Sustrate-specificity of glucomylase (E.C. 3.2.1.3) exemplified by p-nitroaniline n-glucosides.
The present paper supplements the previous investigations on the mechanism of reactions catalyzed by amylolytic enzymes. The performed experiments corroborated the data on transglucosylative properties of animal glucoamylases which were found to depend on the structure and concentration of substrate. The p-nitroanilines were first introduced in this type of research enabling to find the differences of activity mechanism of animal glucoamylases and Aspergillus niger glucoamylase. In complement to the data reported by Japanese students the transglucosylative properties of glucoamylases were shown to depend not only on the enzyme origin and substrate concentration but also on the chemical composition of applied substrate and concentration of hydrogen ions in the reaction medium.
D000814:Aniline Compounds / Q000378:metabolism; D000818:Animals; D001234:Aspergillus niger / Q000201:enzymology; D001665:Binding Sites; D002417:Cattle; D005947:Glucose / Q000378:metabolism; D005959:Glucosidases / Q000378:metabolism*; D005960:Glucosides / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008320:Maltose / Q000378:metabolism; D009574:Nitro Compounds / Q000378:metabolism; D013045:Species Specificity; D013154:Spleen / Q000201:enzymology; D013329:Structure-Activity Relationship
D000814:Aniline Compounds; D005960:Glucosides; D009574:Nitro Compounds; D008320:Maltose; D005959:Glucosidases; D005947:Glucose