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Information on EC 3.2.1.209 - endoplasmic reticulum Man9GlcNAc2 1,2-alpha-mannosidase
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EC Tree
3.2.1.209 endoplasmic reticulum Man9GlcNAc2 1,2-alpha-mannosidaseIUBMB 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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Word Map
- 3.2.1.209
-
er-associated
-
misfolded
-
trim
- n-glycans
- calnexin
-
edems
-
reticulum-associated
- kifunensine
- man8glcnac2
-
degradation-enhancing
-
retrotranslocation
-
er-derived
-
mannose-trimming
- 1-deoxymannojirimycin
-
p58ipk
-
xtp3-b
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
edem1, ermani, edem3, er mannosidase i, alpha1,2-mannosidases, alpha1,2-mannosidase e-i, er mani, er alpha1,2-mannosidase i, class i alpha1,2-mannosidase, endoplasmic reticulum alpha1,2-mannosidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-mannosidase
alpha1,2-mannosidases
endoplasmic reticulum alpha1,2-mannosidase
ER ManI
ER mannosidase I
ERManI
Golgi alpha1,2-mannosidase IA
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
Golgi alpha1,2-mannosidase IB
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
MAN1B1
MNS1
MNS3
MAN1B1
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MNS1
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MNS3
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Man9GlcNAc2-[protein] + H2O = Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,3) + D-mannopyranose
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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
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.
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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
2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose + H2O
2 alpha-D-mannose
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-
-
?
4-methylumbelliferyl alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranoside
4-methylumbelliferyl-alpha-D-mannopyranoside
4-methylumbelliferone + D-mannose
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MUaMan, fluorogenic substrate
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-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannose
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + D-mannopyranose
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-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + D-mannose
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MUaMan fluorogenic substrate to measure enzyme activity
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?
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine + 3 H2O
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine + 3 D-mannopyranose
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-
-
?
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine + 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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine + D-mannopyranose
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)]-alpha-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->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein] + D-mannopyranose
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-
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?
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 + 2 H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[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 + 2 D-mannose
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?
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 + 3 H2O
alpha-D-mannopyranosyl-(1,2)-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 + 3 D-mannose
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-
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?
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
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?
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 + H2O
? + D-mannose
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to measure enzyme activity
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?
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 + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[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 + D-mannose
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 + H2O
? + D-mannose
-
to measure enzyme activity
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-
?
alpha1-antitrypsin NHK + H2O
? + D-mannose
substrate is a variant of alpha1-antitrypsin and substrate for ER-associated degradation of misfolded proteins
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-
?
alpha1-antitrypsin null + H2O
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 + D-mannose
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[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 + D-mannose
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[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 + D-mannose
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-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 + D-mannose
alpha1-antitrypsin null + 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 + D-mannose
Glc3Man9GlcNAc2 + H2O
alpha-D-mannopyranose + ?
-
from oligosaccharide-lipid
-
?
Glcalpha(1-3)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
Glcalpha(1-3)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
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-
-
-
?
glycan residues of alpha1-antitrypsin NHK + H2O
? + D-mannose
substrate is a variant of alpha1-antitrypsin and substrate for ER-associated degradation of misfolded glycoproteins
-
-
?
human alpha1-antitrypsin genetic variant null + H2O
? + D-mannose
substrate misfolds following biosynthesis
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-
?
Man7GlcNAc2 + H2O
alpha-D-mannopyranose + ?
-
from oligosaccharide-lipid, very low activity
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?
Man9GlcNAc2 + H2O
Man5GlcNAc2 + Man6GlcNAc2 + Man7GlcNAc2 + Man8GlcNAc2 + alpha-D-mannopyranose
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from thyroglobulin or oligosaccharide-lipid, trimming the substrate to Man8GlcNAc2, the substrate for oligosaccharide elongation
only alpha-(1-2)-linked terminal mannoses on the alpha-3-branch of the Man9GlcNAc precursor dispensable
?
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
-
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-2)Manalpha(1-3)]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
-
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-2)Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)[Manalpha(1-2)Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
-
-
?
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(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + H2O
Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + D-mannose
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-Asn + H2O
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta + D-mannose
methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
? + D-mannose
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
-
-
-
?
pyridylaminated Man9GlcNAc2 + H2O
pyridylaminated Man8GlcNAc2 + D-mannose
-
-
product is pyridylamino derivative of (Man)8(GlcNAc)2
?
[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
4-methylumbelliferyl alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranoside
-
-
-
-
?
4-methylumbelliferyl alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranoside
-
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannose
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannose
-
-
-
?
4-nitrophenyl alpha-D-mannopyranoside + H2O
4-nitrophenol + alpha-D-mannopyranoside
-
-
-
-
?
4-nitrophenyl alpha-D-mannopyranoside + H2O
4-nitrophenol + alpha-D-mannopyranoside
-
-
-
-
?
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine + 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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine + D-mannopyranose
-
-
-
?
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine + 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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine + D-mannopyranose
pyridylamine-tagged Man9GlcNAc2
-
-
?
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 + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[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 + D-mannose
-
-
-
-
?
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 + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[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 + D-mannose
-
-
-
?
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 + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[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 + D-mannose
-
-
-
-
?
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 + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[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 + D-mannose
-
-
-
?
alpha1-antitrypsin null + H2O
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 + D-mannose
-
-
-
-
?
alpha1-antitrypsin null + H2O
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 + D-mannose
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[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 + D-mannose
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[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 + D-mannose
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[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 + D-mannose
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[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 + D-mannose
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-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 + D-mannose
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-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 + D-mannose
-
-
-
?
alpha1-antitrypsin null + 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 + D-mannose
-
overexpression of each Golgi alpha1,2-mannosidase enhances alpha1-antitrypsin null degradation and trimming of its N-glycans to 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
-
-
?
alpha1-antitrypsin null + 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 + D-mannose
overexpression of each Golgi alpha1,2-mannosidase enhances alpha1-antitrypsin null degradation and trimming of its N-glycans to 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
-
-
?
Man9GlcNAc + H2O
Man8GlcNAc + alpha-D-mannopyranose
-
highly specific soluble catalytic domain of a larger membrane-bound form, does not act on synthetic substrates
releases only one specific mannopyranose residue
?
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(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
cytosolic isoform E-I
-
-
?
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(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
cytosolic isoform E-I
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
product is Man8GlcNAc
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
mutant R273L
product of mutant R273L, product of wild type is Man8GlcNAc
?
Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + H2O
Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + D-mannose
-
-
-
-
?
Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + H2O
Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + D-mannose
-
-
-
-
?
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-Asn + H2O
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta + D-mannose
-
-
-
-
?
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-Asn + H2O
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta + D-mannose
-
-
-
-
?
[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
-
-
-
?
[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
-
-
-
-
?
additional information
?
-
enzyme is involved in the processing of N-linked mannans
-
-
?
additional information
?
-
-
enzyme is involved in the processing of N-linked mannans
-
-
?
additional information
?
-
cytosolic isoform E-I trims free Man8GlcNac2 isomer B into Man7GlcNac2 isomer B
-
-
?
additional information
?
-
-
cytosolic isoform E-I trims free Man8GlcNac2 isomer B into Man7GlcNac2 isomer B
-
-
?
additional information
?
-
cytosolic isoform E-I trims free Man8GlcNac2 isomer B into Man7GlcNac2 isomer B
-
-
?
additional information
?
-
-
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
-
-
?
additional information
?
-
-
targets misfolded glycoproteins for dislocation into the cytosol and destruction by 26 S proteasomes
-
-
?
additional information
?
-
-
when being targeted to endoplasmic reticulum-associated degradation, a misfolded glycoprotein undergoes endoplasmic reticulum mannosidase I-dependent trimming to yield the N-linked oligosaccharide structures Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine and Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine
-
-
?
additional information
?
-
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
-
-
?
additional information
?
-
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine + 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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine + D-mannopyranose
-
-
-
?
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)]-alpha-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->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein] + D-mannopyranose
-
-
-
-
?
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 + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[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 + D-mannose
Glc3Man9GlcNAc2 + H2O
alpha-D-mannopyranose + ?
-
from oligosaccharide-lipid
-
?
Man7GlcNAc2 + H2O
alpha-D-mannopyranose + ?
-
from oligosaccharide-lipid, very low activity
-
?
Man9GlcNAc + H2O
Man8GlcNAc + alpha-D-mannopyranose
-
highly specific soluble catalytic domain of a larger membrane-bound form, does not act on synthetic substrates
releases only one specific mannopyranose residue
?
Man9GlcNAc2 + H2O
Man5GlcNAc2 + Man6GlcNAc2 + Man7GlcNAc2 + Man8GlcNAc2 + alpha-D-mannopyranose
-
from thyroglobulin or oligosaccharide-lipid, trimming the substrate to Man8GlcNAc2, the substrate for oligosaccharide elongation
only alpha-(1-2)-linked terminal mannoses on the alpha-3-branch of the Man9GlcNAc precursor dispensable
?
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(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
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 + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[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 + D-mannose
-
-
-
-
?
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 + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[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 + D-mannose
-
-
-
?
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(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
cytosolic isoform E-I
-
-
?
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(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
cytosolic isoform E-I
-
-
?
additional information
?
-
enzyme is involved in the processing of N-linked mannans
-
-
?
additional information
?
-
-
enzyme is involved in the processing of N-linked mannans
-
-
?
additional information
?
-
-
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
-
-
?
additional information
?
-
-
targets misfolded glycoproteins for dislocation into the cytosol and destruction by 26 S proteasomes
-
-
?
additional information
?
-
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
-
-
?
additional information
?
-
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
Ca2+
-
inhibition by EGTA can be 90% restored after addition of 0.1 mM
Ca2+
-
requirement, protects from thermal inactivation, Km value 0.5 mM
Ca2+
the calcium ion binds to the carbonyl oxygen and the Ogamma of residue T525, and to four water molecules that are in turn hydrogen-bonded to one of the two carboxylate groups of residues E279, E435, E438 and E503
additional information
-
the enzyme activity os not sensitive to the presence of Ca2+, Mg2+ and Mn2+ at concentrations up to 3 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
brefeldin A
-
known inhibitor of vesicle transport, ablated intracellular turnover of the radiolabeled molecules. Plus digestion with potato acid phosphatase implies that phosphorylation of ER mannosidase I is responsible for the altered electrophoretic mobility
D-mannonolactam amidrazone
-
inhibitor is a mimic of the mannopyranosyl cation and acts as a potent broad spectrum mannosidase inhibitor. It is inactive against processing glucosidases I and II
N-carbobenzoxyl-leucinyl-leucinyl-leucinal
-
degradation is inhibited by the proteasomal inhibitor
pepstatin A
-
in the presence of mixed membrane fraction from strain ATTC 26555, the 52 kDa polypeptide is converted into a 43 kDa active product. Protease inhibitors, such as phenylmethylsulphonylfluoride, trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane and 1,10-phenantroline, fail to prevent proteolysis. Pepstatin A, an aspartyl protease inhibitor, fully blocked enzyme processing
1-deoxymannojirimycin
-
trimming is inhibited preferentially by 1-deoxymannojirimycin, inhibits hydrolysis of 4-methylumbelliferyl-alpha-D-mannopyranoside
1-deoxymannojirimycin
-
DMJ, inhibition of 4-methylumbelliferyl-alpha-D-mannopyranoside hydrolysis
1-deoxymannojirimycin
found in crystal structures of the active site
1-deoxymannojirimycin
-
the enzyme is inhibited preferentially by 1-deoxymannojirimycin
Chloroquine
-
lysosomotrophic amine capable of raising the pH of acidic intracellular compartments, added to the medium with weak inhibition
Chloroquine
-
lysosomotrophic amine capable of raising the pH of acidic intracellular compartments, effect on the intracellular fate of endogenous mouse ER mannosidase I
Co2+
-
50% reduction in alpha-mannosidase activity is observed after addition of 3 mM CoCl2
kifunensine
-
inhibits Golgi alpha1,2-mannosidase. Addition of kifunensine completely inhibits mannose trimming from alpha1-antitrypsin null (Hong Kong) in mock transfected cells. Kifunensine inhibits alpha1-antitrypsin null (Hong Kong) degradation in cells co-transfected with the Golgi mannosidases
kifunensine
-
general membrane-permeable inhibitor of alpha-mannosidase activity
kifunensine
inhibits Golgi alpha1,2-mannosidase. Addition of kifunensine completely inhibits mannose trimming from alpha1-antitrypsin null (Hong Kong) in mock transfected cells. Kifunensine inhibits alpha1-antitrypsin null (Hong Kong)degradation in cells co-transfected with the Golgi mannosidases; inhibits Golgi alpha1,2-mannosidase. Addition of kifunensine completely inhibits mannose trimming from alpha1-antitrypsin null (Hong Kong) in mock transfected cells. Kifunensine inhibits alpha1-antitrypsin null (Hong Kong)degradation in cells co-transfected with the Golgi mannosidases
kifunensine
-
general membrane-permeable inhibitor of alpha-mannosidase activity, effect on the intracellular fate of endogenous mouse ER mannosidase I
lactacystin
-
irreversible inhibitor of multicatalytic proteasomes, only a minor effect on the disappearance of radiolabeled human ER mannosidase I
lactacystin
-
irreversible inhibitor of multicatalytic proteasomes, effect on the intracellular fate of endogenous mouse ER mannosidase I
leupeptin
-
lysosomal protease inhibitor, intracellular turnover of pulse-radiolabeled recombinant human ER mannosidase I is substantially inhibited
leupeptin
-
lysosomal protease inhibitor, effect on the intracellular fate of endogenous mouse ER mannosidase I
swainsonine
-
inhibits hydrolysis of 4-methylumbelliferyl-alpha-D-mannopyranoside
swainsonine
-
SW, inhibition of 4-methylumbelliferyl-alpha-D-mannopyranoside hydrolysis
Zn2+
-
50% reduction in alpha-mannosidase activity is observed after addition of 3 mM ZnCl2
additional information
-
staurosporine and genistein have an effect, tesing arrested intracellular turnover in response to selective inhibition of serine kinase activity
-
additional information
-
shift in migration is due to mannose trimming. Effects are not observed with the class II mannosidase inhibitor swainsonine
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
Edem1 activity in the fat body regulates insulin signalling and metabolic homeostasis in Drosophila.
Acquired Immunodeficiency Syndrome
The roles of apoptosis, autophagy and unfolded protein response in arbovirus, influenza virus, and HIV infections.
Carcinogenesis
ERManI Is a Target of miR-125b and Promotes Transformation Phenotypes in Hepatocellular Carcinoma (HCC).
Carcinoma
The roles of apoptosis, autophagy and unfolded protein response in arbovirus, influenza virus, and HIV infections.
Carcinoma, Hepatocellular
Alterations of EDEM1 functions enhance ATF6 pro-survival signaling.
Carcinoma, Hepatocellular
Elucidation of the molecular logic by which misfolded alpha 1-antitrypsin is preferentially selected for degradation.
Carcinoma, Hepatocellular
ERManI Is a Target of miR-125b and Promotes Transformation Phenotypes in Hepatocellular Carcinoma (HCC).
Carcinoma, Renal Cell
Inhibition of Cancer Cell Growth by GRP78 siRNA Lipoplex via Activation of Unfolded Protein Response.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Bi-allelic variants in the ER quality-control mannosidase gene EDEM3 cause a congenital disorder of glycosylation.
COVID-19
Increased susceptibility of human endothelial cells to infections by SARS-CoV-2 variants.
Dengue
Flavivirus infection activates the XBP1 pathway of the unfolded protein response to cope with endoplasmic reticulum stress.
Encephalitis, Japanese
Flavivirus infection activates the XBP1 pathway of the unfolded protein response to cope with endoplasmic reticulum stress.
Encephalitis, Japanese
Pathogenicity and virulence of Japanese encephalitis virus: Neuroinflammation and neuronal cell damage.
endoplasmic reticulum man9glcnac2 1,2-alpha-mannosidase deficiency
EDEM3 Modulates Plasma Triglyceride Level through Its Regulation of LRP1 Expression.
Hepatitis B
MicroRNA-581 promotes hepatitis B virus surface antigen expression by targeting Dicer and EDEM1.
Infections
Coronaviruses Hijack the LC3-I-positive EDEMosomes, ER-derived vesicles exporting short-lived ERAD regulators, for replication.
Infections
Flavivirus infection activates the XBP1 pathway of the unfolded protein response to cope with endoplasmic reticulum stress.
Liver Diseases
Single nucleotide polymorphism-mediated translational suppression of endoplasmic reticulum mannosidase I modifies the onset of end-stage liver disease in alpha1-antitrypsin deficiency.
Lymphoma
The roles of apoptosis, autophagy and unfolded protein response in arbovirus, influenza virus, and HIV infections.
Lymphoma, B-Cell
Pathogenicity and virulence of Japanese encephalitis virus: Neuroinflammation and neuronal cell damage.
Lymphoma, B-Cell
The roles of apoptosis, autophagy and unfolded protein response in arbovirus, influenza virus, and HIV infections.
Mania
Mannosidase IA is in Quality Control Vesicles and Participates in Glycoprotein Targeting to ERAD.
Melanoma
Context-dependent miR-204 and miR-211 affect the biological properties of amelanotic and melanotic melanoma cells.
Melanoma
The roles of apoptosis, autophagy and unfolded protein response in arbovirus, influenza virus, and HIV infections.
Melanoma
Tyrosinase Degradation Is Prevented when EDEM1 Lacks the Intrinsically Disordered Region.
Neoplasms
Edem1 activity in the fat body regulates insulin signalling and metabolic homeostasis in Drosophila.
Neoplasms
ERManI Is a Target of miR-125b and Promotes Transformation Phenotypes in Hepatocellular Carcinoma (HCC).
Neoplasms
Pathogenicity and virulence of Japanese encephalitis virus: Neuroinflammation and neuronal cell damage.
Neoplasms
Tyrosinase Degradation Is Prevented when EDEM1 Lacks the Intrinsically Disordered Region.
Neurodegenerative Diseases
The roles of apoptosis, autophagy and unfolded protein response in arbovirus, influenza virus, and HIV infections.
Parkinson Disease
Novel biomolecular information in rotenone-induced cellular model of Parkinson's disease.
Pulmonary Disease, Chronic Obstructive
Glutathione Peroxidase-1 Suppresses the Unfolded Protein Response upon Cigarette Smoke Exposure.
Severe Acute Respiratory Syndrome
Coronavirus interactions with the cellular autophagy machinery.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
4-methylumbelliferyl alpha-D-mannopyranoside
-
at pH 7.0 in 50 mM MES-Tris buffer and at 37°C
0.015 - 0.51
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
0.09
4-methylumbelliferyl-alpha-D-mannopyranoside
-
hydrolysis of the fluorogenic substrate follows hyperbolic kinetics
0.11
4-methylumbelliferyl-alpha-D-mannopyranoside
-
MUaMan, fluorogenic substrate. Vmax 36.2 nmol of 4-methylumbelliferone min-1 mg-1 of protein
0.015
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.5, mutant enzyme T688A
0.068
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 5.3, mutant enzyme E330Q
0.068
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 5.3, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q
0.09
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 7.1, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q
0.11
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 7.0, wild-type enzyme
0.11
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.8, pyridylamine-tagged Man9GlcNAc2, mutant enzyme D463N
0.11
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 7.1, pyridylamine-tagged Man9GlcNAc2, wild-type enzyme
0.12
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.8, mutant enzyme F659A
0.15
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.6, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q/E599Q
0.16
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.7, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E599Q
0.21
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.9, pyridylamine-tagged Man9GlcNAc2, mutant enzyme H524A
0.26
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.6, pyridylamine-tagged Man9GlcNAc2, mutant enzyme D463N/E599Q
0.33
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.5, mutant enzyme R461L
0.47
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.5, mutant enzyme R597A
0.51
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.5, mutant enzyme R461A
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000026 - 3.7
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
0.000026
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.7, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E599Q
0.000027
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.6, pyridylamine-tagged Man9GlcNAc2, mutant enzyme D463N/E599Q
0.00028
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.6, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q/E599Q
0.0046
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.8, pyridylamine-tagged Man9GlcNAc2, mutant enzyme D463N
0.018
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 7.1, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q
0.03
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.8, mutant enzyme F659A
0.06
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.5, mutant enzyme T688A
0.07
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.5, mutant enzyme R461L
0.084
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 5.3, mutant enzyme E330Q
0.084
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 5.3, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q
0.11
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.5, mutant enzyme R597A
0.6
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.5, mutant enzyme R461A
0.86
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 6.9, pyridylamine-tagged Man9GlcNAc2, mutant enzyme H524A
3.7
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 7.0, wild-type enzyme
3.7
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)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
37°C, pH 7.1, pyridylamine-tagged Man9GlcNAc2, wild-type enzyme
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
D-mannonolactam amidrazone
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0003
kifunensine
Arabidopsis thaliana
pH 6.0, 37°C, substrate methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
0.035
1-deoxymannojirimycin
Arabidopsis thaliana
pH 6.0, 37°C, substrate methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
0.12
1-deoxymannojirimycin
Sporothrix schenckii
-
at pH 7.0 in 50 mM MES-Tris buffer and at 37°C
0.2
1-deoxymannojirimycin
Candida albicans
-
inhibits hydrolysis of 4-methylumbelliferyl-alpha-D-mannopyranoside
0.23
1-deoxymannojirimycin
Candida albicans
-
inhibition of 4-methylumbelliferyl-alpha-D-mannopyranoside hydrolysis
0.47
swainsonine
Candida albicans
-
inhibition of 4-methylumbelliferyl-alpha-D-mannopyranoside hydrolysis
0.55
swainsonine
Candida albicans
-
inhibits hydrolysis of 4-methylumbelliferyl-alpha-D-mannopyranoside
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00003
-
purification of soluble alpha-mannosidase from CAI-4 strain, High-speed supernatant used to measure alpha-mannosidase activity
0.00008
-
purification of soluble alpha-mannosidase from CAI-4 strain, Sepharose CL6B
0.0002
-
mixed membrane fraction (MMF) of ATCC 26555 supernatant, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0005
0.0012
-
mixed membrane fraction (MMF) of CAI-4 and ATCC 26555 pellet, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0019
-
mixed membrane fraction (MMF) of ATCC 26555 pellet, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0021
-
purification of soluble alpha-mannosidase from CAI-4 strain, DEAE Bio-Gel A
0.0022
-
mixed membrane fraction (MMF) of CAI-4 and ATCC 26555 plus 1 mM pepstatin pellet, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0026
-
mixed membrane fraction (MMF) of CAI-4 pellet, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.003
-
purification of soluble alpha-mannosidase from CAI-4 strain, Sephadex G-25
0.0047
-
mixed membrane fraction (MMF) of CAI-4 and ATCC 26555 supernatant, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0057
-
purification of soluble alpha-mannosidase from CAI-4 strain, DEAE Bio-Gel A
0.0101
-
purification of soluble alpha-mannosidase from CAI-4 strain, Con A-Sepharose
0.0108
-
purification of soluble alpha-mannosidase from CAI-4 strain, Sephadex G-25
additional information
-
hydrolysis of the fluorogenic substrate 4-methylumbelliferyl-alpha-D-mannopyranoside follows hyperbolic kinetics and LineweaverBurk plots reveals Vmax values of 30.9 nmol of methylumbelliferone min-1 mg-1 of protein
0.0005
-
mixed membrane fraction (MMF) of CAI-4 and ATCC 26555 plus 1 mM pepstatin supernatant, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0005
-
mixed membrane fraction (MMF) of CAI-4 supernatant, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
6.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC26555, CAI4, SC5314, NGY152, HMY5, HMY6
Uniprot
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
catalytically active soluble domain, released from endogenous proteases
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
pericentriolar endoplasmic reticulum-derived quality control compartment
brenda
-
with the catalytic domain within the lumen of this compartment
brenda
-
with the catalytic domain within the lumen of this compartment
-
brenda
isoform MNS3 probably resides in the cis-Golgi. the C-terminal region of MNS3 is sufficient for proper subcellular targeting
brenda
presence of a 65000 Da membrane-bound isoform that is cleaved by protease Kex2 to soluble 52000 Da isoform E-I
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
endoplasmic reticulum mannosidase I knockdown does not affect binding of an endoplasmic reticulum-associated degradation substrate glycoprotein to EDEM1
physiological function
physiological function
-
endoplasmic reticulum mannosidase I activity is not required for association of H2a with EDEM1
physiological function
in the MNS3 single mutant, formation of aberrant N-glycans is observed. A triple mutant lacking mannosidases MNS1, MNS2, both EC 3.2.1.209, and MNS3 reveals the almost exclusive presence of Man9GlcNAc2 glycans. The MNS triple mutants display short, radially swollen roots and altered cell walls. Pharmacological inhibition of class I alpha-mannosidases in wild-type seedlings results in a similar root phenotype
physiological function
mutation results in the formation of aberrant N-glycans in the Mns3 single mutant. In the Mns1/Mns2/Mns3 triple mutant, Man(9)GlcNAc(2) glycans are almost exclusively present. The Mns triple mutants display short, radially swollen roots and altered cell walls
physiological function
overexpression of misfolded protein leads to increased expression of mannosidase ERManI. Expression of ER degradation-enhancing mannosidase-like protein EDEM1 results in stabilization of a higher molecular weight form of ERManI. Knockdown of ERManI, but not EDEM1, diminishes basal endoplasmic reticulum-associated degradation
physiological function
presence of the lectin hOS-9 enhances ER-associated degradation (ERAD) of misfolded glycoproteins, the enhancement depends on the N-glycan structures of the substrate. N-glycans lacking the terminal mannose from the C branch are recognized by hOS-9 and targeted for degradation
physiological function
presence of the lectin hOS-9 enhances ER-associated degradation (ERAD) of misfolded glycoproteins, the enhancement depends on the N-glycan structures of the substrate. N-glycans lacking the terminal mannose from the C branch are recognized by hOS-9 and targeted for degradation
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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). MNS1_ARATH
560
1
63532
Swiss-Prot
Mitochondrion (Reliability: 1)
MNS3_ARATH
624
1
69069
Swiss-Prot
other Location (Reliability: 2)
MNS1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
549
1
63057
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23000
27000
-
analytical electrophoresis of the purified preparation reveals two polypeptides
43000
52000
65000
75000
79000
-
Western blotting of cell lysates, transiently expressed recombinant human ER mannosidase I is absent from mock transfected cells but detected as a single immunoreactive 79 kDa band following transient expression
23000
-
analytical electrophoresis of the purified enzyme reveals two polypeptides of 52 and 23 kDa, 52000 Da polypeptide being responsible for enzyme activity as revealed by zymogram analysis
43000
-
Candida albicans CAI-4 mutant generating an active 43 kDa polypeptide. Zymogram analysis shows that the single proteolytic product of 43 kDa is able to hydrolyze the fluorogenic substrate and, this is not observed when proteolysis is blocked by pepstatin
43000
-
converting the 52 kDa alpha-mannosidase into a polypeptide of 43 kDa retaining full enzyme activity demonstrated in membranes of ATCC 26555, support a precursor-product relationship between soluble alpha1,2-mannosidase E-I (52 kDa) and alpha1,2-mannosidase E-II (43 kDa)
43000
-
purified alpha-mannosidase E-II remains unaltered after treatment with aspartyl protease and retains full activity on artificial substrate 4-methylumbelliferyl-alpha-D-mannopyranoside
52000
-
alpha1,2-mannosidase E-I. Analytical electrophoresis of the purified enzyme reveals two polypeptides of 52 and 23 kDa, 52000 Da polypeptide being responsible for enzyme activity as revealed by zymogram analysis
52000
-
analytical electrophoresis of the purified preparation reveals two polypeptides. Responsible for enzyme activity. Active on the fluorogenic substrate 4-methylumbelliferyl-alpha-D-mannopyranoside as revealed by zymogram analysis
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
additional information
-
contains two disulfide bonds and one free thiol group, soluble catalytic domain, recombinant enzyme
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-complex with an uncleaved thiodisaccharide substrate analog, hanging drop vapor diffusion method
docking studies, twelve of the 38 possible conformers of beta-D-mannopyranosyl-1C4 optimally docked in subsite-1 of the active site
structure reaveals a (alphaalpha)7-barrel in which an N?glycan from one molecule extends into the barrel of an adjacent molecule, interacting with the essential acidic residues and calcium ion
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D463N
D463N/E599Q
pH-optimum is 6.6 compared to 7.1 for wild-type enzyme, kcat/Km is 8.3fold lower than wild-type value
E220Q
-
the mutant contains a conserved acidic amino acid mutation that abolishes alpha1,2-mannosidase enzyme activity
E330Q
E330Q/E599Q
pH-optimum is 6.6 compared to 7.1 for wild-type enzyme, kcat/Km is 340000fold lower than wild-type value
E599Q
F659A
H524A
pH-optimum is 6.9 compared to 7.1 for wild-type enzyme, kcat/Km is 28.3fold lower than wild-type value
R334A
mutant enzyme is not detected in the culture medium, kcat/Km is 28.3fold lower than wild-type value
R461A
R461L
R597A
T688A
C468S
-
Km is 0.7 mM for (Man)9GlcNAc, same specificity as wild type
C471S
-
Km is 0.7 mM for (Man)9GlcNAc, same specificity as wild type
C485S
-
Km is 0.4 mM for (Man)9GlcNAc, same specificity as wild type
D121A
-
putative EF hand Ca2+ binding loop, no effect on Ca2+ binding
D121A/E132V
-
putative EF hand Ca2+ binding loop, no effect on Ca2+ binding
D121N
-
putative EF hand Ca2+ binding loop, no effect on Ca2+ binding
E132Q
E132V
-
putative EF hand Ca2+ binding loop, no effect on Ca2+ binding
R273L
instead of Man8GlcNAc, substrate is transformed to Man5GlcNAc
additional information
D463N
pH-optimum is 6.8 compared to 7.1 for wild-type enzyme, kcat/Km is 212500fold lower than wild-type value
E330Q
pH-optimum for mutant enzyme is 5.3 compared to 7.0 for wild-type enzyme. kcat/Km is 27.5fold lower than wild-type value. Enzyme possesses increased glycan binding affinity but compromised glycan hydrolysis
E330Q
pH-optimum is 5.3 compared to 7.1 for wild-type enzyme, kcat/Km is 809.5fold lower than wild-type value
E599Q
pH-optimum is 6.7 compared to 7.1 for wild-type enzyme, kcat/Km is 17895fold lower than wild-type value
F659A
pH-optimum for mutant enzyme is 6.8 compared to 7.0 for wild-type enzyme. kcat/Km is 132fold lower than wild-type value
R461A
pH-optimum for mutant enzyme is 6.5 compared to 7.0 for wild-type enzyme. kcat/Km is 27.5fold lower than wild-type value
R461L
pH-optimum for mutant enzyme is 6.5 compared to 7.0 for wild-type enzyme, mutant enzyme exhibits the ability to readily hydrolyze Man9GlcNAc2 to Man6GlcNAc2. kcat/Km is 157fold lower than wild-type value
R597A
pH-optimum for mutant enzyme is 6.5 compared to 7.0 for wild-type enzyme. kcat/Km is 143fold lower than wild-type value
T688A
pH-optimum for mutant enzyme is 6.5 compared to 7.0 for wild-type enzyme. kcat/Km is 8.25fold lower than wild-type value
E132Q
-
putative EF hand Ca2+ binding loop, no effect on Ca2+ binding
additional information
-
genetic-engineered removal of the amino-terminal cytoplasmic tail. Removal of the tail does not influence the remaining structure of the molecule, including the original transmembrane domain, noncleavable ER sorting signal, and proposed stem and catalytic domains. Synthesized with slightly different molecular weights, its absence did not diminish the efficiency of protein translation. Investigation of involvement of the tail by fluorescent fusion proteins
additional information
-
the missense mutations G1418A (DeltaW473), G1189A (E397K) and C1000T (R334C) segregates with nonsyndromic autosomal-recessive intellectual disability
additional information
-
knockdown experiments show that ERManI is indeed involved in mannose trimming to Man6-5 leading to endoplasmic reticulum-associated degradation
additional information
-
deletion of N-terminal 174 amino acids, marginal effects on catalytic properties
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by conventional methods of protein isolation and affinity chromatography in Concanavalin A-Sepharose 4B. Alpha-mannosidase E-I is purified by a fungal aspartyl protease
-
ion exchange chromatography, used to measure protein and enzyme activity, Sepharose CL6B, DEAE Bio-Gel A, Sephadex G-25, DEAE Bio-Gel A, Con A-Sepharose, Sephadex G-25
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
expression in Pichia pastoris as secreted glycoprotein, beginning at residue 34
overexpressed in HEK-293 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
homozygosity for the minor A allele rs4567(A), but not rs4567(G), suppresses ERManI translation under endoplasmic reticulum stress conditions
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ziegler, F.D.; Trimble, R.B.
Glycoprotein biosynthesis in yeast: purification and characterization of the endoplasmatic reticulum Man9 processing alpha-mannosidase
Glycobiology
1
605-614
1991
Saccharomyces cerevisiae
brenda
Jelinek-Kelly, S.; Herscovics, A.
Glycoprotein biosynthesis in Saccharomyces cerevisiae. Purification of the alpha-mannosidase which removes one specific mannose residue from Man9GlcNAc
J. Biol. Chem.
263
14757-14763
1988
Saccharomyces cerevisiae
brenda
Lipari, F.; Herscovics, A.
Production, purification and characterization of recombinant yeast processing alpha 1,2-mannosidase
Glycobiology
4
697-702
1994
Saccharomyces cerevisiae
brenda
Lipari, F.; Herscovics, A.
Calcium Binding to the Class I alpha-1,2-mannosidase from Saccharomyces cerevisiae occurs outside the EF hand motif
Biochemistry
38
1111-1118
1999
Saccharomyces cerevisiae
brenda
Romero, P.A.; Vallee, F.; Howell, P.L.; Herscovics, A.
Mutation of Arg273 to Leu alters the specificity of the yeast N-glycan processing class I alpha-1,2-mannosidase
J. Biol. Chem.
275
11071-11074
2000
Saccharomyces cerevisiae (P32906), Saccharomyces cerevisiae
brenda
Gonzalez, D.S.; Karaveg, K.; Vandersall-Nairn, A.S.; Lal, A.; Moremen, K.W.
Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis
J. Biol. Chem.
274
21375-21386
1999
Homo sapiens (Q9UKM7), Homo sapiens
brenda
Lipari, F.; Herscovics, A.
Role of the cysteine residues in the alpha-1,2-mannosidase involved in N-glycan biosynthesis in Saccharomyces cerevisiae. The conserved Cys340 and Cys385 residues form an essential disulfide bond
J. Biol. Chem.
271
27615-27622
1996
Saccharomyces cerevisiae
brenda
Lobsanov, Y.D.; Vallee, F.; Imberty, A.; Yoshida, T.; Yip, P.; Herscovics, A.; Howell, P.L.
Structure of Penicillium citrinum alpha-1,2-mannosidase reveals the basis for differences in specificity of the endoplasmic reticulum and golgi class I enzymes
J. Biol. Chem.
277
5620-5630
2002
Saccharomyces cerevisiae (P32906), Saccharomyces cerevisiae, Homo sapiens (Q9UKM7), Homo sapiens
brenda
Hamagashira, N.; Oku, H.; Mega, T.; Hase, S.
Purification and characterization of hen oviduct alpha 1,2-mannosidase
J. Biochem.
119
998-1003
1996
Gallus gallus
brenda
Yoshida, T.; Kato, Y.; Asada, Y.; Nakajima, T.
Filamentous fungus Aspergillus oryzae has two types of alpha-1,2-mannosidases, one of which is a microsomal enzyme that removes a single mannose residue from Man9GlcNAc2
Glycoconj. J.
17
745-748
2001
Aspergillus oryzae
brenda
Dole, K.; Lipari, F.; Herscovics, A.; Howell, P.L.
Crystallization and preliminary X-ray analysis of the class 1 alpha 1,2-mannosidase from Saccharomyces cerevisiae
J. Struct. Biol.
120
69-72
1997
Saccharomyces cerevisiae
brenda
Bieberich E.;Treml K.;Volker C.;Rolfs A.;Kalz-Fuller B.;Bause E
Man9-mannosidase from pig liver is a type-II membrane protein that resides in the endoplasmic reticulum. cDNA cloning and expression of the enzyme in COS 1 cells
Eur. J. Biochem.
246
681-689
1997
Sus scrofa
brenda
Karaveg, K.; Siriwardena, A.; Tempel, W.; Liu, Z.; Glushka, J.; Wang, B.; Moremen, K.W.
Mechanism of class 1 (glycosylhydrolase family 47) alpha-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control
J. Biol. Chem.
280
16197-16207
2005
Homo sapiens (Q9UKM7)
brenda
Karaveg, K.; Moremen, K.W.
Energetics of substrate binding and catalysis by class 1 (glycosylhydrolase family 47) alpha-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control
J. Biol. Chem.
280
29837-29848
2005
Homo sapiens (Q9UKM7)
brenda
Mora-Montes, H.M.; Lopez-Romero, E.; Zinker, S.; Ponce-Noyola, P.; Flores-Carreon, A.
Conversion of alpha1,2-mannosidase E-I from Candida albicans to alpha1,2-mannosidase E-II by limited proteolysis
Antonie van Leeuwenhoek
93
61-69
2008
Candida albicans
brenda
Hosokawa, N.; You, Z.; Tremblay, L.O.; Nagata, K.; Herscovics, A.
Stimulation of ERAD of misfolded null Hong Kong alpha1-antitrypsin by Golgi alpha1,2-mannosidases
Biochem. Biophys. Res. Commun.
362
626-632
2007
Homo sapiens, Mus musculus (P39098), Mus musculus (P45700)
brenda
Mulakala, C.; Nerinckx, W.; Reilly, P.J.
The fate of beta-D-mannopyranose after its formation by endoplasmic reticulum alpha-(1-->2)-mannosidase I catalysis
Carbohydr. Res.
342
163-169
2007
Homo sapiens, Saccharomyces cerevisiae (P32906), Saccharomyces cerevisiae
brenda
Mora-Montes, H.M.; Lopez-Romero, E.; Zinker, S.; Ponce-Noyola, P.; Flores-Carreon, A.
Purification of soluble alpha1,2-mannosidase from Candida albicans CAI-4
FEMS Microbiol. Lett.
256
50-56
2006
Candida albicans
brenda
Wu, Y.; Termine, D.J.; Swulius, M.T.; Moremen, K.W.; Sifers, R.N.
Human endoplasmic reticulum mannosidase I is subject to regulated proteolysis
J. Biol. Chem.
282
4841-4849
2007
Homo sapiens, Mus musculus
brenda
Mast, S.W.; Moremen, K.W.
Family 47 alpha-mannosidases in N-glycan processing
Methods Enzymol.
415
31-46
2006
Saccharomyces cerevisiae (P32906), Homo sapiens (Q9UKM7)
brenda
Avezov, E.; Frenkel, Z.; Ehrlich, M.; Herscovics, A.; Lederkremer, G.Z.
Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation
Mol. Biol. Cell
19
216-225
2008
Mus musculus
brenda
Cantu, D.; Nerinckx, W.; Reilly, P.J.
Theory and computation show that Asp463 is the catalytic proton donor in human endoplasmic reticulum alpha-(1-->2)-mannosidase I
Carbohydr. Res.
343
2235-2242
2008
Homo sapiens (Q9UKM7), Homo sapiens
brenda
Mora-Montes, H.M.; Lopez-Romero, E.; Zinker, S.; Ponce-Noyola, P.; Flores-Carreon, A.
Heterologous expression and biochemical characterization of an alpha1,2-mannosidase encoded by the Candida albicans MNS1 gene
Mem. Inst. Oswaldo Cruz
103
724-730
2008
Candida albicans (Q8J0Q0), Candida albicans
brenda
Mora-Montes, H.M.; Bader, O.; Lopez-Romero, E.; Zinker, S.; Ponce-Noyola, P.; Hube, B.; Gow, N.A.; Flores-Carreon, A.
Kex2 protease converts the endoplasmic reticulum alpha1,2-mannosidase of Candida albicans into a soluble cytosolic form
Microbiology
154
3782-3794
2008
Candida albicans (Q8J0Q0), Candida albicans, Candida albicans ATCC 26555 (Q8J0Q0)
brenda
Hosokawa, N.; Tremblay, L.O.; Sleno, B.; Kamiya, Y.; Wada, I.; Nagata, K.; Kato, K.; Herscovics, A.
EDEM1 accelerates the trimming of alpha1,2-linked mannose on the C branch of N-glycans
Glycobiology
20
567-575
2010
Homo sapiens
brenda
Pan, S.; Huang, L.; McPherson, J.; Muzny, D.; Rouhani, F.; Brantly, M.; Gibbs, R.; Sifers, R.N.
Single nucleotide polymorphism-mediated translational suppression of endoplasmic reticulum mannosidase I modifies the onset of end-stage liver disease in alpha1-antitrypsin deficiency
Hepatology
50
275-281
2009
Homo sapiens
brenda
Rafiq, M.; Kuss, A.; Puettmann, L.; Noor, A.; Ramiah, A.; Ali, G.; Hu, H.; Kerio, N.; Xiang, Y.; Garshasbi, M.; et al
Mutations in the alpha 1,2-mannosidase gene, MAN1B1, cause autosomal-recessive intellectual disability
Am. J. Hum. Genet.
89
176-182
2011
Homo sapiens
brenda
Groisman, B.; Shenkman, M.; Ron, E.; Lederkremer, G.Z.
Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps
J. Biol. Chem.
286
1292-1300
2011
Homo sapiens
brenda
Mora-Montes, H.M.; Robledo-Ortiz, C.I.; Gonzalez-Sanchez, L.C.; Lopez-Esparza, A.; Lopez-Romero, E.; Flores-Carreon, A.
Purification and biochemical characterisation of endoplasmic reticulum alpha1,2-mannosidase from Sporothrix schenckii
Mem. Inst. Oswaldo Cruz
105
79-85
2010
Sporothrix schenckii, Sporothrix schenckii EH206
brenda
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)
brenda
Vallee, F.; Lipari, F.; Yip, P.; Sleno, B.; Herscovics, A.; Howell, P.L.
Crystal structure of a class I alpha1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality control
EMBO J.
19
581-588
2000
Saccharomyces cerevisiae (P32906), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P32906)
brenda
Lal, A.; Pang, P.; Kalelkar, S.; Romero, P.A.; Herscovics, A.; Moremen, K.W.
Substrate specificities of recombinant murine Golgi alpha-1,2-mannosidases IA and IB and comparison with endoplasmic reticulum and Golgi processing alpha-1,2-mannosidases
Glycobiology
8
981-995
1998
Rattus norvegicus
brenda
Pan, Y.T.; Kaushal, G.P.; Papandreou, G.; Ganem, B.; Elbein, A.D.
D-Mannonolactam amidrazone. A new mannosidase inhibitor that also inhibits the endoplasmic reticulum or cytoplasmic alpha-mannosidase
J. Biol. Chem.
267
8313-8318
1992
Rattus norvegicus
brenda
Hosokawa, N.; Kamiya, Y.; Kamiya, D.; Kato, K.; Nagata, K.
Human OS-9, a lectin required for glycoprotein ERAD, recognizes mannose-trimmed N-glycans
J. Biol. Chem.
284
17061-17068
2009
Mus musculus (Q2HXL6), Homo sapiens (Q9UKM7), Homo sapiens
brenda
Termine, D.J.; Moremen, K.W.; Sifers, R.N.
The mammalian UPR boosts glycoprotein ERAD by suppressing the proteolytic downregulation of ER mannosidase I
J. Cell Sci.
122
976-984
2009
Homo sapiens (Q9UKM7)
brenda
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