Rhea - reaction knowledgebase

Enzymes

UniProtKB ^help_outline	8 proteins
Enzyme class ^help_outline	EC 3.2.1.207 mannosyl-oligosaccharide alpha-1,3-glucosidase

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Name ^help_outline H₂O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) ^help_outline Charge 0 Formula H2O InChIKey^help_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILES^help_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name^help_outline N⁴-(α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-asparaginyl-[protein] Identifier RHEA-COMP:14355 Reactive part ^help_outline
- Name ^help_outline N⁴-(α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-Asn residue Identifier CHEBI:59082 Charge 0 Formula C86H142N4O67 SMILES^help_outline [C@@H]1([C@H]([C@H]([C@@H]([C@H](O1)CO[C@@H]2[C@H]([C@H]([C@@H]([C@H](O2)CO[C@@H]3[C@H]([C@H]([C@@H]([C@H](O3)CO)O)O)O[C@@H]4[C@H]([C@H]([C@@H]([C@H](O4)CO)O)O)O)O)O[C@@H]5[C@H]([C@H]([C@@H]([C@H](O5)CO)O)O)O[C@@H]6[C@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O)O)O)O[C@@H]7[C@H]([C@H]([C@@H]([C@H](O7)CO)O)O)O[C@@H]8[C@H]([C@H]([C@@H]([C@H](O8)CO)O)O)O[C@@H]9[C@H]([C@H]([C@@H]([C@H](O9)CO)O)O[C@@H]%10[C@@H]([C@H]([C@@H]([C@H](O%10)CO)O)O[C@@H]%11[C@@H]([C@H]([C@@H]([C@H](O%11)CO)O)O)O)O)O)O)O[C@H]%12[C@@H]([C@H]([C@@H](O[C@@H]%12CO)O[C@H]%13[C@@H]([C@H]([C@@H](O[C@@H]%13CO)NC(C[C@@H](C(=O)*)N*)=O)NC(=O)C)O)NC(=O)C)O 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
Search links Involved in 2 reaction(s) Find proteins in UniProtKB for this molecule
Name ^help_outline β-D-glucose Identifier CHEBI:15903 (Beilstein: 1281607; CAS: 492-61-5) ^help_outline Charge 0 Formula C6H12O6 InChIKey^help_outline WQZGKKKJIJFFOK-VFUOTHLCSA-N SMILES^help_outline OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 39 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name^help_outline N⁴-(α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-asparaginyl-[protein] Identifier RHEA-COMP:14357 Reactive part ^help_outline
- Name ^help_outline N⁴-(α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-Asn residue Identifier CHEBI:59080 Charge 0 Formula C80H132N4O62 SMILES^help_outline [C@@H]1([C@H]([C@H]([C@@H]([C@H](O1)CO[C@@H]2[C@H]([C@H]([C@@H]([C@H](O2)CO[C@@H]3[C@H]([C@H]([C@@H]([C@H](O3)CO)O)O)O[C@@H]4[C@H]([C@H]([C@@H]([C@H](O4)CO)O)O)O)O)O[C@@H]5[C@H]([C@H]([C@@H]([C@H](O5)CO)O)O)O[C@@H]6[C@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O)O)O)O[C@@H]7[C@H]([C@H]([C@@H]([C@H](O7)CO)O)O)O[C@@H]8[C@H]([C@H]([C@@H]([C@H](O8)CO)O)O)O[C@@H]9[C@H]([C@H]([C@@H]([C@H](O9)CO)O)O[C@@H]%10[C@@H]([C@H]([C@@H]([C@H](O%10)CO)O)O)O)O)O)O[C@H]%11[C@@H]([C@H]([C@@H](O[C@@H]%11CO)O[C@H]%12[C@@H]([C@H]([C@@H](O[C@@H]%12CO)NC(C[C@@H](C(=O)*)N*)=O)NC(=O)C)O)NC(=O)C)O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Search links Involved in 3 reaction(s) Find proteins in UniProtKB for this molecule

Cross-references

	RHEA:55996	RHEA:55997	RHEA:55998	RHEA:55999
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	8 proteins
EC numbers ^help_outline	3.2.1.207
KEGG ^help_outline				R05980
MetaCyc ^help_outline		RXN-18907

Publications

Two isoforms of trimming glucosidase II exist in mammalian tissues and cell lines but not in yeast and insect cells.

Ziak M., Meier M., Etter K.S., Roth J.

We previously cloned glucosidase II and provided in vivo evidence for its involvement in protein folding quality control. DNA-sequencing of different clones demonstrated the existence of two isoforms of glucosidase II which differed by 66 nucleotides due to alternative splicing. The existence of t ... >> More

We previously cloned glucosidase II and provided in vivo evidence for its involvement in protein folding quality control. DNA-sequencing of different clones demonstrated the existence of two isoforms of glucosidase II which differed by 66 nucleotides due to alternative splicing. The existence of two enzyme isoforms in various organs of pig and rat as well as human, bovine, rat, and mouse cell lines could be demonstrated by RT-PCR and Western blotting. Furthermore, the two isoforms of glucosidase II could be detected in embryonic and postnatal rat kidney and liver. In yeast, Saccharomyces cerevisiae, and in insects, Drosophila S2 cells, only one isoforms of the enzyme was detectable. The ubiquitous occurrence of the two glucosidase II isoforms in mammalian tissues and cell lines might be indicative of a special function of each isoform. << Less

Biochem Biophys Res Commun 280:363-367(2001) [PubMed] [EuropePMC]

This publication is cited by 1 other entry.
Endoplasmic reticulum alpha-glycosidases of Candida albicans are required for N glycosylation, cell wall integrity, and normal host-fungus interaction.

Mora-Montes H.M., Bates S., Netea M.G., Diaz-Jimenez D.F., Lopez-Romero E., Zinker S., Ponce-Noyola P., Kullberg B.J., Brown A.J., Odds F.C., Flores-Carreon A., Gow N.A.

The cell surface of Candida albicans is enriched in highly glycosylated mannoproteins that are involved in the interaction with the host tissues. N glycosylation is a posttranslational modification that is initiated in the endoplasmic reticulum (ER), where the Glc(3)Man(9)GlcNAc(2) N-glycan is pro ... >> More

The cell surface of Candida albicans is enriched in highly glycosylated mannoproteins that are involved in the interaction with the host tissues. N glycosylation is a posttranslational modification that is initiated in the endoplasmic reticulum (ER), where the Glc(3)Man(9)GlcNAc(2) N-glycan is processed by alpha-glucosidases I and II and alpha1,2-mannosidase to generate Man(8)GlcNAc(2). This N-oligosaccharide is then elaborated in the Golgi to form N-glycans with highly branched outer chains rich in mannose. In Saccharomyces cerevisiae, CWH41, ROT2, and MNS1 encode for alpha-glucosidase I, alpha-glucosidase II catalytic subunit, and alpha1,2-mannosidase, respectively. We disrupted the C. albicans CWH41, ROT2, and MNS1 homologs to determine the importance of N-oligosaccharide processing on the N-glycan outer-chain elongation and the host-fungus interaction. Yeast cells of Cacwh41Delta, Carot2Delta, and Camns1Delta null mutants tended to aggregate, displayed reduced growth rates, had a lower content of cell wall phosphomannan and other changes in cell wall composition, underglycosylated beta-N-acetylhexosaminidase, and had a constitutively activated PKC-Mkc1 cell wall integrity pathway. They were also attenuated in virulence in a murine model of systemic infection and stimulated an altered pro- and anti-inflammatory cytokine profile from human monocytes. Therefore, N-oligosaccharide processing by ER glycosidases is required for cell wall integrity and for host-fungus interactions. << Less

Eukaryot Cell 6:2184-2193(2007) [PubMed] [EuropePMC]

This publication is cited by 1 other entry.
Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum.

Wilkinson B.M., Purswani J., Stirling C.J.

Glucosidase II is essential for sequential removal of two glucose residues from N-linked glycans during glycoprotein biogenesis in the endoplasmic reticulum. The enzyme is a heterodimer whose alpha-subunit contains the glycosyl hydrolase active site. The function of the beta-subunit has yet to be ... >> More

Glucosidase II is essential for sequential removal of two glucose residues from N-linked glycans during glycoprotein biogenesis in the endoplasmic reticulum. The enzyme is a heterodimer whose alpha-subunit contains the glycosyl hydrolase active site. The function of the beta-subunit has yet to be defined, but mutations in the human gene have been linked to an autosomal dominant form of polycystic liver disease. Here we report the identification and characterization of a Saccharomyces cerevisiae gene, GTB1, encoding a polypeptide with 21% sequence similarity to the beta-subunit of human glucosidase II. The Gtb1 protein was shown to be a soluble glycoprotein (96-102 kDa) localized to the endoplasmic reticulum lumen where it was present in a complex together with the yeast alpha-subunit homologue Gls2p. Surprisingly, we found that Deltagtb1 mutant cells were specifically defective in the processing of monoglucosylated glycans. Thus, although Gls2p is sufficient for cleavage of the penultimate glucose residue, Gtb1p is essential for cleavage of the final glucose. Our data demonstrate that Gtb1p is required for normal glycoprotein biogenesis and reveal that the final two glucose-trimming steps in N-glycan processing are mechanistically distinct. << Less

J. Biol. Chem. 281:6325-6333(2006) [PubMed] [EuropePMC]

This publication is cited by 1 other entry.
Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit.

Trombetta E.S., Simons J.F., Helenius A.

Trimming of glucoses from N-linked core glycans on newly synthesized glycoproteins occurs sequentially through the action of glucosidases I and II in the endoplasmic reticulum (ER). We isolated enzymatically active glucosidase II from rat liver and found that, in contrast with previous reports, it ... >> More

Trimming of glucoses from N-linked core glycans on newly synthesized glycoproteins occurs sequentially through the action of glucosidases I and II in the endoplasmic reticulum (ER). We isolated enzymatically active glucosidase II from rat liver and found that, in contrast with previous reports, it contains two subunits (alpha and beta). Sequence analysis of peptides derived from them allowed us to identify their corresponding human cDNA sequences. The sequence of the alpha subunit predicted a soluble protein (104 kDa) devoid of known signals for residence in the ER. It showed homology with several other glucosidases but not with glucosidase I. Among the homologues, we identified a Saccharomyces cerevisiae gene, which we showed by gene disruption experiments to be the functional catalytic subunit of glucosidase II. The disrupted yeast strains had no detectable growth defect. The sequence of the beta subunit (58 kDa) showed no sequence homology with other known proteins. It encoded a soluble protein rich in glutamic and aspartic acid with a putative ER retention signal (HDEL) at the C terminus. This suggested that the beta subunit is responsible for the ER localization of the enzyme. << Less

J. Biol. Chem. 271:27509-27516(1996) [PubMed] [EuropePMC]

This publication is cited by 1 other entry.

Enzymes

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Cross-references

Publications

Two isoforms of trimming glucosidase II exist in mammalian tissues and cell lines but not in yeast and insect cells.

Endoplasmic reticulum alpha-glycosidases of Candida albicans are required for N glycosylation, cell wall integrity, and normal host-fungus interaction.

Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum.

Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit.