Synthesis and tyrosinase inhibitory activity of novel N-hydroxybenzyl-N-nitrosohydroxylamines.
Several novel N-substituted N-nitrosohydroxylamines were synthesized. They all inhibited mushroom tyrosinase, but the type of inhibition was different depending on the substituent. Some N-(mono- or dihydroxybenzyl)-N-nitrosohydroxylamines exhibited uncompetitive inhibition with respect to L-dopa. Among them, compound 6 was also a competitive inhibitor with respect to oxygen. This observation suggests that another interaction by the meta- or para-hydroxyl group might stabilize the binding of the inhibitor to the enzyme through the oxygen binding site.
Shiino
Mitsuhiro
M
Laboratory of Chemistry, School of Medicine, Keio University, 4-1-1 Hiyoshi, Kohoku-ku, Yokohama 223-8521, Japan. mitsuhir@hc.cc.keio.ac.jp
Watanabe
Yumi
Y
Umezawa
Kazuo
K
D000363:Agaricales / Q000201:enzymology; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry; D006898:Hydroxylamines / Q000138:chemical synthesis* / Q000737:chemistry; D014442:Monophenol Monooxygenase / Q000037:antagonists & inhibitors*; D009603:Nitroso Compounds / Q000138:chemical synthesis* / Q000737:chemistry; D013329:Structure-Activity Relationship
D004791:Enzyme Inhibitors; D006898:Hydroxylamines; D009603:Nitroso Compounds; D014442:Monophenol Monooxygenase