[Inhibition of the activity of urinary N-acetyl-beta-D-glucosaminidase (NAG) and its isoenzymes by amikacin].
Our study indicates that amikacin (AK) inhibited urinary N-acetyl-beta-D-glucosaminidase (NAG) activity. In vivo and in vitro experiments showed significant increase of Michaelis constant of urinary NAG, in human and in rat, treated by amikacin. Our data indicate that the inhibition of amikacin on NAG and its isoenzymes was "apparently competitive" rather than competitive as reported by others. In the "apparently competitive" inhibition the amikacin-enzyme binding would be irreversible, including combined action of many hydrogen bonds which could have a strength like covalent bond.
Mozer
J L
JL
Laboratoire de Biochimie, Centre Hospitalier et Universitaire, Besançon, France.
Gibey
R
R
Henry
J C
JC
D000118:Acetylglucosaminidase / Q000037:antagonists & inhibitors / Q000652:urine*; D000583:Amikacin / Q000494:pharmacology*; D000818:Animals; D001667:Binding, Competitive; D006596:Hexosaminidases / Q000652:urine*; D006801:Humans; D007527:Isoenzymes / Q000037:antagonists & inhibitors*; D051381:Rats
D007527:Isoenzymes; D000583:Amikacin; D006596:Hexosaminidases; D000118:Acetylglucosaminidase
Inhibition de l'activité de la N-acétyl-beta-D-glucosaminidase (NAG) urinaire et de ses isoenzymes par l'amikacine.