006900:Hydroxylation; D008239:Lysine / Q000031:analogs & derivatives* / Q000494:pharmacology; D019001:Nitric Oxide Synthase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D009952:Ornithine / Q000031:analogs & derivatives* / Q000494:pharmacology
D004791:Enzyme Inhibitors; C090663:N(6)-(1-iminoethyl)lysine; C065027:N(G)-iminoethylornithine; D009952:Ornithine; D019001:Nitric Oxide Synthase; D008239:Lysine