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Information on EC 3.2.1.114 - mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LFR0
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3.2.1.114 mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidaseIUBMB Comments
The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. It removes two mannosyl residues, one linked by alpha1,3 linkage, and the other linked by alpha1,6 linkage, both of which are removed by the same catalytic site. The enzyme is sensitive to swainsonine.
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Word Map
- 3.2.1.114
- swainsonine
-
n-linked
- n-glycans
- brefeldin
- castanospermine
-
endoglycosidase
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asparagine-linked
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high-mannose
-
hybrid-type
-
complex-type
- alpha-mannosidases
-
locoweed
-
indolizidine
- 1-deoxymannojirimycin
-
locoism
- kifunensine
- giantin
- medicine
-
swainsonine-treated
- man5glcnac
-
intra-golgi
- 1-deoxynojirimycin
- oxytropis
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high-mannose-type
- beta-cop
- mannostatins
- glcnacman5glcnac2
- biotechnology
- drug development
- pharmacology
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
mannosidase ii, jack bean alpha-mannosidase, man2a1, alpha-mannosidase iix, dgmii, manii, alpha-mii, drosophila gmii, alpha-d-mannosidase ii, afams1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-D-mannosidase II
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-
-
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alpha-mannosidase II
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-
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alpha-mannosidase III
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-
-
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alpha1-3,6-mannosidase
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-
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exo-1,3-1,6-alpha-mannosidase
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-
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GlcNAc transferase I-dependent alpha1,3[alpha1,6]mannosidase
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-
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Golgi alpha-mannosidase II
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-
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Man II
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-
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MAN IIx
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-
-
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ManIII
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-
-
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mannosidase II
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-
-
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mannosidase, exo-1,3-1,6-alpha-
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-
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mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
(1->3)-(1->6)-mannosyl-oligosaccharide alpha-D-mannohydrolase (configuration-retaining)
The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. It removes two mannosyl residues, one linked by alpha1,3 linkage, and the other linked by alpha1,6 linkage, both of which are removed by the same catalytic site. The enzyme is sensitive to swainsonine.
CAS REGISTRY NUMBER
COMMENTARY
349553-33-9
alpha-mannosidase III
82047-77-6
alpha-mannosidase II
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-mannoside + H2O
4-nitrophenol + alpha-D-mannose
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-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))(Xylbeta(1-4))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + H2O
Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))(Xylbeta(1-4))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + alpha-D-mannose
-
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + H2O
Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + alpha-D-mannose
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside + H2O
Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside + alpha-D-mannose
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-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + H2O
Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + alpha-D-mannose
physiological substrate, conversion by sequential removal of two alpha1,6-linked and alpha1,3-linked mannose residues from the alpha-1,6-branch of the substrate
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-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + H2O
Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + alpha-D-mannose
conversion by sequential removal of two alpha1,6-linked and alpha1,3-linked mannose residues from the alpha-1,6-branch of the substrate
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-
?
additional information
?
-
Golgi alpha-mannosidase II is a key enzyme in the formation of complex N-glycans in plants
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-
?
additional information
?
-
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Golgi alpha-mannosidase II is a key enzyme in the formation of complex N-glycans in plants
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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
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + H2O
Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + alpha-D-mannose
physiological substrate, conversion by sequential removal of two alpha1,6-linked and alpha1,3-linked mannose residues from the alpha-1,6-branch of the substrate
-
-
?
additional information
?
-
Golgi alpha-mannosidase II is a key enzyme in the formation of complex N-glycans in plants
-
-
?
additional information
?
-
-
Golgi alpha-mannosidase II is a key enzyme in the formation of complex N-glycans in plants
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
the recombinant GMII contains zinc in a stoichiometric amount
additional information
additional information
no effect on recombinant GMII through Ca2+, Co2+, Mn2+, Ni2+, and Zn2+
additional information
-
no effect on recombinant GMII through Ca2+, Co2+, Mn2+, Ni2+, and Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no inhibition of recombinant GMII by EDTA
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.38
purified recombinant GMII expressed in insect cells, substrate 4-nitrophenyl alpha-mannoside
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Golgi alpha-mannosidase II, the enzyme has a transmembrane domain and a cytoplasmic tail sufficient for localisation of the enzyme to the Golgi complex, retention by lumenal sequences is not involved, retention mechanism
Golgi alpha-mannosidase II is a type II membrane protein
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). GMAN2_ARATH
1173
1
134726
Swiss-Prot
other Location (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme has a transmembrane domain and a cytoplasmic tail sufficient for localisation of the enzyme to the Golgi complex, retention by lumenal sequences is not involved
additional information
-
the enzyme has a transmembrane domain and a cytoplasmic tail sufficient for localisation of the enzyme to the Golgi complex, retention by lumenal sequences is not involved
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
recombinant secreted His-tagged soluble enzyme from culture medium of Spodoptera frugiperda Sf21 insect cells is N-glycosylated ans sensitive to PNGaseF
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of two Golgi alpha-mannosidase II knockout mutant plants, lines Salk_052443 and Salk_141821, resulting in predominant presence of unprocessed N-glycans but revealing also that alternative routes for N-glycan processing exist in the plants, mutant substrate specificity analysis, overview
additional information
-
construction of two Golgi alpha-mannosidase II knockout mutant plants, lines Salk_052443 and Salk_141821, resulting in predominant presence of unprocessed N-glycans but revealing also that alternative routes for N-glycan processing exist in the plants, mutant substrate specificity analysis, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant secreted His-tagged soluble enzyme from culture medium of Spodoptera frugiperda Sf21 insect cells by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
GMII, DNA and amino acid sequence determination and analysis, expression of His-tagged functional Golgi alpha-mannosidase II as soluble protein, which is secreted to the culture medium, in Spodoptera frugiperda Sf21 insect cells using the baculovirus transfection system, transient expression of GFP-tagged enzyme in Nicotiana benthamiana plants shows localization of the recombinant enzyme to the Golgi and endoplasmic reticulum
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Strasser, R.; Schoberer, J.; Jin, C.; Gloessl, J.; Mach, L.; Steinkellner, H.
Molecular cloning and characterization of Arabidopsis thaliana Golgi alpha-mannosidase II, a key enzyme in the formation of complex N-glycans in plants
Plant J.
45
789-803
2006
Arabidopsis thaliana (Q9LFR0), Arabidopsis thaliana
EXTERNAL LINKS (specific for EC-Number 3.2.1.114)
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