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PMID: 2936346 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Demonstration of GlcNAc transferase I in plants.

Biochemical and biophysical research communications ·Vol. 134 ·No. 3 ·1986-02-13 ·Pages 1395-403

Szumilo T, Kaushal GP, Elbein AD

Abstract

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.

MeSH Terms
Alkaloids/pharmacology Enzyme Activation Fabaceae/enzymology Glucosyltransferases/metabolism N-Acetylglucosaminyltransferases Plants/enzymology Plants, Medicinal Solubility Swainsonine
Chemicals
Alkaloids Glucosyltransferases Man5-acetylglucosamine acetylglucosaminyltransferase N-Acetylglucosaminyltransferases Swainsonine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Szumilo T
Kaushal G P
Elbein A D
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1986-02-13
Pages
1395-403
Language
English
Region
United States
NLM ID
0372516
Subset
IM
Grants
NIADDK NIH HHS · AM-21800 · United States
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