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Information on EC 3.2.1.130 - glycoprotein endo-alpha-1,2-mannosidase and Organism(s) Rattus norvegicus and UniProt Accession Q5GF25
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3.2.1.130 glycoprotein endo-alpha-1,2-mannosidaseIUBMB Comments
The enzyme catalyses the hydrolysis of the terminal alpha-D-glucosyl-(1->3)-D-mannosyl unit from the GlcMan9(GlcNAc)2 oligosaccharide component of N-glucosylated proteins during their processing in the Golgi apparatus. The name for the isomer is based on a nomenclature proposed by Prien et al .
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Word Map
- 3.2.1.130
- oligosaccharide
-
glucosidase
-
n-linked
-
deglucosylation
-
trim
-
glucosylated
- castanospermine
-
polymannose
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glucose-substituted
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monoglucosylated
-
spiro
- man8glcnac
- 1-deoxymannojirimycin
-
triglucosylated
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castanospermine-treated
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ii-deficient
- 1-deoxynojirimycin
-
paranoia
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glc1man9glcnac
- medicine
- synthesis
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
endomannosidase, manea, endo-alpha-d-mannosidase, endo-alpha-mannosidase, golgi-endomannosidase, alpha-endomannosidase, glucosyl mannosidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
endo-alpha-D-mannosidase
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-
-
-
endo-alpha-mannosidase
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-
-
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endomannosidase
glucosyl mannosidase
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-
-
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glucosylmannosidase
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-
-
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endomannosidase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
-
PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
glycoprotein glucosylmannohydrolase
The enzyme catalyses the hydrolysis of the terminal alpha-D-glucosyl-(1->3)-D-mannosyl unit from the GlcMan9(GlcNAc)2 oligosaccharide component of N-glucosylated proteins during their processing in the Golgi apparatus. The name for the isomer is based on a nomenclature proposed by Prien et al [7].
CAS REGISTRY NUMBER
COMMENTARY
108022-16-8
-
125858-79-9
-
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
GlcMan5GlcNAc2 + H2O
alpha-D-glucosyl-1,3-D-mannopyranose + Man4GlcNAc2
37°C
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
-
-
?
human alpha1-antitrypsin + H2O
?
acts on both native and misfolded variants of alpha1-antitrypsin, establishing its function as a Golgi apparatus-located back-up mechanism for protein N-glycosylation
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
at 11% the rate of GlcMan9GlcNAc hydrolysis
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
-
-
cleaves internally between the glucose-substituted mannose and the remaining oligosaccharide to release a Glcalpha1,3Man disaccharide
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
-
best substrate
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
-
biosynthesis of N-linked glycoproteins
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
-
glucose trimming of asparagine-linked oligosaccharides
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
-
only processing enzyme which cleaves internally and provides an alternate deglucosylation pathway
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
-
processing enzyme, accomplishes deglucosylation of glycoproteins with N-linked carbohydrate units
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?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
-
triming of N-linked oligosaccharides
-
?
vesicular stomatitis virus G protein + H2O
?
-
G protein processing in vivo
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-
?
additional information
?
-
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little or no activity with di- or triglucosylated oligosaccharide as substrate
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-
?
additional information
?
-
-
also acts effectively on oligosaccharide lipids
-
-
?
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
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
-
biosynthesis of N-linked glycoproteins
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
-
glucose trimming of asparagine-linked oligosaccharides
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
-
only processing enzyme which cleaves internally and provides an alternate deglucosylation pathway
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
-
processing enzyme, accomplishes deglucosylation of glycoproteins with N-linked carbohydrate units
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
-
triming of N-linked oligosaccharides
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not impaired by 1-deoxynojirimycin, no inhibition by EDTA
-
additional information
-
brefeldin A prevents the maturation of endomannosidase
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
specific activity 10.855 units/mg, 1 unit is the amount of enzyme that catalyzes the release of 1000 dpm of glucosyl-alpha-3Man in 1 h
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
endothelial cells are unreactive for endomannosidase, no activity in stomach mucosa, adrenal cortex and medulla, and testis sertoli cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
its cytoplasmic domain is required for its efficient Golgi localization. Proper topology rather than the presence of positively charged amino acids in the cytoplasmic tail is critical for Golgi localization of rat endomannosidase
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recombinant rat endomannosidase exhibits a cis- and medial-Golgi localization
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rat endomannosidase is a type II membrane protein, its transmembrane domain is required for its efficient Golgi localization, i.e. is necessary for the Golgi retention
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). MANEA_RAT
462
1
53416
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58000
Golgi-localized rat endomannosidase species, immunoprecipitation/Western blot analysis
61000
Golgi-localized rat endomannosidase species, immunoprecipitation/Western blot analysis
56000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
W188C
processing of the oligosaccharides of alpha1-antitrypsin is reduced, greatly diminished enzyme activity
additional information
-
in CHO-K1 cells expressing DELTAsig-rEndo, lacking the whole signal sequence, or DELTATMD-rEndo, lacking the transmembrane domain, endomannosidase is undetectable. DELTACT-rEndo, lacking the cytoplasmic tail, exhibits an ER localization and fails to maintain a type II membrane topology
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, isolated membranes, storage for 40 days with several freeze-thawings results in about a 30% loss in activity
-
-80°C, purified enzyme, at 0.03 mg protein/ml pH 6.8, 50% loss of activity within 6 months, increased stability at 0.5 mg protein/ml, bovine serum albumin stabilizes
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
myc-tagged rat endomannosidase expressed in CHO Lec23 cells, generation of rat/CHO endomannosidase hybrid constructs
subcloned into the expression vector pcDNA6/myc-His, overexpression in clone 9 cells and castanospermine-treated hepatocytes
endomannosidase subcloned into the HindIII/XhoI site of the pcDNA6 vector in frame with the myc-tag or into the Hind III/Bam HI site of the pEGFP vector for endomannosidase, expressed in CHO-K1 cells. CHO-K1 cells expressing DELTAsig-rEndo or DELTATMD-rEndo
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lubas, W.A.; Spiro, R.G.
Golgi endo-alpha-D-mannosidase from rat liver, a novel N-linked carbohydrate unit processing enzyme
J. Biol. Chem.
262
3775-3781
1987
Rattus norvegicus, Rattus norvegicus Cd
Tulsiani, D.R.P.; Coleman, V.D.; Touster, O.
Asparagine-linked glycoprotein biosynthesis in rat brain: identification of glucosidase I, glucosidase II, and and endomannosidase (glucosyl mannosidase)
Arch. Biochem. Biophys.
277
114-121
1990
Rattus norvegicus, Rattus norvegicus Wistar
Hiraizumi, S.; Spohr, U.; Spiro, R.G.
Ligand affinity chromatographic purification of rat liver Golgi endomannosidase
J. Biol. Chem.
269
4697-4700
1994
Rattus norvegicus, Rattus norvegicus Cd
Spiro, M.J.; Bhoyroo, V.D.; Spiro, R.G.
Molecular cloning and expression of rat liver endo-alpha-mannosidase, an N-linked oligosaccharide processing enzyme
J. Biol. Chem.
272
29356-29363
1997
Rattus norvegicus (Q5GF25)
Karaivanova, V.K.; Luan, P.; Spiro, R.G.
Processing of viral envelope glycoprotein by the endomannosidase pathway: evaluation of host cell specificity
Glycobiology
8
725-730
1998
Bos taurus, Canis lupus familiaris, Dipodomys ordii, Mesocricetus auratus, Mus musculus, no activity in Cricetulus griseus, Rattus norvegicus, Sus scrofa
Dong, Z.; Zuber, C.; Spiro, M.J.; Spiro, R.G.; Roth, J.
Immunohistochemical evaluation of endomannosidase distribution in rat tissues: evidence for cell type-specific expression
Histochem. Cell Biol.
114
461-467
2000
no activity in Cricetulus griseus, Rattus norvegicus
Spiro, M.J.; Spiro, R.G.
Use of recombinant endomannosidase for evaluation of the processing of N-linked oligosaccharides of glycoproteins and their oligosaccharide-lipid precursors
Glycobiology
10
521-529
2000
no activity in Cricetulus griseus, Rattus norvegicus
Zuber, C.; Spiro, M.J.; Guhl, B.; Spiro, R.G.; Roth, J.
Golgi apparatus immunolocalization of endomannosidase suggests post-endoplasmic reticulum glucose trimming: implications for quality control
Mol. Biol. Cell
11
4227-4240
2000
Rattus norvegicus, Rattus norvegicus Wistar
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
Rattus norvegicus
Hamilton, S.R.; Li, H.; Wischnewski, H.; Prasad, A.; Kerley-Hamilton, J.S.; Mitchell, T.; Walling, A.J.; Davidson, R.C.; Wildt, S.; Gerngross, T.U.
Intact alpha-1,2-endomannosidase is a typical type II membrane protein
Glycobiology
15
615-624
2005
Homo sapiens (Q5SRI9), Homo sapiens, Rattus norvegicus (Q5GF25)
Torossi, T.; Fan, J.Y.; Sauter-Etter, K.; Roth, J.; Ziak, M.
Endomannosidase processes oligosaccharides of alpha1-antitrypsin and its naturally occurring genetic variants in the Golgi apparatus
Cell. Mol. Life Sci.
63
1923-1932
2006
Rattus norvegicus (Q5GF25)
Torossi, T.; Roth, J.; Ziak, M.
A single tryptophan residue of endomannosidase is crucial for Golgi localization and in vivo activity
Cell. Mol. Life Sci.
64
1881-1889
2007
Cricetulus griseus, Rattus norvegicus (Q5GF25)
Stehli, J.; Torossi, T.; Ziak, M.
Triple arginines in the cytoplasmic tail of endomannosidase are not essential for type II membrane topology and Golgi localization
Cell. Mol. Life Sci.
65
1609-1619
2008
Rattus norvegicus
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