Enzymes
| UniProtKB help_outline | 2,272 proteins |
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Name help_outline
3-O-{[α-D-Xyl-(1→3)-β-D-GlcA-(1→3)]n-(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:177354
Charge
-5
Formula
C58H92N3O54P3
Search links
Involved in 2 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:17484Polymer name: 3-O-{(1→[3)-α-D-Xyl-(1→3)-β-D-GlcA-(1→](n)-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-Thr-[protein]Polymerization index help_outline nFormula C41H70N3O38P3(C11H15O10)nCharge (-4)(-1)nMol File for the polymer
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- Name help_outline UDP-α-D-glucuronate Identifier CHEBI:58052 Charge -3 Formula C15H19N2O18P2 InChIKeyhelp_outline HDYANYHVCAPMJV-LXQIFKJMSA-K SMILEShelp_outline O[C@@H]1[C@@H](COP([O-])(=O)OP([O-])(=O)O[C@H]2O[C@@H]([C@@H](O)[C@H](O)[C@H]2O)C([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 107 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
3-O-{β-D-GlcA-(1→3)-[α-D-Xyl-(1→3)-β-D-GlcA-(1→3)]n-(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:177355
Charge
-6
Formula
(C11H15O10)n.C47H77N3O44P3
Search links
Involved in 3 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:17486Polymer name: 3-O-{β-D-GlcA-(1→[3)-α-D-Xyl-(1→3)-β-D-GlcA-(1→](n)-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-Thr-[protein]Polymerization index help_outline nFormula C47H77N3O44P3(C11H15O10)nCharge (-5)(-1)nMol File for the polymer
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- 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 637 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 9,932 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:67924 | RHEA:67925 | RHEA:67926 | RHEA:67927 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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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.