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Information on EC 3.2.1.209 - endoplasmic reticulum Man9GlcNAc2 1,2-alpha-mannosidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q93Y37

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IUBMB Comments
The enzyme, located in the endoplasmic reticulum, primarily trims a single alpha-1,2-linked mannose residue from Man9GlcNAc2 to produce Man8GlcNAc2 isomer 8A1,2,3B1,3 (the names of the isomers listed here are based on a nomenclature system proposed by Prien et al ). The removal of the single mannosyl residue occurs in all eukaryotes as part of the processing of N-glycosylated proteins, and is absolutely essential for further elongation of the outer chain of properly-folded N-glycosylated proteins in yeast. In addition, the enzyme is involved in glycoprotein quality control at the ER quality control compartment (ERQC), helping to target misfolded glycoproteins for degradation. When present at very high concentrations in the ERQC, the enzyme can trim the carbohydrate chain further to Man(5-6)GlcNAc2.
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Arabidopsis thaliana
UNIPROT: Q93Y37
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
edem1, ermani, edem3, er mannosidase i, alpha1,2-mannosidases, er mani, alpha1,2-mannosidase e-i, er alpha1,2-mannosidase i, class i alpha1,2-mannosidase, endoplasmic reticulum alpha1,2-mannosidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MAN1B1
-
-
-
-
MNS1
-
-
-
-
MNS3
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
Man9GlcNAc2-[protein]2-alpha-mannohydrolase (configuration-inverting)
The enzyme, located in the endoplasmic reticulum, primarily trims a single alpha-1,2-linked mannose residue from Man9GlcNAc2 to produce Man8GlcNAc2 isomer 8A1,2,3B1,3 (the names of the isomers listed here are based on a nomenclature system proposed by Prien et al [7]). The removal of the single mannosyl residue occurs in all eukaryotes as part of the processing of N-glycosylated proteins, and is absolutely essential for further elongation of the outer chain of properly-folded N-glycosylated proteins in yeast. In addition, the enzyme is involved in glycoprotein quality control at the ER quality control compartment (ERQC), helping to target misfolded glycoproteins for degradation. When present at very high concentrations in the ERQC, the enzyme can trim the carbohydrate chain further to Man(5-6)GlcNAc2.
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(1-3)[Manalpha(1-2)Manalpha(1-6)]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(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 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->2)-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)-alpha-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->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc]-N-Asn-[protein] + D-mannopyranose
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxymannojirimycin
-
additional information
not inhibitory: swainsonine
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035
1-deoxymannojirimycin
Arabidopsis thaliana
pH 6.0, 37°C, substrate methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
0.0003
kifunensine
Arabidopsis thaliana
pH 6.0, 37°C, substrate methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
isoform MNS3 probably resides in the cis-Golgi. the C-terminal region of MNS3 is sufficient for proper subcellular targeting
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MNS3_ARATH
624
1
69069
Swiss-Prot
other Location (Reliability: 2)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana benthamiana leaf epidermal cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q93Y37)
Manually annotated by BRENDA team