Enzymes
| UniProtKB help_outline | 2,195 proteins |
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Namehelp_outline
3-O-[β-D-GlcA-(1→3)-β-D-Xyl-(1→4)-Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-(O-6-P-α-D-Man)]-Thr-[protein]
Identifier
RHEA-COMP:17482
Reactive part
help_outline
- Name help_outline 3-O-[β-D-GlcA-(1→3)-β-D-Xyl-(1→4)-Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man]-L-threonine residue Identifier CHEBI:177336 Charge -5 Formula C47H77N3O44P3 SMILEShelp_outline O([C@@H]1[C@H]([C@H]([C@@H]([C@H](O1)COP([O-])([O-])=O)O[C@H]2[C@@H]([C@H]([C@@H]([C@H](O2)CO)O)O[C@H]3[C@@H]([C@H]([C@H]([C@H](O3)CO)O)OP(OC[C@H]([C@H]([C@H](COP(OC[C@H]([C@H]([C@H](CO)O)O)O[C@H]4[C@@H]([C@H]([C@@H](CO4)O[C@H]5[C@@H]([C@H]([C@@H]([C@H](O5)C([O-])=O)O)O)O)O)O)([O-])=O)O)O)O)([O-])=O)NC(C)=O)NC(C)=O)O)O)[C@@H]([C@@H](C(*)=O)N*)C 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP-α-D-xylose Identifier CHEBI:57632 Charge -2 Formula C14H20N2O16P2 InChIKeyhelp_outline DQQDLYVHOTZLOR-OCIMBMBZSA-L SMILEShelp_outline O[C@@H]1CO[C@H](OP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2ccc(=O)[nH]c2=O)[C@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
3-O-[α-D-Xyl-(1→3)-β-D-GlcA-(1→4)-β-D-Xyl-(1→4)-Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-(O-6-P-α-D-Man)]-Thr-[protein]
Identifier
RHEA-COMP:17483
Reactive part
help_outline
- Name help_outline 3-O-[α-D-Xyl-(1→3)-β-D-GlcA-(1→4)-β-D-Xyl-(1→4)-Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man]-L-threonine residue Identifier CHEBI:177352 Charge -5 Formula C52H85N3O48P3 SMILEShelp_outline O([C@@H]1[C@H]([C@H]([C@@H]([C@H](O1)COP([O-])([O-])=O)O[C@H]2[C@@H]([C@H]([C@@H]([C@H](O2)CO)O)O[C@H]3[C@@H]([C@H]([C@H]([C@H](O3)CO)O)OP(OC[C@H]([C@H]([C@H](COP(OC[C@H]([C@H]([C@H](CO)O)O)O[C@H]4[C@@H]([C@H]([C@@H](CO4)O[C@H]5[C@@H]([C@H]([C@@H]([C@H](O5)C([O-])=O)O)O[C@@H]6[C@@H]([C@H]([C@@H](CO6)O)O)O)O)O)O)([O-])=O)O)O)O)([O-])=O)NC(C)=O)NC(C)=O)O)O)[C@@H]([C@@H](C(*)=O)N*)C 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP Identifier CHEBI:58223 Charge -3 Formula C9H11N2O12P2 InChIKeyhelp_outline XCCTYIAWTASOJW-XVFCMESISA-K SMILEShelp_outline O[C@@H]1[C@@H](COP([O-])(=O)OP([O-])([O-])=O)O[C@H]([C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 611 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,717 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:57336 | RHEA:57337 | RHEA:57338 | RHEA:57339 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| MetaCyc help_outline |
Publications
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Xylosyl- and glucuronyltransferase functions of LARGE in alpha-dystroglycan modification are conserved in LARGE2.
Inamori K., Hara Y., Willer T., Anderson M.E., Zhu Z., Yoshida-Moriguchi T., Campbell K.P.
LARGE-dependent modification enables α-dystroglycan (α-DG) to bind to its extracellular matrix ligands. Mutations in the LARGE gene and several others involved in O-mannosyl glycan synthesis have been identified in congenital and limb-girdle muscular dystrophies that are characterized by perturbed ... >> More
LARGE-dependent modification enables α-dystroglycan (α-DG) to bind to its extracellular matrix ligands. Mutations in the LARGE gene and several others involved in O-mannosyl glycan synthesis have been identified in congenital and limb-girdle muscular dystrophies that are characterized by perturbed glycosylation and reduced ligand-binding affinity of α-DG. LARGE is a bifunctional glycosyltransferase that alternately transfers xylose and glucuronic acid, thereby generating the heteropolysaccharides on α-DG that confer its ligand binding. Although the LARGE paralog LARGE2 (also referred to as GYLTL1B) has likewise been shown to enhance the functional modification of α-DG in cultured cells, its enzymatic activities have not been identified. Here, we report that LARGE2 is also a bifunctional glycosyltransferase and compare its properties with those of LARGE. By means of a high-performance liquid chromatography-based enzymatic assay, we demonstrate that like LARGE, LARGE2 has xylosyltransferase (Xyl-T) and glucuronyltransferase (GlcA-T) activities, as well as polymerizing activity. Notably, however, the pH optima of the Xyl-T and GlcA-T of LARGE2 are distinct from one another and also from those of LARGE. Our results suggest that LARGE and LARGE2 catalyze the same glycosylation reactions for the functional modification of α-DG, but that they have different biochemical properties. << Less
Glycobiology 23:295-302(2013) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Dystroglycan function requires xylosyl- and glucuronyltransferase activities of LARGE.
Inamori K., Yoshida-Moriguchi T., Hara Y., Anderson M.E., Yu L., Campbell K.P.
Posttranslational modification of alpha-dystroglycan (α-DG) by the like-acetylglucosaminyltransferase (LARGE) is required for it to function as an extracellular matrix (ECM) receptor. Mutations in the LARGE gene have been identified in congenital muscular dystrophy patients with brain abnormalitie ... >> More
Posttranslational modification of alpha-dystroglycan (α-DG) by the like-acetylglucosaminyltransferase (LARGE) is required for it to function as an extracellular matrix (ECM) receptor. Mutations in the LARGE gene have been identified in congenital muscular dystrophy patients with brain abnormalities. However, the precise function of LARGE remains unclear. Here we found that LARGE could act as a bifunctional glycosyltransferase, with both xylosyltransferase and glucuronyltransferase activities, which produced repeating units of [-3-xylose-α1,3-glucuronic acid-β1-]. This modification allowed α-DG to bind laminin-G domain-containing ECM ligands. << Less
Science 335:93-96(2012) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.