Demonstration of a new glycopeptidase, from jack-bean meal, acting on aspartylglucosylamine linkages.
An enzyme preparation from jack-bean meal hydrolyzed beta-aspartylglucosylamine linkages in glycopeptides. The enzyme could release sialic acid-containing complex-type oligosaccharides as well as high-mannose-type and hybrid-type oligosaccharides. The products were equimolar amounts of ammonia, oligosaccharide and peptide. The enzyme cleaved glycopeptides with three or more amino acid residues, whereas it did not hydrolyze GlcNAc-Asn. The mechanism of action of the enzyme and substrate specificity so far tested were similar to those of the glycopeptidase from almonds.
D000117:Acetylglucosamine / Q000031:analogs & derivatives* / Q000378:metabolism; D000581:Amidohydrolases / Q000302:isolation & purification* / Q000502:physiology; D000641:Ammonia / Q000378:metabolism; D001216:Asparagine / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D007887:Fabaceae / Q000201:enzymology*; D005944:Glucosamine / Q000031:analogs & derivatives*; D006868:Hydrolysis; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D010946:Plants, Medicinal; D013329:Structure-Activity Relationship
C000009:N-acetylglucosaminylasparagine; D001216:Asparagine; D000641:Ammonia; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D005944:Glucosamine; D000117:Acetylglucosamine