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Literature summary for 3.2.1.207 extracted from

  • Hu, D.; Kamiya, Y.; Totani, K.; Kamiya, D.; Kawasaki, N.; Yamaguchi, D.; Matsuo, I.; Matsumoto, N.; Ito, Y.; Kato, K.; Yamamoto, K.
    Sugar-binding activity of the MRH domain in the ER alpha-glucosidase II beta subunit is important for efficient glucose trimming (2009), Glycobiology, 19, 1127-1135.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant beta-subunits and enzymes in HeLaS3 cells, overexpression in HEK 293T cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information a mutant enzyme with the mutant subunit IIbeta loses the sugar-binding activity of the GIIbeta-MRH domain, but hydrolyzes 4-nitrophenyl-alpha-glucopyranoside, although the capacity to remove glucose residues from G1M9 and G2M9 is significantly decreased, phenotype, overview Homo sapiens
Q420E site-directed mutagenesis of the mannose 6-phosphate receptor homology domain of the beta-subunit, GIIbeta-MRH, leading to reduced activity with substrates G1M9 and G2M9 Homo sapiens
Y410A site-directed mutagenesis of the mannose 6-phosphate receptor homology domain of the beta-subunit, GIIbeta-MRH, leading to reduced activity with substrates G1M9 and G2M9 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum membrane
-
Homo sapiens 5789
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Glc2Man9GlcNAc2 + H2O Homo sapiens i.e. G1M9 GlcMan9GlcNAc2 + D-glucopyranose
-
?
GlcMan9GlcNAc2 + H2O Homo sapiens G2M9 Man9GlcNAc2 + D-glucopyranose
-
?
additional information Homo sapiens glucosidase II is a glycan-processing enzyme that trims two alpha1,3-linked glucose residues from N-glycan on newly synthesized glycoproteins ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl alpha-D-glucopyranoside + H2O
-
Homo sapiens 4-nitrophenol + D-glucopyranose
-
?
Glc2Man9GlcNAc2 + H2O i.e. G1M9 Homo sapiens GlcMan9GlcNAc2 + D-glucopyranose
-
?
Glc2Man9GlcNAc2 + H2O i.e. G1M9, usage of synthetic methotrexate-coupled glycan substrate, G1M9-MTX Homo sapiens GlcMan9GlcNAc2 + D-glucopyranose
-
?
GlcMan9GlcNAc2 + H2O G2M9 Homo sapiens Man9GlcNAc2 + D-glucopyranose
-
?
GlcMan9GlcNAc2 + H2O G2M9, usage of synthetic methotrexate-coupled glycan substrate, G2M9-MTX Homo sapiens Man9GlcNAc2 + D-glucopyranose
-
?
mannose oligosaccharide + H2O substrate specificity of wild-type and mutant enzymes with different mannose oligosaccharides, overview Homo sapiens ?
-
?
additional information glucosidase II is a glycan-processing enzyme that trims two alpha1,3-linked glucose residues from N-glycan on newly synthesized glycoproteins Homo sapiens ?
-
?
additional information the isolated beta-subunit domain GIIbeta-MRH binds to high-mannose-type glycans in HeLaS3 cells, most strongly to the glycans with the alpha1,2-linked mannobiose structure, overview Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
heterodimer glucosidase II is a heterodimeric complex consisting of a catalytic alpha subunit GIIalpha, and a tightly associated beta subunit GIIbeta that contains a mannose 6-phosphate receptor homology domain, MRH domain, which is responsible for the glucose trimming process via its putative sugar-binding activity Homo sapiens

Synonyms

Synonyms Comment Organism
alpha-glucosidase II
-
Homo sapiens

General Information

General Information Comment Organism
physiological function glucosidase II is a glycan-processing enzyme that trims two alpha1,3-linked glucose residues from N-glycan on newly synthesized glycoproteins. Trimming of the first alpha1,3-linked glucose from Glc2Man9GlcNAc2 is important for a glycoprotein to interact with calnexin/calreticulin, and cleavage of the innermost glucose from GlcMan9GlcNAc2 sets glycoproteins free from the CNX/CRT cycle and allows them to proceed to the Golgi apparatus Homo sapiens