Enzymes
| UniProtKB help_outline | 578 proteins |
Reaction participants Show >> << Hide
-
Name help_outline
β-D-mannosyl-(1→4)-N,N'-diacetylchitobiosyldiphosphodolichol
Identifier
CHEBI:58472
Charge
-2
Formula
(C5H8)n.C42H72N2O22P2
Search links
Involved in 3 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
-
Identifier: RHEA-COMP:19511Polymer name: a β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphospho-di-trans,poly-cis-dolicholPolymerization index help_outline n-1Formula C42H72N2O22P2(C5H8)n-1Charge (-2)(0)n-1Mol File for the polymer
-
- Name help_outline GDP-α-D-mannose Identifier CHEBI:57527 (Beilstein: 6630718) help_outline Charge -2 Formula C16H23N5O16P2 InChIKeyhelp_outline MVMSCBBUIHUTGJ-GDJBGNAASA-L SMILEShelp_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→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:19514Polymer 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-dolicholPolymerization index help_outline n-1Formula C48H82N2O27P2(C5H8)n-1Charge (-2)(0)n-1Mol File for the polymer
-
- Name help_outline GDP Identifier CHEBI:58189 Charge -3 Formula C10H12N5O11P2 InChIKeyhelp_outline QGWNDRXFNXRZMB-UUOKFMHZSA-K SMILEShelp_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 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:79023 | RHEA:79024 | RHEA:79025 | RHEA:79026 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
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 ManGlcNAc<sub>2</sub>-pyrophosphate-dolichol (M<sub>1</sub>Gn<sub>2</sub>-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 ManGlcNAc<sub>2</sub>-pyrophosphate-dolichol (M<sub>1</sub>Gn<sub>2</sub>-PDol) in either order to generate the branched M<sub>3</sub>Gn<sub>2</sub>-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 M<sub>1</sub>Gn<sub>2</sub> before adding the α1,6-Man. However, this bias is altered by an excess of GDP-Man donor or an increased level of M<sub>1</sub>Gn<sub>2</sub> substrate, both of which trigger production of the M<sub>2</sub>Gn<sub>2</sub>(α-1,6)-PDol. These results suggest that Alg2 may regulate the LLO biosynthetic pathway by controlling accumulation of M<sub>2</sub>Gn<sub>2</sub> (α-1,6) intermediate. << Less
Commun. Biol. 5:117-117(2022) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.