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Information on EC 3.2.1.207 - mannosyl-oligosaccharide alpha-1,3-glucosidase and Organism(s) Schizosaccharomyces pombe and UniProt Accession Q9US55

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EC Tree
IUBMB 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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Schizosaccharomyces pombe
UNIPROT: Q9US55
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The taxonomic range for the selected organisms is: Schizosaccharomyces pombe
The enzyme appears in selected viruses and cellular organisms
Synonyms
prkcsh, ganab, giibeta, er glucosidase ii, alpha glucosidase ii, glucosidase ii beta-subunit, endoplasmic reticulum glucosidase ii, plant glucosidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-glucosidase II
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ER glucosidase II
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GANAB
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-
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PRKCSH
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-
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ROT2
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trimming glucosidase II
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PATHWAY SOURCE
PATHWAYS
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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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucose
show the reaction diagram
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-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucose
show the reaction diagram
-
-
-
?
maltohexaose + H2O
maltopentaose + D-glucose
show the reaction diagram
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-
-
?
maltose + H2O
2 D-glucose
show the reaction diagram
-
-
-
?
nigerose + H2O
2 D-glucose
show the reaction diagram
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
show the reaction diagram
-
the GIIbeta subunit is not required for GIIalpha activity toward the substrate
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-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucopyranose
show the reaction diagram
GlcMan9GlcNAc + H2O
D-glucose + Man9GlcNAc
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucopyranose
show the reaction diagram
GlcNAcalpha(1->3)GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + H2O
GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + D-glucose
show the reaction diagram
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-
-
-
?
GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + H2O
Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + D-glucose
show the reaction diagram
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-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucopyranose
show the reaction diagram
-
-
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucopyranose
show the reaction diagram
-
-
-
-
?
additional information
?
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the enzyme heterodimer is required to efficiently deglucosylate the physiological substrates G2M9 and G1M9
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
40 mM, 63% loss of activity
1-deoxynojirimycin
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-
additional information
NaCl, NaH2PO4, Na2SO4, NaNO3, KCl, MgCl2, or EDTA up to 40 mM do not affect activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
the interaction of the mannose 6-phosphate receptor homologous domain present in GIIbeta with mannoses in the B and/or C arms of the glycans mediates glycan hydrolysis enhancement
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15.3
maltohexaose
pH 6.5, 30°C
18
maltose
pH 6.5, 30°C
2.13
nigerose
pH 6.5, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.109
maltohexaose
pH 6.5, 30°C
0.241
maltose
pH 6.5, 30°C
0.102
nigerose
pH 6.5, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.15
maltohexaose
pH 6.5, 30°C
13.4
maltose
pH 6.5, 30°C
48.1
nigerose
pH 6.5, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit alpha
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the enzyme contains a signal peptide (first 23 amino acids) sequence
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
-
the inability of beta-subunit MRH domain to efficiently recognize glucose eliminates the potential for the beta-subunit to compete with the catalytic alpha-subunit of GII for glucose present in arm A of the N-glycan, ligand binding structures, overview. Possible models for the influence of Trp409 in enzyme activity
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
additional information
-
the interaction of the mannose 6-phosphate receptor homologous domain present in GIIbeta with mannoses in the B and/or C arms of the glycans mediates glycan hydrolysis enhancement
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mannose 6-phosphate receptor homology domain of GII beta subunit bound to mannose, to 1.6 A resolution. No major difference in the overall fold of ligand-bound and unbound structures, but a repositioning of side chains throughout the binding pocket, including Y372
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E114A
-
inactive towards Glc1Man9GlcNAc2
E457Q
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site-directed mutagenesis
E73A
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inactive towards Glc1Man9GlcNAc2
Q408E
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site-directed mutagenesis
R438K
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site-directed mutagenesis
W409A
W409F
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site-directed mutagenesis of the beta subunit MRH domain, the mutant shows altered ligand binding activity compared to the wild-type beta-subunit
Y372A
mutation of Y372 substantially decreases GII activity
Y372F
mutation of Y372 substantially decreases GII activity
Y463F
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site-directed mutagenesis
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 9.1
-
744528
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
complete inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 2 days, more than 60% loss of activity, presence of 10% v/v glycerol prevents this loss
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged beta-subunit by immobilized metal affinity chromatography from Escherichia coli strain BL21(pREP4)
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
beta-subunit, DNA and amino acid sequence determination and analysis, recombinant expression as His-tagged protein in Escherichia coli strain BL21(pREP4)
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cloning of alpha- and beta-subunits and expression in Escherichia coli strains DH5alpha and JA226
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expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in live Schizosaccharomyces pombe cells, a decrease in the number of mannoses in the glycan results in decreased glucosidase II activity
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
D'Alessio, C.; Fernndez, F.; Trombetta, E.S.; Parodi, A.J.
Genetic evidence for the heterodimeric structure of glucosidase II: the effect of disrupting the subunit-encoding genes on glycoprotein folding
J. Biol. Chem.
274
25899-25905
1996
Schizosaccharomyces pombe
Manually annotated by BRENDA team
Stigliano, I.D.; Caramelo, J.J.; Labriola, C.A.; Parodi, A.J.; DAlessio, C.
Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals
Mol. Biol. Cell
20
3974-3984
2009
Rattus norvegicus, Schizosaccharomyces pombe
Manually annotated by BRENDA team
Stigliano, I.D.; Alculumbre, S.G.; Labriola, C.A.; Parodi, A.J.; DAlessio, C.
Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo
Mol. Biol. Cell
22
1810-1823
2011
Leishmania mexicana, Schizosaccharomyces pombe
Manually annotated by BRENDA team
Olson, L.J.; Orsi, R.; Alculumbre, S.G.; Peterson, F.C.; Stigliano, I.D.; Parodi, A.J.; DAlessio, C.; Dahms, N.M.
Structure of the lectin mannose 6-phosphate receptor homology (MRH) domain of glucosidase II, an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum
J. Biol. Chem.
288
16460-16475
2013
Schizosaccharomyces pombe
Manually annotated by BRENDA team
Olson, L.; Orsi, R.; Peterson, F.; Parodi, A.; Kim, J.; DAlessio, C.; Dahms, N.
Crystal structure and functional analyses of the lectin domain of glucosidase II insights into oligomannose recognition
Biochemistry
54
4097-4111
2015
Schizosaccharomyces pombe (Q9USH8), Schizosaccharomyces pombe 972 (Q9USH8)
Manually annotated by BRENDA team
Okuyama, M.; Miyamoto, M.; Matsuo, I.; Iwamoto, S.; Serizawa, R.; Tanuma, M.; Ma, M.; Klahan, P.; Kumagai, Y.; Tagami, T.; Kimura, A.
Substrate recognition of the catalytic alpha-subunit of glucosidase II from Schizosaccharomyces pombe
Biosci. Biotechnol. Biochem.
81
1503-1511
2017
Schizosaccharomyces pombe (Q9US55), Schizosaccharomyces pombe 972 (Q9US55)
Manually annotated by BRENDA team