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Name ^help_outline α-D-Man-(1→6)-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol Identifier CHEBI:229641 Charge -2 Formula (C5H8)n.C48H82N2O27P2 Search links Involved in 2 reaction(s) Find proteins in UniProtKB for this molecule Form(s) in this reaction:
- Identifier: RHEA-COMP:19514
  
  Polymer name: an α-D-Man-(1→6)-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol
  
  Polymerization index ^help_outline n-1
  
  Formula C48H82N2O27P2(C5H8)_n-1
  
  Charge (-2)(0)_n-1
  Mol File for the polymer
Name ^help_outline GDP-α-D-mannose Identifier CHEBI:57527 (Beilstein: 6630718) ^help_outline Charge -2 Formula C16H23N5O16P2 InChIKey^help_outline MVMSCBBUIHUTGJ-GDJBGNAASA-L SMILES^help_outline Nc1nc2n(cnc2c(=O)[nH]1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)O[C@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]2O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 54 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol Identifier CHEBI:132511 Charge -2 Formula (C5H8)n.C54H92N2O32P2 Search links Involved in 3 reaction(s) Find proteins in UniProtKB for this molecule Form(s) in this reaction:
- Identifier: RHEA-COMP:19515
  
  Polymer name: an α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol
  
  Polymerization index ^help_outline n-1
  
  Formula C54H92N2O32P2(C5H8)_n-1
  
  Charge (-2)(0)_n-1
  Mol File for the polymer
Name ^help_outline GDP Identifier CHEBI:58189 Charge -3 Formula C10H12N5O11P2 InChIKey^help_outline QGWNDRXFNXRZMB-UUOKFMHZSA-K SMILES^help_outline Nc1nc2n(cnc2c(=O)[nH]1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 186 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 InChIKey^help_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILES^help_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:79027	RHEA:79028	RHEA:79029	RHEA:79030
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	578 proteins	578 proteins

Publications

Topological and enzymatic analysis of human Alg2 mannosyltransferase reveals its role in lipid-linked oligosaccharide biosynthetic pathway.

Xiang M.H., Xu X.X., Wang C.D., Chen S., Xu S., Xu X.Y., Dean N., Wang N., Gao X.D.

N-glycosylation starts with the biosynthesis of lipid-linked oligosaccharide (LLO) on the endoplasmic reticulum (ER). Alg2 mannosyltransferase adds both the α1,3- and α1,6-mannose (Man) onto ManGlcNAc2-pyrophosphate-dolichol (M1Gn2-PDol) in either order to generate ... >> More

N-glycosylation starts with the biosynthesis of lipid-linked oligosaccharide (LLO) on the endoplasmic reticulum (ER). Alg2 mannosyltransferase adds both the α1,3- and α1,6-mannose (Man) onto ManGlcNAc2-pyrophosphate-dolichol (M1Gn2-PDol) in either order to generate the branched M3Gn2-PDol product. The well-studied yeast Alg2 interacts with ER membrane through four hydrophobic domains. Unexpectedly, we show that Alg2 structure has diverged between yeast and humans. Human Alg2 (hAlg2) associates with the ER via a single membrane-binding domain and is markedly more stable in vitro. These properties were exploited to develop a liquid chromatography-mass spectrometry quantitative kinetics assay for studying purified hAlg2. Under physiological conditions, hAlg2 prefers to transfer α1,3-Man onto M1Gn2 before adding the α1,6-Man. However, this bias is altered by an excess of GDP-Man donor or an increased level of M1Gn2 substrate, both of which trigger production of the M2Gn2(α-1,6)-PDol. These results suggest that Alg2 may regulate the LLO biosynthetic pathway by controlling accumulation of M2Gn2 (α-1,6) intermediate. << Less

Commun. Biol. 5:117-117(2022) [PubMed] [EuropePMC]

This publication is cited by 3 other entries.

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Cross-references

Publications

Topological and enzymatic analysis of human Alg2 mannosyltransferase reveals its role in lipid-linked oligosaccharide biosynthetic pathway.