Studies on Enzymes Acting on Glycopeptides*

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Abstract
1. An enzyme, tentatively named glycopeptidase, was found in blood serum and tissues. This enzyme degraded synthetic β-aspartylglycosylamine and an ovalbumin glycopeptide to yield aspartic acid, ammonia and N-acetylglucosamine (or an oligosaccharide with N-acetyl-glucosamine at the reducing terminal). 2. Glycopeptidase was found to hydrolyze the amide bond of β-aspartylglycosylamine producing glycosylamine, while the glycosylamine was subsequently hydrolyzed non-enzymatically. 3. Glycopeptidase appeared to require for its action both α-amino and α-carboxyl groups of aspartic acid linked to carbohydrate. 4. A glycosylamine, 1-amino-N-acetylglucosamine, was synthesized and fully characterized in the identification of the product of glycopeptidase action on synthetic β-aspartylglycosylamine.