Inhibition of glycosidases by aldonolactones of corresponding configuration. The specificity of alpha-L-arabinosidase.
1. The previous study (Conchie, Gelman & Levvy, 1967b) of the specificity of beta-glucosidase, beta-galactosidase and beta-d-fucosidase in barley, limpet, almond emulsin and rat epididymis was extended to alpha-l-arabinosidase. 2. The inhibitory action of l-arabinono-(1-->5)-lactone was tested against all four types of enzyme, and alpha-l-arabinosidase was examined for inhibition by glucono-, galactono- and d-fucono-lactone. 3. In emulsin, the enzyme that hydrolyses beta-glucosides, beta-galactosides and beta-d-fucosides also hydrolyses alpha-l-arabinosides. Rat epididymis resembles emulsin except that, as already noted, it lacks beta-glucosidase activity. 4. In the limpet, alpha-l-arabinosidase activity is associated with the enzyme that hydrolyses beta-glucosides and beta-d-fucosides, and not with the separate beta-galactosidase. 5. The effects of the different lactones on the barley preparation suggest that alpha-l-arabinosidase activity is associated with the beta-galactosidase rather than with the enzyme that hydrolyses beta-glucosides and beta-d-fucosides. Fractionation and heat-inactivation experiments indicate that there is also a separate alpha-l-arabinosidase in the preparation.
D000447:Aldehydes; D000818:Animals; D001089:Arabinose; D002523:Edible Grain / Q000201:enzymology; D004822:Epididymis / Q000201:enzymology; D005643:Fucose; D005690:Galactose; D005696:Galactosidases / Q000037:antagonists & inhibitors; D005947:Glucose; D005959:Glucosidases / Q000037:antagonists & inhibitors; D006026:Glycoside Hydrolases / Q000032:analysis / Q000037:antagonists & inhibitors*; D007700:Kinetics; D007783:Lactones; D008297:Male; D008974:Mollusca / Q000201:enzymology; D009754:Nuts; D051381:Rats
D000447:Aldehydes; D007783:Lactones; D005643:Fucose; D001089:Arabinose; D005696:Galactosidases; D005959:Glucosidases; D006026:Glycoside Hydrolases; D005947:Glucose; D005690:Galactose