A solubilized enzyme preparation from mung bean seedlings catalyzed the transfer of GlcNAc from UDP-GlcNAc to the Man5GlcNAc acceptor to form GlcNAc-Man5GlcNAc. In the presence of the mannosidase inhibitor, swainsonine, this oligosaccharide accumulated, but in the absence of this inhibitor, the oligosaccharide was processed further to smaller sized oligosaccharides with the release of radioactive mannose. The formation of GlcNAc-Man5GlcNAc required the presence of Man5GlcNAc, UDP-GlcNAc, Mn++ and swainsonine. The product, GlcNAc-Man5GlcNAc was characterized by chromatography on calibrated columns of Biogel P-4, and by various enzymatic digestions. These data indicate the presence of GlcNAc transferase I and mannosidase II in plants.
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