Document Detail


LARGE2 generates the same xylose and glucuronic acid containing glycan structures as LARGE.
MedLine Citation:
PMID:  23135544     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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 cellular level the enzyme can substitute LARGE in glycosylating dystroglycan. Here we show that LARGE2 catalyzes the same glycosylation reaction as LARGE. It is a bifunctional glycosyltransferase using UDP-xylose and UDP-glucuronic acid as donor sugars to produce a xyloglucuronan with alternating xylose and glucuronic acid residues.
Authors:
Angel Ashikov; Falk F R Buettner; Birgit Tiemann; Rita Gerardy-Schahn; Hans Bakker
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-11-7
Journal Detail:
Title:  Glycobiology     Volume:  -     ISSN:  1460-2423     ISO Abbreviation:  Glycobiology     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-8     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9104124     Medline TA:  Glycobiology     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Department of Cellular Chemistry, Hannover Medical School, Carl-Neuberg-Strasse 1, D-30625 Hannover, Germany.
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