Almond glycopeptidase acting on aspartylglycosylamine linkages. Multiplicity and substrate specificity.
The glycopeptidase preparation that has been isolated from almond emulsin and acts on beta-aspartylglycosylamine linkages in glycopeptides was separated into three active fractions by DEAE-cellulose column chromatography. The three discrete species of glycopeptidase (Groups A, B and C) have been purified 30-, 136-, and 99-fold, respectively. The optimum pH value of Group A was 6.0 and those of Groups B and C, 5.0. Isoelectric points of Groups A, B and C were pH 7.7, 8.6 and 8.7, respectively. All three glycopeptidases hydrolyzed quantitatively glycopeptides with 3-11 amino acid residues prepared from stem bromelain, ovalbumin and ovotransferrin. Group C preferred glycopeptides with shorter peptide chains, whereas Groups A and B preferred those with longer chains. Glycopeptidase Group A also hydrolyzed intact glycoproteins such as stem bromelain, ovalbumin, Taka-amylase A and desialylated human transferrin.
D000117:Acetylglucosamine / Q000031:analogs & derivatives; D000581:Amidohydrolases / Q000302:isolation & purification / Q000378:metabolism*; D001224:Aspartic Acid / Q000031:analogs & derivatives; D006020:Glycopeptides / Q000302:isolation & purification / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D010944:Plants / Q000201:enzymology*; D013379:Substrate Specificity
D006020:Glycopeptides; C000009:N-acetylglucosaminylasparagine; D001224:Aspartic Acid; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D000117:Acetylglucosamine