Information on EC 3.2.1.130 - glycoprotein endo-alpha-1,2-mannosidase

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The expected taxonomic range for this enzyme is: Eutheria

EC NUMBER
COMMENTARY
3.2.1.130
-
RECOMMENDED NAME
GeneOntology No.
glycoprotein endo-alpha-1,2-mannosidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hydrolysis of the terminal alpha-D-glucosyl-(1,3)-D-mannosyl unit from the GlcMan9(GlcNAc)2 oligosaccharide component of the glycoprotein produced in the Golgi membrane
show the reaction diagram
involved in the synthesis of glycoproteins
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
glycoprotein glucosylmannohydrolase
Involved in the synthesis of glycoproteins.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
alpha-1,2-endomannosidase
Q5SRI9
-
alpha-1,2-endomannosidase
Q5GF25
-
alpha-endomannosidase
-
-
endo-alpha-D-mannosidase
-
-
-
-
endo-alpha-mannosidase
-
-
-
-
endomannosidase
-
-
-
-
endomannosidase
-
-
endomannosidase
-
-
endomannosidase
Q5GF25
-
glucosyl mannosidase
-
-
-
-
glucosylmannosidase
-
-
-
-
Golgi-endomannosidase
-
-
Golgi-endomannosidase
Q5GF25
-
MANEA
-
-
CAS REGISTRY NUMBER
COMMENTARY
108022-16-8
-
125858-79-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
bovine
-
-
Manually annotated by BRENDA team
kangaroo rat
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
syrian or golden hamster
-
-
Manually annotated by BRENDA team
no activity in Cricetulus griseus
-
-
-
Manually annotated by BRENDA team
no activity in Cricetulus griseus
CHO cell line having no detectable endomannosidase activity
-
-
Manually annotated by BRENDA team
no activity in Cricetulus griseus
mutant Lec23
-
-
Manually annotated by BRENDA team
buffalo rat
-
-
Manually annotated by BRENDA team
buffalo rat; Wistar
-
-
Manually annotated by BRENDA team
Rattus norvegicus Cd
CD-strain
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
Wistar
-
-
Manually annotated by BRENDA team
pig
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Glc2Man9GlcNAc + H2O
?
show the reaction diagram
-
at 14% the rate of GlcMan9GlcNAc hydrolysis
-
-
?
Glc3Man9GlcNAc2 + H2O
?
show the reaction diagram
-
-
-
-
?
Glc3Man9GlcNAc2 + H2O
?
show the reaction diagram
-
at 11% the rate of GlcMan9GlcNAc hydrolysis
-
-
?
Glc3Man9GlcNAc2 + H2O
?
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
-
?
GlcMan5GlcNAc2 + H2O
alpha-D-glucosyl-1,3-D-mannopyranose + Man4GlcNAc2
show the reaction diagram
-
37C
-
-
?
GlcMan5GlcNAc2 + H2O
alpha-D-glucosyl-1,3-D-mannopyranose + Man4GlcNAc2
show the reaction diagram
Q5SRI9
37C
-
-
?
GlcMan7GlcNAc + H2O
?
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Wistar
-
at 71% the rate of GlcMan9GlcNAc hydrolysis
-
-
?
GlcMan8GlcNAc + H2O
?
show the reaction diagram
-
-
-
-
-
GlcMan8GlcNAc + H2O
?
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Wistar
-
at 89% the rate of GlcMan9GlcNAc hydrolysis
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
Q5GF25
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
cleaves internally between the glucose-substituted mannose and the remaining oligosaccharide to release a Glcalpha1,3Man disaccharide
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
best substrate, biosynthesis of N-linked glycoproteins
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
glucose trimming of asparagine-linked oligosaccharides
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
only processing enzyme which cleaves internally and provides an alternate deglucosylation pathway
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
processing enzyme, accomplishes deglucosylation of glycoproteins with N-linked carbohydrate units
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
triming of N-linked oligosaccharides
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
Rattus norvegicus Cd
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
Rattus norvegicus Cd
-
-, processing enzyme, accomplishes deglucosylation of glycoproteins with N-linked carbohydrate units
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
Rattus norvegicus Wistar
-
best substrate, biosynthesis of N-linked glycoproteins
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
Rattus norvegicus Wistar
-
-, triming of N-linked oligosaccharides
-
?
human alpha1-antitrypsin + H2O
?
show the reaction diagram
-
-
-
-
?
vesicular stomatitis virus G protein + H2O
?
show the reaction diagram
-
-
-
-
?
vesicular stomatitis virus G protein + H2O
?
show the reaction diagram
-
G protein processing in vivo
-
-
?
human alpha1-antitrypsin + H2O
?
show the reaction diagram
-
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
-
-
?
additional information
?
-
-
little or no activity with di- or triglucosylated oligosaccharide as substrate
-
-
-
additional information
?
-
-
also acts effectively on oligosaccharide lipids
-
-
-
additional information
?
-
Rattus norvegicus Wistar
-
little or no activity with di- or triglucosylated oligosaccharide as substrate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
Q5GF25
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
biosynthesis of N-linked glycoproteins
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
glucose trimming of asparagine-linked oligosaccharides
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
only processing enzyme which cleaves internally and provides an alternate deglucosylation pathway
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
processing enzyme, accomplishes deglucosylation of glycoproteins with N-linked carbohydrate units
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
-
triming of N-linked oligosaccharides
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
Rattus norvegicus Cd
-
-
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
Rattus norvegicus Cd
-
processing enzyme, accomplishes deglucosylation of glycoproteins with N-linked carbohydrate units
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
Rattus norvegicus Wistar
-
biosynthesis of N-linked glycoproteins
-
?
GlcMan9GlcNAc + H2O
Man8GlcNAc + glucosyl alpha1,3-mannose
show the reaction diagram
Rattus norvegicus Wistar
-
triming of N-linked oligosaccharides
-
?
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Glucosyl alpha1-3(1-deoxy)mannojirimycin
-
-
additional information
-
not impaired by 1-deoxynojirimycin, no inhibition by EDTA
-
additional information
-
unaffected by glucosidase inhibitors
-
additional information
-
brefeldin A prevents the maturation of endomannosidase
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Triton X-100
-
requirement, membrane-bound enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.2
-
Q5SRI9
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
9
-
about half-maximal activity at pH 6 and 8.5
5.5
7.5
-
about half-maximal activity at pH 5.8 and 7.7
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
Q5SRI9
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
baby hamster kidney cell line served as host for vesicular stomatitis virus
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
liver cell line served as host for vesicular stomatitis virus
Manually annotated by BRENDA team
-
BRL3A cell line
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
BRL3A cell line
-
Manually annotated by BRENDA team
-
thymoma cell line served as host for vesicular stomatitis virus
Manually annotated by BRENDA team
-
no activity due to molecular defect in endomannosidase, CHO cells have a W188C substitution, Trp188 is critical for Golgi localization and in vivo activity of endomannosidase
Manually annotated by BRENDA team
-
surface epithelium and crypt epithelium
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
clone 9
-
Manually annotated by BRENDA team
-
villus epithelium and crypt epithelium
Manually annotated by BRENDA team
-
distal and collecting tubules, no activity in proximal tubules
Manually annotated by BRENDA team
Q5SRI9
most prominent
Manually annotated by BRENDA team
-
most prominent
Manually annotated by BRENDA team
Rattus norvegicus Cd
-
;
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
cell line served as host for vesicular stomatitis virus
Manually annotated by BRENDA team
-
cell line serves as host for vesicular stomatitis virus
Manually annotated by BRENDA team
-
cell line serves as host for vesicular stomatitis virus
Manually annotated by BRENDA team
-
liver cell line
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
liver cell line
-
Manually annotated by BRENDA team
-
seminiferous tubules and Leydig cells
Manually annotated by BRENDA team
-
kidney cell line served as host for vesicular stomatitis virus
Manually annotated by BRENDA team
additional information
-
endothelial cells are unreactive for endomannosidase, no activity in stomach mucosa, adrenal cortex and medulla, and testis sertoli cells
Manually annotated by BRENDA team
additional information
-
clone 9 hepatocyte
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
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
Manually annotated by BRENDA team
-
rough endoplasmic reticulum
Manually annotated by BRENDA team
Rattus norvegicus Cd
-
rough endoplasmic reticulum
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
; pre-Golgi intermediate
Manually annotated by BRENDA team
-
in pre-Golgi intermediates
Manually annotated by BRENDA team
-
recombinant rat endomannosidase exhibits a cis- and medial-Golgi localization
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Cd
-
;
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Rattus norvegicus Cd
-
;
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
intrinsic microsomal membrane component
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
intrinsic microsomal membrane component
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
52000
-
-
cDNA analysis
53000
-
-
ER-retained CHO cell endomannosidase, immunoprecipitation/Western blot analysis
53220
-
-
sequence analysis
56000
-
-
SDS-PAGE
58000
-
-
Golgi-localized rat endomannosidase species, immunoprecipitation/Western blot analysis
61000
-
-
Golgi-localized rat endomannosidase species, immunoprecipitation/Western blot analysis
380000
-
-
gel filtration
560000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q5SRI9
x * 55000, SDS-PAGE
?
-
x * 59000, SDS-PAGE
oligomer
-
? * 56000 + ? * 60000, 8-10 subunits, SDS-PAGE
oligomer
Rattus norvegicus Cd
-
? * 56000 + ? * 60000, 8-10 subunits, SDS-PAGE
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
phosphorylation is occurring in the Golgi apparatus
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, isolated membranes, storage for 40 days with several freeze-thawings results in about a 30% loss in activity
-
-80C, in intact Golgi membranes, 10% loss of activity within 6 months
-
-80C, 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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant protein, expressed in Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cloning of endomannosidase from CHO-K1 cells, amplicon subcloned into the Hind III/Xho I sites of the expression vector pcDNA6/myc-His, in frame with the C-terminal myc- and His-tag. Myc-tagged CHO endomannosidase expressed in CHO Lec23 cells. Generation of rat/CHO endomannosidase hybrid constructs
-
expression in Pichia pastoris
Q5SRI9
cDNA expressed in Escherichia coli
-
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
-
expressed in CHO-K1 cells
-
expressed in Escherichia coli JM109
-
expression in Pichia pastoris
-
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
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C188A
-
enzymatic activity can not be fully rescued with a back-engineered Cys188Ala CHO cell endomannosidase
C188S
-
enzymatic activity can not be fully rescued with a back-engineered Cys188Ser CHO cell endomannosidase
C188W
-
enzyme activity can be reversed in cells with a back-engineered Cys188Trp CHO cell endomannosidase, in particular N-glycans of alpha1-antitrypsin become fully processed
W188C
-
processing of the oligosaccharides of alpha1-antitrypsin is reduced, greatly diminished enzyme activity
W188C
-
molecular defect in CHO cells, is functionally important since it alone results in endoplasmic reticulum mislocalization of endomannosidase and causes greatly reduced in vivo 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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
cocaine-induced paranoia is associated with 6 single-nucleotide polymorphisms in European American families and 9 single-nucleotide polymorphisms in African American families. Association of MANEA single-nucleotide polymorphisms with cocaine dependence in both family samples is much weaker. The A allele of the 3' untranslated region single-nucleotide polymorphism rs9387522 is associated with increased risk of cocaine-induced paranoia