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 |
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 |
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 | - |
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] | - |
? |
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 |
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 |