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Literature summary 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 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.B80 expression in HEK-293 cell Homo sapiens
2.4.2.B18 expression in HEK-293 cell Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.B80 D242N/D244N glucuronyltransferase activity is comparable to that in wild type, whereas xylosyltransferase activity is undetectable Homo sapiens
2.4.1.B80 D563N/D565N glucuronyltransferase activity is comparable to that in wild type, whereas xylosyltransferase activity is undetectable Homo sapiens
2.4.2.B18 D242N/D244N glucuronyltransferase activity is comparable to that in wild type, whereas xylosyltransferase activity is undetectable Homo sapiens
2.4.2.B18 D563N/D565N glucuronyltransferase activity is comparable to that in wild type, whereas xylosyltransferase activity is undetectable Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.B80 Homo sapiens O95461 bifunctional glycosyltransferase, with both xylosyltransferase and glucuronyltransferase activities
-
2.4.2.B18 Homo sapiens O95461 bifunctional glycosyltransferase, with both xylosyltransferase and glucuronyltransferase activities
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.B80 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
-
 ?
2.4.1.B80 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
-
 ?
2.4.2.B18 additional information 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-] Homo sapiens ?
-
-
2.4.2.B18 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
-
 ?
2.4.2.B18 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
-
 ?
2.4.2.B18 UDP-alpha-D-xylose + beta-D-glucuronosyl-[O-mannosyl-chain of alpha-dystroglycan]
-
 Homo sapiens UDP + alpha-D-xylosyl-(1->3)-beta-D-glucuronosyl-(1->3)-[O-mannosyl-chain of alpha-dystroglycan]
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.B80 LARGE1
-
 Homo sapiens
2.4.1.B80 like-acetylglucosaminyltransferase
-
 Homo sapiens
2.4.2.B18 LARGE1
-
 Homo sapiens
2.4.2.B18 like-acetylglucosaminyltransferase
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
2.4.1.B80 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
2.4.2.B18 physiological function enzyme acts as a bifunctional glycosyltransferase, with both xylosyltransferase and glucuronyltransferase activities, producing repeating units of [3-xylose-alpha-(1->3)-glucuronic acid-beta-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