ENZYMATIC-SYNTHESIS OF THE N-GLYCOSIDIC BOND BY BETA-ASPARTYLATION OFGLYCOSYLAMINES

Citation
I. Mononen et al., ENZYMATIC-SYNTHESIS OF THE N-GLYCOSIDIC BOND BY BETA-ASPARTYLATION OFGLYCOSYLAMINES, Biochemical and biophysical research communications, 218(2), 1996, pp. 510-513
Citations number
11
Categorie Soggetti
Biology,Biophysics
ISSN journal
0006291X
Volume
218
Issue
2
Year of publication
1996
Pages
510 - 513
Database
ISI
SICI code
0006-291X(1996)218:2<510:EOTNBB>2.0.ZU;2-6
Abstract
Glycosylasparaginase (EC 3.5.1.26) is an amidase, which cleaves the N- glycosidic linkage during glycoprotein degradation leading to the libe ration of L-aspartic acid from various glycoasparagines. In this work we demonstrate that glycosylasparaginase is also capable of catalyzing the synthesis of the N-glycosidic bond by N-beta-aspartylation of bet a-glycosylamine using 1-amino-N-acetylglucosamine as the nucleophile a nd L-aspartic acid beta-methyl ester as the beta-aspartyl donor. Kinet ic studies indicated that beta-glycosylamine has 1390-fold higher reac tivity than water in the de-beta-aspartylation of the beta-aspartylenz pme, indicative of the presence of a beta-glycosylamine binding sub-si te at the substrate binding site of glycosylasparaginase. The reaction can be applied to glycosylasparaginase-catalyzed biosynthesis of nove l glycoasparagines. (C) 1996 Academic Press, Inc.