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Figure 1.
Figure 1. Hydrolysis reaction catalyzed by GA amidase. GA
cleaves the β-N-aspartylglucosylamine bond (indicated by the
bold arrow) of its natural substrate NAcGlc-Asn during
proteolytic processings of asparagine-linked glycoproteins,
resulting in the release of apartic acid and aminoglycan. The
latter product is then further hydrolyzed non-enzymatically to
release ammonia and oligosaccharide. Figure 1. Hydrolysis
reaction catalyzed by GA amidase. GA cleaves the
β-N-aspartylglucosylamine bond (indicated by the bold arrow) of
its natural substrate NAcGlc-Asn during proteolytic processings
of asparagine-linked glycoproteins, resulting in the release of
apartic acid and aminoglycan. The latter product is then further
hydrolyzed non-enzymatically to release ammonia and
oligosaccharide.
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