Literature summary for 2.4.1.B80 extracted from

Inamori, K.; Yoshida-Moriguchi,T.; Hara, Y.; Anderson, M.E.; Yu, L.; Campbell, K.P.
Dystroglycan function requires xylosyl- and glucuronyltransferase activities of LARGE (2012), Science, 335, 93-96 .

Search for more literature for 2.4.1.B80

Cloned(Commentary)

Cloned (Comment)	Organism
expression in HEK-293 cell	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
D242N/D244N	glucuronyltransferase activity is comparable to that in wild type, whereas xylosyltransferase activity is undetectable	Homo sapiens
D563N/D565N	glucuronyltransferase activity is comparable to that in wild type, whereas xylosyltransferase activity is undetectable	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O95461	bifunctional glycosyltransferase, with both xylosyltransferase and glucuronyltransferase activities	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-alpha-D-glucuronate + 4-nitrophenyl alpha-D-xyloside	glucuronosyltransferase activity of the bifunctional enzyme	Homo sapiens	UDP + 4-nitrophenyl beta-D-glucuronyl-(1->3)-alpha-D-xyloside	-	?
UDP-alpha-D-xylose + 4-methylumbelliferyl beta-D-glucuronate	xylosyltransferase activity of the bifunctional enzyme	Homo sapiens	UDP + 4-methylumbelliferyl alpha-D-xylosyl-(1->3)-beta-D-glucuronate	-	?

Synonyms

Synonyms	Comment	Organism
LARGE1	-	Homo sapiens
like-acetylglucosaminyltransferase	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	enzyme acts as a bifunctional glycosyltransferase, with both xylosyltransferase and glucuronyltransferase activities, producing repeating units of [3-alpha-D-xylosyl-(1->3)-beta-D-glucuronyl-1-]. LARGE synthesizes the polymer on the O-mannosyl glycan of alpha-dystroglycan in vivo. The LARGE-synthesized, negatively charged glycan on alpha-dystroglycan likely binds to laminin through electrostatic associations with these basic patches	Homo sapiens

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Release 2023.1 (January 2023)