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Information on EC 3.2.1.207 - mannosyl-oligosaccharide alpha-1,3-glucosidase and Organism(s) Mus musculus and UniProt Accession Q8BHN3
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3.2.1.207 mannosyl-oligosaccharide alpha-1,3-glucosidaseIUBMB Comments
This eukaryotic enzyme cleaves off sequentially the two alpha-1,3-linked glucose residues from the Glc2Man9GlcNAc2 oligosaccharide precursor of immature N-glycosylated proteins.
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Word Map
- 3.2.1.207
-
polycystic
- cyst
-
hepatocystin
-
cystogenesis
-
adpld
- polycystin-1
-
cholangiocytes
-
glucosidases
-
glc1man9glcnac2
-
glycan-processing
-
dnajb11
-
sec61b
- analysis
- medicine
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
prkcsh, ganab, giibeta, er glucosidase ii, alpha glucosidase ii, glucosidase ii beta-subunit, endoplasmic reticulum glucosidase ii, plant glucosidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-glucosidase II
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ER glucosidase II
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GANAB
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-
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GTB1
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PRKCSH
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ROT2
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trimming glucosidase II
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SYSTEMATIC NAME
IUBMB Comments
Glc2Man9GlcNAc2-[protein] 3-alpha-glucohydrolase (configuration-inverting)
This eukaryotic enzyme cleaves off sequentially the two alpha-1,3-linked glucose residues from the Glc2Man9GlcNAc2 oligosaccharide precursor of immature N-glycosylated proteins.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
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-
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?
additional information
?
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the catalytic enzyme alpha subunit, with the help of mannose 6-phosphate receptor homology domain of the beta-subunit, sequentially hydrolyzes two alpha1-3-linked glucose residues in the second step of N-linked oligosaccharide-mediated protein folding
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?
additional information
?
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Catalyzes the hydrolysis of the inner two alpha-1,3-linked glucose residues present in all N-linked immature oligosaccharides, associates with and glycosylates the protein CD45, possible role in CD45 regulation
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?
additional information
?
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involved in early glycoprotein biogenesis, catalyzes the hydrolysis of two alpha-1,3-linked glucose residues present on all Asn-linked precursor oligosaccharides
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Catalyzes the hydrolysis of the inner two alpha-1,3-linked glucose residues present in all N-linked immature oligosaccharides, associates with and glycosylates the protein CD45, possible role in CD45 regulation
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-
?
additional information
?
-
-
involved in early glycoprotein biogenesis, catalyzes the hydrolysis of two alpha-1,3-linked glucose residues present on all Asn-linked precursor oligosaccharides
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-
?
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
mRNA level and enzyme activity reach its peak level in the mid- or late lactation stages, like other N-glycosylation enzymes, and shows an up-regulation of 2.5-4fold at mid- to late lactation
additional information
tissue-specific expression pattern of the enzyme, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the soluble alpha subunit is retained in the endoplasmic reticulum through its interaction with the HDEL-containing beta subunit
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme is continuously requirement in correct folding of cell surface proteins
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GANAB_MOUSE
944
1
106911
Swiss-Prot
Mitochondrion (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
116000
80000
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alpha, beta, 1 * 116000 + 1 * 80000, SDS-PAGE, the beta subunit contains two domains that are capable to associate with the alpha subunit
116000
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alpha, beta, 1 * 116000 + 1 * 80000, SDS-PAGE, the beta subunit contains two domains that are capable to associate with the alpha subunit
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
enzyme peptide proteolysis and fragment analysis, overview
dimer
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alpha, beta, 1 * 116000 + 1 * 80000, SDS-PAGE, the beta subunit contains two domains that are capable to associate with the alpha subunit
dimer
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alpha, beta, 1* 116000 + 1 * 84000, SDS-PAGE, catalytically active alpha subunit, beta subunit with unknown function
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
small-angle X-ray scattering and crystal structures of enzyme alone and in complex with key ligands of its catalytic cycle and antiviral iminosugars. A conformational rearrangement is needed for the simultaneous binding of a monoglucosylated glycan to both subunits. An insertion between the +1 and +2 subsites contributes to the enzyme's activity and substrate specificity, and the presence of D-mannose at the +1 subsite renders the acid catalyst less efficient during the cleavage of the monoglucosylated substrate
structures of a trypsinolytic fragment, alone and in complex with catalytic cycle ligands, and four different broad-spectrum antiviral iminosugar inhibitors
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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construction of several truncated forms of the beta subunit with different capabilities of binding the alpha subunit
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant fusion forms of the enzyme in Sf9 insect cells
fragments and full length beta-subunit expressed as GST-fusion protein in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ethanol-sensitive GIIbeta is upregulated by about 70% in ethanol-exposed cerebral cortex
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
inhibitors of the enzyme are used to inhibit cell proliferation and migration in a variety of different pathologies, such as viral infection, cancer, and diabetes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Roth, J.; Ziak, M.; Zuber, C.
The role of glucosidase II and endomannosidase in glucose trimming of asparagine-linked oligosaccharides
Biochimie
85
287-294
2003
Bos taurus, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Sus scrofa
Arendt, C.W.; Ostergaard, H.L.
Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit
Glycobiology
10
487-492
2000
Mus musculus
Baldwin, T.A.; Gogela-Spehar, M.; Ostergaard, H.L.
Specific isoforms of the resident endoplasmic reticulum protein glucosidase II associate with the CD45 protein-tyrosine phosphatase via a lectin-like interaction
J. Biol. Chem.
275
32071-32076
2000
Mus musculus
Feng, J.; Romaniouk, A.V.; Samal, S.K.; Vijay, I.K.
Processing enzyme glucosidase II: proposed catalytic residues and developmental regulation during the ontogeny of the mouse mammary gland
Glycobiology
14
909-921
2004
Mus musculus (Q8BHN3)
Anji, A.; Kumari, M.
A cis-acting region in the N-methyl-D-aspartate R1 3'-untranslated region interacts with the novel RNA-binding proteins beta subunit of alpha glucosidase II and annexin A2 - effect of chronic ethanol exposure in vivo
Eur. J. Neurosci.
34
1200-1211
2011
Mus musculus
Anji, A.; Miller, H.; Raman, C.; Phillips, M.; Ciment, G.; Kumari, M.
Expression of alpha-subunit of alpha-glucosidase II in adult mouse brain regions and selected organs
J. Neurosci. Res.
93
82-93
2015
Mus musculus (Q8BHN3), Mus musculus C57BL/6 (Q8BHN3)
Anji, A.; Miller, H.; Raman, C.; Phillips, M.; Ciment, G.; Kumari, M.
Expression of alpha subunit of alpha-glucosidase II in adult mouse brain regions and selected organs
J. Neurosci. Res.
93
82-93
2015
Mus musculus
Caputo, A.; Alonzi, D.; Marti, L.; Reca, I.; Kiappes, J.; Struwe, W.; Cross, A.; Basu, S.; Lowe, E.; Darlot, B.; Santino, A.; Roversi, P.; Zitzmann, N.
Structures of mammalian ER α-glucosidase II capture the binding modes of broad-spectrum iminosugar antivirals
Proc. Natl. Acad. Sci. USA
113
E4630-E4638
2016
Mus musculus (Q8BHN3)
Caputo, A.; Alonzi, D.; Kiappes, J.; Struwe, W.; Cross, A.; Basu, S.; Darlot, B.; Roversi, P.; Zitzmann, N.
Structural insights into the broad-spectrum antiviral target endoplasmic reticulum alpha-glucosidase II
Adv. Exp. Med. Biol.
1062
265-276
2018
Mus musculus (Q8BHN3), Mus musculus
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Release 2023.1 (January 2023)
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