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Information on EC 3.2.1.113 - mannosyl-oligosaccharide 1,2-alpha-mannosidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9C512

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IUBMB Comments
This family of mammalian enzymes, located in the Golgi system, participates in the maturation process of N-glycans that leads to formation of hybrid and complex structures. The enzymes catalyse the hydrolysis of the four (1->2)-linked alpha-D-mannose residues from the Man9GlcNAc2 oligosaccharide attached to target proteins as described in reaction (1). Alternatively, the enzymes act on the Man8GlcNAc2 isomer formed by EC 3.2.1.209, endoplasmic reticulum Man9GlcNAc2 1,2-alpha-mannosidase, as described in reaction (2). The enzymes are type II membrane proteins, require Ca2+, and use an inverting mechanism. While all three human enzymes can catalyse the reactions listed here, some of the enzymes can additionally catalyse hydrolysis in an alternative order, generating additional isomeric intermediates, although the final product is the same. The names of the isomers listed here are based on a nomenclature system proposed by Prien et al .
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Arabidopsis thaliana
UNIPROT: Q9C512
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
mania, manic, mannosidase i, man1b1, man1a1, man9-mannosidase, man1c1, man1a2, golgi alpha-mannosidase i, mns1p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(alpha1,2)-mannosidase-I
-
-
-
-
1,2-alpha-mannosidase
-
-
-
-
alpha-1,2 mannosidase I
-
-
alpha-1,2-mannosidase
-
-
-
-
alpha-1,2-mannosidase IC
-
-
-
-
ER alpha-1,2-mannosidase
-
-
-
-
exo-alpha-1,2-mannanase
-
-
-
-
glycoprotein processing mannosidase I
-
-
-
-
Golgi alpha-mannosidase I
-
-
HMIC
-
-
-
-
Man(9)-alpha-mannosidase
-
-
-
-
Man9-mannosidase
-
-
-
-
Man9GlcNAc2-specific processing alpha-mannosidase
-
-
-
-
MANIa
MANIb
-
isozyme
mannose-9 processing alpha-mannosidase
-
-
-
-
mannosidase 1A
-
-
-
-
mannosidase 1B
-
-
-
-
mannosidase I
-
-
-
-
mannosidase, exo-1,2-alpha-
-
-
-
-
N-glycan processing class I alpha-1,2-mannosidase
-
-
-
-
processing alpha-1,2-mannosidase IC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Man9GlcNAc2-[protein] alpha-2-mannohydrolase (configuration-inverting)
This family of mammalian enzymes, located in the Golgi system, participates in the maturation process of N-glycans that leads to formation of hybrid and complex structures. The enzymes catalyse the hydrolysis of the four (1->2)-linked alpha-D-mannose residues from the Man9GlcNAc2 oligosaccharide attached to target proteins as described in reaction (1). Alternatively, the enzymes act on the Man8GlcNAc2 isomer formed by EC 3.2.1.209, endoplasmic reticulum Man9GlcNAc2 1,2-alpha-mannosidase, as described in reaction (2). The enzymes are type II membrane proteins, require Ca2+, and use an inverting mechanism. While all three human enzymes can catalyse the reactions listed here, some of the enzymes can additionally catalyse hydrolysis in an alternative order, generating additional isomeric intermediates, although the final product is the same. The names of the isomers listed here are based on a nomenclature system proposed by Prien et al [7].
CAS REGISTRY NUMBER
COMMENTARY hide
9068-25-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-3)[Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNACbeta(1-4)GlcNAc + 3 D-mannose
show the reaction diagram
-
-
-
?
methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
? + D-mannose
show the reaction diagram
-
-
-
?
[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc]-N-Asn-[protein] + H2O
[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc]-N-Asn-[protein] + D-mannose
show the reaction diagram
i.e. isomer 8A1,2,3B1,3
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + 4 H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + 4 D-mannose
show the reaction diagram
-
-
-
-
?
Man8GlcNAc2 + H2O
Man5GlcNAc2 + D-mannose
show the reaction diagram
-
-
-
-
?
Man9GlcNAc2 + 4 H2O
Man5GlcNAc2 + 4 D-mannose
show the reaction diagram
-
-
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNACbeta(1-4)GlcNAc + H2O
Manalpha(1-3)[Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNACbeta(1-4)GlcNAc + 4 D-mannose
show the reaction diagram
-
-
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-3)[Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNACbeta(1-4)GlcNAc + 3 D-mannose
show the reaction diagram
methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
? + D-mannose
show the reaction diagram
-
-
-
?
[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc]-N-Asn-[protein] + H2O
[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc]-N-Asn-[protein] + D-mannose
show the reaction diagram
i.e. isomer 8A1,2,3B1,3
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
required for activity, isozyme MANIa shows 450% relative activity at 15 mM Ca2+, isozyme MANIb shows 600% relative activity at 15 mM Ca2+
additional information
-
Co2+, Cu2+, Mg2+, Mn2+, and Zn2+ have no effect on activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxymannojirimycin
-
1-deoxymannojirimycin
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
1-deoxymannojirimycin
Arabidopsis thaliana
37°C, pH 6.0, substrate methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
0.00035
kifunensine
Arabidopsis thaliana
37°C, pH 6.0, substrate methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
0.04
1-deoxymannojirimycin
Arabidopsis thaliana
37°C, pH 6.0, substrate methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
0.00047
kifunensine
Arabidopsis thaliana
37°C, pH 6.0, substrate methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
isozyme MANIb
7
-
isozyme MANIa
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
isozymes MANIa and MANIb
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
abolishment of two functionally redundant mannosidases, MNS1 and MNS2, responsible for alpha-1,2-mannose trimming on the A and C branches of plant N-glycans lead to severe root growth inhibition under salt stress conditions in Arabidopsis
physiological function
malfunction
abolishment of two functionally redundant mannosidases, MNS1 and MNS2, responsible for alpha-1,2-mannose trimming on the A and C branches of plant N-glycans lead to severe root growth inhibition under salt stress conditions in Arabidopsis
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MNS1_ARATH
560
1
63532
Swiss-Prot
Mitochondrion (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
-
His-tagged isozymes MANIa and MANIb, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
ManI fusion constructs are derived from the full-length GFP fusion
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 6.5
-
isozyme MANIb
703909
5 - 10
-
isozyme MANIa
703909
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
isozymes MANIa and MANIb are relatively stable at lower temperature and still retain 50% of their original activities after incubation at 25°C for 1 h and show a significant decrease of activities at higher temperatures with 10% activity at 30°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Co2+-affinity column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana benthamiana leaf epidermal cells
expressed in Nicotiana benthamiana leaf epidermal cells
expressed in Sf9 cells as insoluble forms and in Escherichia coli as soluble forms
-
GFP-fusions are transferred into Agrobacterium tumefaciens by heat shock
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saint-Jore-Dupas, C.; Nebenfuehr, A.; Boulaflous, A.; Follet-Gueye, M.L.; Plasson, C.; Hawes, C.; Driouich, A.; Faye, L.; Gomord, V.
Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway
Plant Cell
18
3182-3200
2006
Arabidopsis thaliana, Solanum lycopersicum, Nicotiana tabacum, Glycine max (Q9SEH8), Glycine max
Manually annotated by BRENDA team
Kajiura, H.; Koiwa, H.; Nakazawa, Y.; Okazawa, A.; Kobayashi, A.; Seki, T.; Fujiyama, K.
Two Arabidopsis thaliana Golgi alpha-mannosidase I enzymes are responsible for plant N-glycan maturation
Glycobiology
20
235-247
2010
Arabidopsis thaliana
Manually annotated by BRENDA team
Liu, C.; Niu, G.; Zhang, H.; Sun, Y.; Sun, S.; Yu, F.; Lu, S.; Yang, Y.; Li, J.; Hong, Z.
Trimming of N-glycans by the Golgi-localized alpha-1,2-mannosidases, MNS1 and MNS2, is crucial for maintaining RSW2 protein abundance during salt stress in Arabidopsis
Mol. Plant
11
678-690
2018
Arabidopsis thaliana (Q8H116), Arabidopsis thaliana (Q9C512)
Manually annotated by BRENDA team
Liebminger, E.; Huettner, S.; Vavra, U.; Fischl, R.; Schoberer, J.; Grass, J.; Blaukopf, C.; Seifert, G.J.; Altmann, F.; Mach, L.; Strasser, R.
Class I alpha-mannosidases are required for N-glycan processing and root development in Arabidopsis thaliana
Plant Cell
21
3850-3867
2009
Arabidopsis thaliana (Q8H116), Arabidopsis thaliana (Q9C512)
Manually annotated by BRENDA team