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Glycobiology. 2013 Mar;23(3):303-9. doi: 10.1093/glycob/cws153. Epub 2012 Nov 7.

LARGE2 generates the same xylose- and glucuronic acid-containing glycan structures as LARGE.

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1
Department of Cellular Chemistry, Hannover Medical School, Carl-Neuberg-Strasse 1, D-30625 Hannover, Germany.

Abstract

LARGE (like-glycosyltransferase) and LARGE2 (glycosyltransferase-like 1B (GYLTL1B)) are homologous Golgi glycosyltransferases possessing two catalytic domains with homology to members of glycosyltransferase families GT8 and GT49. Mutations in human and mouse Large result in muscular dystrophy due to underglycosylation of dystroglycan. The systemic function of LARGE2 is unknown, but at a cellular level the enzyme can substitute for LARGE in glycosylating dystroglycan. Here, we show that LARGE2 catalyzes the same glycosylation reaction as LARGE. It is a bifunctional glycosyltransferase using uridine diphosphate (UDP)-xylose (Xyl) and UDP-glucuronic acid (GlcA) as donor sugars to produce a xyloglucuronan with alternating Xyl and GlcA residues.

PMID:
23135544
DOI:
10.1093/glycob/cws153
[Indexed for MEDLINE]
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