Studies on relationships between the structure and the glycosidase-inhibiting activity of HPAAO and its analogs.
p-Hydroxyphenylacetaldoxime (HPAAO) (anti and syn forms) obtained by fermentation and its analogs chemically synthesized were tested for their activities to inhibit various glycosidases. HPAAO inhibited bovine liver beta-galactosidase in a competitive manner at pH 7.0 with an apparent Ki value of 8 x 10(-8) M. HPAAO also inhibited various mammalian beta-glycosidases which had pH optima between 6.0 and 8.0. The syn form of HPAAO was found to be more active than the anti form against bovine liver neutral beta-galactosidase. It was concluded that the oxime moiety of HPAAO and its analogs was essential for their enzyme-inhibiting activity and the activities of aromatic or aliphatic oxime derivatives were dependent on the number of carbon atoms in their alkyl-chains.
D000118:Acetylglucosaminidase / Q000037:antagonists & inhibitors; D000818:Animals; D002417:Cattle; D005260:Female; D005696:Galactosidases / Q000037:antagonists & inhibitors; D005966:Glucuronidase / Q000037:antagonists & inhibitors; D006026:Glycoside Hydrolases / Q000037:antagonists & inhibitors*; D006801:Humans; D007700:Kinetics; D010091:Oximes / Q000494:pharmacology*; D011247:Pregnancy; D051381:Rats; D013329:Structure-Activity Relationship; D013552:Swine
D010091:Oximes; D005696:Galactosidases; D006026:Glycoside Hydrolases; D005966:Glucuronidase; D000118:Acetylglucosaminidase