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Information on EC 3.2.1.114 - mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase
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EC Tree
3.2.1.114 mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidaseIUBMB Comments
The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. It removes two mannosyl residues, one linked by alpha1,3 linkage, and the other linked by alpha1,6 linkage, both of which are removed by the same catalytic site. The enzyme is sensitive to swainsonine.
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Word Map
- 3.2.1.114
- glycoprotein
- swainsonine
-
n-linked
- brefeldin
- n-glycans
-
endoglycosidase
- castanospermine
-
asparagine-linked
-
complex-type
- alpha-mannosidases
-
high-mannose
-
indolizidine
-
hybrid-type
-
locoweed
- 1-deoxymannojirimycin
- mannostatins
- medicine
- kifunensine
- giantin
- glcnacman5glcnac2
-
locoism
- oxytropis
- beta-cop
-
swainsonine-treated
- 1-deoxynojirimycin
- man5glcnac
-
high-mannose-type
-
intra-golgi
- drug development
- biotechnology
- pharmacology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
1,3(1,6)-alpha-D-mannosidase, 1,6-alpha-D-mannosidase, Afams1, alpha-1,3 mannosidase, alpha-1,3-mannosidase, alpha-D-mannosidase II, alpha-mannosidase, alpha-mannosidase II, alpha-mannosidase III, alpha-mannosidase IIx, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Afams1
alpha-D-mannosidase II
-
-
-
-
alpha-mannosidase
alpha-mannosidase II
alpha-mannosidase III
-
-
-
-
alpha-mannosidase IIx
alpha1-3,6-mannosidase
-
-
-
-
class II alpha-mannosidase
class IIC alpha-mannosidase
dGMII
exo-1,3-1,6-alpha-mannosidase
-
-
-
-
GlcNAc transferase I-dependent alpha1,3[alpha1,6]mannosidase
-
-
-
-
GmII
Golgi alpha-mannosidase II
Golgi mannosidase IIx
Man II
MAN IIx
-
-
-
-
MAN2A1
ManIII
-
-
-
-
mannosidase II
mannosidase, exo-1,3-1,6-alpha-
-
-
-
-
mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase
-
-
-
-
additional information
alpha-mannosidase II
-
-
-
-
alpha-mannosidase IIx
-
homolog to alpha-mannosidase II with different substrate specificity
GmII
-
-
Golgi alpha-mannosidase II
-
-
-
-
Golgi alpha-mannosidase II
-
-
Golgi mannosidase IIx
-
close homolog to Golgi mannosidase II with different substrate specificity
Golgi mannosidase IIx
-
close homolog to Golgi mannosidase II with different substrate specificity
Man II
-
-
-
-
mannosidase II
-
-
-
-
additional information
-
member of glycosyl hydrolase family 38
additional information
-
Bt3991 belongs to the glycosyl hydrolase family 92, GH92
additional information
the enzyme belongs to the family GH38 of alpha-mannosidases
additional information
-
the enzyme belongs to the glycoside hydrolase family 38
additional information
-
not identical with aryl-alpha-mannosidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Man5GlcNAc3-[protein] + 2 H2O = Man3GlcNAc3-[protein] + 2 alpha-D-mannopyranose
-
-
-
-
Man5GlcNAc3-[protein] + 2 H2O = Man3GlcNAc3-[protein] + 2 alpha-D-mannopyranose
catalytic mechanism
-
Man5GlcNAc3-[protein] + 2 H2O = Man3GlcNAc3-[protein] + 2 alpha-D-mannopyranose
the conformational change of the bound mannoside to a high-energy B2,5 conformation is facilitated by steric hindrance from, and the formation of strong hydrogen bonds to, resiude D204
-
Man5GlcNAc3-[protein] + 2 H2O = Man3GlcNAc3-[protein] + 2 alpha-D-mannopyranose
reaction mechanism via glycosyl-enzyme intermediate, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of O-glycosyl bond
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(1->3)-(1->6)-mannosyl-oligosaccharide alpha-D-mannohydrolase (configuration-retaining)
The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. It removes two mannosyl residues, one linked by alpha1,3 linkage, and the other linked by alpha1,6 linkage, both of which are removed by the same catalytic site. The enzyme is sensitive to swainsonine.
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CAS REGISTRY NUMBER
COMMENTARY
349553-33-9
alpha-mannosidase III
82047-77-6
alpha-mannosidase II
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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
(Man)9GlcNAc + H2O
(Man)5GlcNAc + D-mannose
-
hydrolysis to (Man)5GlcNAc in the presence of Fe2+, Co2+, and Mn2+. Without activating cations the main reaction product is (Man)8GlcNAc
-
-
?
2,4-dinitrophenyl alpha-D-mannopyranoside + H2O
2,4-dinitrophenol + alpha-D-mannopyranose
-
-
-
?
2,4-dinitrophenyl-alpha-D-mannopyranoside + H2O
2,4-dinitrophenol + D-mannose
-
-
-
-
?
2,5-dinitrophenyl-alpha-D-mannopyranoside + H2O
2,4-dinitrophenol + D-mannose
-
-
-
?
2,5-dinitrophenyl-alpha-D-mannopyranoside + H2O
2,5-dinitrophenol + alpha-D-mannose
pH 5.6, room temperature
-
-
?
2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1->2)-alpha-D-mannopyranosyl-(1->3)-[alpha-D-mannopyranosyl-(1->3)-alpha-D-mannopyranosyl-(1->6)]-beta-D-mannopyranosyl-(1->4)-2-(acetylamino)-2-deoxy-alpha-D-glucopyranose + H2O
2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1->2)-alpha-D-mannopyranosyl-(1->3)-[alpha-D-mannopyranosyl-(1->6)]-beta-D-mannopyranosyl-(1->4)-2-(acetylamino)-2-deoxy-alpha-D-glucopyranose + D-mannose
-
-
-
-
ir
2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(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-alpha-D-glucopyranose + H2O
2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1->2)-alpha-D-mannopyranosyl-(1->3)-[alpha-D-mannopyranosyl-(1->3)-alpha-D-mannopyranosyl-(1->6)]-beta-D-mannopyranosyl-(1->4)-2-(acetylamino)-2-deoxy-alpha-D-glucopyranose + D-mannose
-
-
-
-
ir
2-deoxy-2-fluoro-alpha-D-mannosyl fluoride
?
-
wild-type and D341N mutant GMII, acts as very slow substrate of the mutant enzyme with a rate-limiting deglycosylation step
-
-
?
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose + H2O
2 alpha-D-mannopyranose
-
Bt3991 displays particularly high activity against alpha-1,3-mannobiose
-
-
?
4-methyl-umbelliferyl-alpha-D-mannopyranoside + H2O
4-methyl-umbelliferone + alpha-D-mannopyranose
-
30 min, 37°C
-
-
?
4-methylumbelliferyl alpha-D-mannopyranoside + H2O
4-methylumbelliferol + alpha-D-mannopyranose
4-methylumbelliferyl alpha-D-mannoside + H2O
4-methylumbelliferol + alpha-D-mannose
-
-
-
-
?
4-nitrophenyl alpha-D-mannopyranoside + H2O
4-nitrophenol + D-mannopyranose
-
-
-
?
4-nitrophenyl-alpha-D-mannopyranoside + H2O
4-nitrophenol + alpha-D-mannopyranose
-
30 min, 37°C
-
-
?
4-nitrophenyl-alpha-D-mannopyranoside + H2O
4-nitrophenol + alpha-D-mannose
30 min, 20°C
-
-
?
4-nitrophenyl-alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
-
?
5-fluoro-beta-L-gulosyl fluoride + H2O
?
-
acts as slow substrate with a rate-limiting deglycosylation step, wild-type and D341N mutant GMII
-
-
?
D-Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + H2O
?
-
NaBH4 reduced, poor substrate
-
-
?
D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-Asn + H2O
D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-Asn + alpha-D-mannose
-
i.e. glycopeptide III, derived from ovalbumin, no hydrolysis of the innermost alpha-1,6-linked or the alpha-1,2-linked mannose
i.e. glycopeptide II
?
D-Manalpha(1-6)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
D-Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
NaBH4 reduced, at lower rate than Manalpha(1-3)Manbeta(1-4)GlcNAc hydrolysis
NaBH4 reduced
?
GlcNAcbeta(1-2)Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
?
-
NaBH4 reduced, hydrolysis at equal rate as Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc, galactosyl and sialyl-galactosyl derivatives are substrates, too
-
-
?
GlcNAcbeta(1-6)(GlcNAcbeta(1-2))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
?
-
NaBH4 reduced, rate at 50% of Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc hydrolysis
-
-
?
high mannose chains of thyroglobulin and phytohemagglutinin-P + H2O
? + D-mannose
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thyroglobulin: 70% of alpha1,2-mannose residues accessible
-
-
-
Manalpha(1-3)Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside + H2O
Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside + alpha-D-mannose
-
-
-
-
?
Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside + H2O
Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside + alpha-D-mannose
-
-
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))(Xylbeta(1-4))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + H2O
Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))(Xylbeta(1-4))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + alpha-D-mannose
-
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + H2O
Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + alpha-D-mannose
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside + H2O
Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside + alpha-D-mannose
-
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 H2O
Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)4(GlcNAc)2 + (Man)3(GlcNAc)2 + D-mannose
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-6)(Manalpha(1-3))D-Manalpha(1-6)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
NaBH4 reduced
NaBH4 reduced
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside + H2O
Manalpha(1-3)Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside + alpha-D-mannose
-
-
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-6)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside + H2O
Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-pyridylaminoside + alpha-D-mannose
-
-
-
-
?
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 H2O
Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-Asn + H2O
Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-Asn + alpha-D-mannose
-
processing of asparagine-linked oligosaccharides by alpha-D-mannosidase dependent on the prior action of UDP-GlcNAc:alpha-D-mannoside beta2-N-acetylglucosaminyltransferase I, removes 2 mannosyl residues, via GlcNAc(Man)4(GlcNAc)2Asn
-
?
methyl-2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside + H2O
? + D-mannose
-
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
-
-
-
-
?
pyridylaminated D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
pyridylaminated D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
2,4-dinitrophenyl alpha-D-mannoside + H2O
2,4-dinitrophenol + alpha-D-mannose
-
-
-
?
2,4-dinitrophenyl alpha-D-mannoside + H2O
2,4-dinitrophenol + alpha-D-mannose
-
-
-
-
?
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose + H2O
alpha-D-mannopyranose
-
-
-
-
?
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose + H2O
alpha-D-mannopyranose
the enzyme is only active with the alpha-1,3-linked disaccharide
-
-
?
4-methylumbelliferyl alpha-D-mannopyranoside + H2O
4-methylumbelliferol + alpha-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl alpha-D-mannopyranoside + H2O
4-methylumbelliferol + alpha-D-mannopyranose
-
-
-
?
4-methylumbelliferyl alpha-D-mannoside + H2O
4-methylumbelliferone + alpha-D-mannose
-
-
-
-
?
4-methylumbelliferyl alpha-D-mannoside + H2O
4-methylumbelliferone + alpha-D-mannose
-
-
-
-
-
4-methylumbelliferyl alpha-D-mannoside + H2O
4-methylumbelliferone + alpha-D-mannose
-
-
-
-
?
4-methylumbelliferyl alpha-D-mannoside + H2O
4-methylumbelliferone + alpha-D-mannose
-
catalytic domain of alpha-mannosidase IIx
-
-
?
4-methylumbelliferyl alpha-D-mannoside + H2O
4-methylumbelliferone + alpha-D-mannose
-
-
-
-
?
4-methylumbelliferyl alpha-D-mannoside + H2O
4-methylumbelliferone + alpha-D-mannose
-
-
-
?
4-methylumbelliferyl alpha-D-mannoside + H2O
4-methylumbelliferone + alpha-D-mannose
-
-
-
-
?
4-methylumbelliferyl alpha-D-mannoside + H2O
4-methylumbelliferone + alpha-D-mannose
-
-
-
-
?
4-nitrophenyl alpha-D-mannopyranoside + H2O
4-nitrophenol + alpha-D-mannopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-mannopyranoside + H2O
4-nitrophenol + alpha-D-mannopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-mannopyranoside + H2O
4-nitrophenol + alpha-D-mannopyranose
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
alpha-mannosidase IIx
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
rat
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
rate at 23.5% of GlcNAc(Man)5GlcNAc hydrolysis
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
alpha-mannosidase III
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
-
?
D-Manalpha(1-3)Manbeta(1-4)GlcNAc + H2O
D-Manbeta(1-4)GlcNAc + alpha-D-mannose
-
NaBH4 reduced, good substrate
-
-
?
D-Manalpha(1-3)Manbeta(1-4)GlcNAc + H2O
D-Manbeta(1-4)GlcNAc + alpha-D-mannose
-
NaBH4 reduced, good substrate
NaBH4 reduced
?
D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
-
-
?
D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
alpha-mannosidase II
-
?
D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
-
-
?
D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
-
-
?
D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
-
-
?
GlcNAc(Man)5GlcNAc + 2 H2O
GlcNAc(Man)3GlcNAc + 2 alpha-D-mannose
-
-
-
-
?
GlcNAc(Man)5GlcNAc + 2 H2O
GlcNAc(Man)3GlcNAc + 2 alpha-D-mannose
-
-
-
-
?
GlcNAc(Man)5GlcNAc + 2 H2O
GlcNAc(Man)3GlcNAc + 2 alpha-D-mannose
-
-
-
?
GlcNAc(Man)5GlcNAc + 2 H2O
GlcNAc(Man)3GlcNAc + 2 alpha-D-mannose
-
preferred substrate
-
-
?
GlcNAc(Man)5GlcNAc + 2 H2O
GlcNAc(Man)3GlcNAc + 2 alpha-D-mannose
-
removes the exposed alpha-1,3- and alpha-1,6-mannosyl residues
-
?
GlcNAc(Man)5GlcNAc + 2 H2O
GlcNAc(Man)3GlcNAc + 2 alpha-D-mannose
-
natural substrate, involved in the processing of N-linked oligosaccharides
-
?
GlcNAc(Man)5GlcNAc + 2 H2O
GlcNAc(Man)3GlcNAc + 2 alpha-D-mannose
-
-
-
-
?
GlcNAc(Man)5GlcNAc + 2 H2O
GlcNAc(Man)3GlcNAc + 2 alpha-D-mannose
-
strict substrate specificity
final product, via GlcNAc(Man)4GlcNAc
?
GlcNAc(Man)5GlcNAc + 2 H2O
GlcNAc(Man)3GlcNAc + 2 alpha-D-mannose
-
excellent substrate, removes the alpha-1,3- and alpha-1,6-mannosyl residues with preference for the alpha-1,6-linkage
final product, via GlcNAc(Man)4GlcNAc, product structure: GlcNAcManalpha(1-3)(Manalpha(1-6))ManbetaGlcNAc
?
GlcNAc(Man)5GlcNAc + 2 H2O
GlcNAc(Man)3GlcNAc + 2 alpha-D-mannose
-
natural substrate, involved in the processing of N-linked oligosaccharides
-
-
?
GlcNAc(Man)5GlcNAc2 + H2O
GlcNAc(Man)3GlcNAc2 + D-mannose
-
alpha-mannosidase IIx protein
-
-
?
Man5GlcNAc2 + H2O
Man3GlcNAc2 + 2 alpha-D-mannopyranose
-
the alpha-1,3-mannosidase Bt3991, while unable to hydrolyze Man9GlcNAc2, converts Man5GlcNAc2 into Man3GlcNAc2 hydrolyzing the distal alpha-1,6-mannosidic linkage in high-mannose N-glycans. The alpha-1,3-mannosidic linkages in N-glycans are available to the enzyme once the terminal alpha-1,2-linked mannosyl residues are removed
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + H2O
Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + alpha-D-mannose
physiological substrate, conversion by sequential removal of two alpha1,6-linked and alpha1,3-linked mannose residues from the alpha-1,6-branch of the substrate
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + H2O
Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + alpha-D-mannose
conversion by sequential removal of two alpha1,6-linked and alpha1,3-linked mannose residues from the alpha-1,6-branch of the substrate
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 H2O
Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
-
recombinant alpha-mannosidase IIx, expressed in CHO cells, hydrolyzes 2 peripheral Manapha(1-6) and Manalpha(1-3) residues
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 H2O
Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
-
alpha-mannosidase IIx, M6Gn2 is the primary target in vivo, integral part of N-glycan biosynthesis
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)4(GlcNAc)2 + (Man)3(GlcNAc)2 + D-mannose
-
i.e. Manalpha(1-2)Manalpha(1-2)Manalpha(1-3) (Manalpha(1-6))ManbetaGlcNAc-betaGlcNAc
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)4(GlcNAc)2 + (Man)3(GlcNAc)2 + D-mannose
-
i.e. Manalpha(1-2)Manalpha(1-2)Manalpha(1-3) (Manalpha(1-6))ManbetaGlcNAc-betaGlcNAc
-
?
Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-6)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
-
-
-
-
Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-6)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
NaBH4 reduced, cleaves the Manalpha(1-6)Man linkage only after its Manalpha(1-3) residue is removed
NaBH4 reduced, no product: Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc
?
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 H2O
Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
-
N-glycosylation pathway
-
?
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 H2O
Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
-
alpha-mannosidase II
-
?
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 H2O
Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
-
alpha-mannosidase II, biosynthesis of N-glycans
-
?
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 H2O
Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
-
acts after GlcNAc transferase I to remove the alpha-1,3- and alpha-1,6-linked mannose residue
-
?
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 H2O
Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
-
non-reduced and NaBH4 reduced substrate, removes the alpha-1,3- and alpha-1,6-mannosyl residues with preference for the alpha-1,6-linked mannose residue on the alpha-1,6-linked mannose arm, via GlcNAc(Man)4(GlcNAc)2
-
-
-
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 H2O
Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
-
involved in N-glycan maturation, acts after GlcNAc transferase I to remove 2 mannose residues to form GlcNAc(Man)3(GlcNAc)2 prior to extension into complex N-glycans
-
?
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 H2O
Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
-
-
-
?
pyridylaminated (Man)5(GlcNAc)2 + H2O
pyridylaminated (Man)3(GlcNAc)2 + alpha-D-mannose
-
via a (Man)4(GlcNAc)2 intermediate
-
?
pyridylaminated (Man)5(GlcNAc)2 + H2O
pyridylaminated (Man)3(GlcNAc)2 + alpha-D-mannose
-
alpha-mannosidase III
-
?
pyridylaminated (Man)5(GlcNAc)2 + H2O
pyridylaminated (Man)3(GlcNAc)2 + alpha-D-mannose
-
alpha-mannosidase III
-
?
pyridylaminated D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
pyridylaminated D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
via the intermediate product GlcNAc(Man)4(GlcNAc)2, the alpha-1,6-linked mannosyl residue is removed first, then the 1,3-linked
-
?
pyridylaminated D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
pyridylaminated D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
dependent on the prior action of N-acetylglucosaminyl transferase I on (Man)5(GlcNAc)2
-
?
pyridylaminated D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
pyridylaminated D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
via the intermediate product GlcNAc(Man)4(GlcNAc)2, the alpha-1,6-linked mannosyl residue is removed first, then the 1,3-linked
-
?
pyridylaminated D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
pyridylaminated D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
dependent on the prior action of N-acetylglucosaminyl transferase I on (Man)5(GlcNAc)2
-
?
pyridylaminated D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
pyridylaminated D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
-
-
?
pyridylaminated D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
pyridylaminated D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
-
-
?
pyridylaminated D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
pyridylaminated D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
-
-
?
pyridylaminated D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
pyridylaminated D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
-
-
?
pyridylaminated D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
pyridylaminated D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
via the intermediate product GlcNAc(Man)4(GlcNAc)2, the alpha-1,6-linked mannosyl residue is removed first, then the 1,3-linked
-
?
pyridylaminated D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
pyridylaminated D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
via the intermediate product GlcNAc(Man)4(GlcNAc)2, the alpha-1,6-linked mannosyl residue is removed first, then the 1,3-linked
-
?
additional information
?
-
-
Golgi alpha-mannosidase II is a key enzyme in the formation of complex N-glycans in plants
-
-
-
additional information
?
-
Golgi alpha-mannosidase II is a key enzyme in the formation of complex N-glycans in plants
-
-
-
additional information
?
-
-
not: D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-4))[GlcNAcbeta(1-4)(GlcNAcbeta(1-2))Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc, GlcNAcbeta(1-2)Manalpha(1-3)(Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc, GlcNAcbeta(1-4)Manalpha(1-3)(Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc, all sodium borate reduced
-
-
-
additional information
?
-
-
not: Manalpha(1-6)(R-Manalpha(1-3))Manbeta(1-4)GlcNAc
-
-
-
additional information
?
-
-
substrate specificity, hydrolysis mechanism of branched oligosaccharides
-
-
-
additional information
?
-
-
asparagine-linked glycoprotein biosynthesis
-
-
-
additional information
?
-
-
enzyme/active site structure and substrate binding, catalytic mechanism
-
-
-
additional information
?
-
-
asparagine-linked glycoprotein biosynthesis
-
-
-
additional information
?
-
-
about 80-fold preference of isoform GMII for the cleavage of substrates containing a nonreducing beta-(1,2)-linked GlcNAc group
-
-
-
additional information
?
-
-
GMII is involved in the creation of glycoproteins that contain complex carbohydrates. It is responsible for the formation of the core trimannose structure to which all complex carbohydrates are appended. It catalyses the hydrolysis of an alpha(1,6)- and an alpha(1,3)-linked mannose from GlcNAc-Man5-GlcNAc2 to form GlcNAc-Man3-GlcNAc2-Asn-X
-
-
-
additional information
?
-
-
the cleavage mechanism involves formation of a covalent glycosyl-enzyme intermediate and results in net retention of configuration
-
-
-
additional information
?
-
-
Co2+ regulates the substrate specificity, overview
-
-
-
additional information
?
-
-
in vitro hydrolysis of high-mannose type N-glycans, removal of terminal alpha-1,2-mannose residues, substrate specificity and isomeric substrate/product structures, overview
-
-
-
additional information
?
-
-
Man II catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures
-
-
-
additional information
?
-
-
involved in trimming reactions in N-glycan maturation in the Golgi complex
-
-
-
additional information
?
-
-
co-expression of beta1,4-N-acetylglucosaminyltransferase III-ManIII and ManII, or of beta1,4-N-acetylglucosaminyltransferase III and ManII leads to the formation of bisected non-fucosylated glycans of the complex type
-
-
-
additional information
?
-
-
Bt1769, Bt3858 and Bt3991 are alpha-1,3-mannosidases that display particularly high activity against alpha-1,3-mannobiose
-
-
-
additional information
?
-
-
alpha-1,3-mannosidases, Bt3858 and Bt1769, convert Man4GlcNAc2 to Man3GlcNAc2, but do not attack Man5GlcNAc2, indicating that these enzymes cannot tolerate alpha-1,6-Man side chains
-
-
-
additional information
?
-
Man II catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures
-
-
-
additional information
?
-
-
involved in trimming reactions in N-glycan maturation in the Golgi complex
-
-
-
additional information
?
-
-
MII and alpha-mannosidase IIx function in N-glycan processing in a similar manner
-
-
-
additional information
?
-
-
MII and alpha-mannosidase IIx function in N-glycan processing in a similar manner. Alpha-mannosidase IIx shows no reactivity to high-mannose-type carbohydrates
-
-
-
additional information
?
-
-
involved in asparagine-linked oligosaccharide processing
-
-
-
additional information
?
-
-
required in the maturation of asparagine-linked oligosaccharides in the Golgi complex
-
-
-
additional information
?
-
-
biosynthesis of complex-type N-linked oligosaccharides of glycoproteins
-
-
-
additional information
?
-
-
function in Golgi membranes: presumably glycopolymer metabolism
-
-
-
additional information
?
-
-
Man II catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures
-
-
-
additional information
?
-
-
asparagine-linked glycoprotein biosynthesis
-
-
-
additional information
?
-
-
alpha-mannosidase III hydrolyzes (Man)5-9(GlcNAc)2, not: GlcNAc(Man)5(GlcNAc)2
-
-
-
additional information
?
-
-
alpha-mannosidase III hydrolyzes (Man)5-9(GlcNAc)2, not: GlcNAc(Man)5(GlcNAc)2
-
-
-
additional information
?
-
-
alpha-mannosidase III probably provides an alternate N-glycan processing pathway in Sf-9 cells
-
-
-
additional information
?
-
-
asparagine-linked glycoprotein biosynthesis
-
-
-
additional information
?
-
-
study of biosynthesis and processing of alpha-mannosidase III
-
-
-
additional information
?
-
higher eukaryotic GH38 alpha-mannosides play a key role in the modification and diversification of hybrid N-glycans, processes with strong cellular links to cancer and autoimmune disease
-
-
-
additional information
?
-
SpGH38 is an alpha-mannosidase with specificity for alpha-1,3 mannosidic linkages, active site structure, overview
-
-
-
additional information
?
-
-
the exo-type cytosolic class II enzyme cleaves off alpha-1,2-, alpha-1,3-, and alpha-1,6-mannose residues
-
-
-
additional information
?
-
-
no hydrolysis of alpha1,6-linkages
-
-
-
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
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose + H2O
alpha-D-mannopyranose
-
-
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + H2O
Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-1-Asn + alpha-D-mannose
physiological substrate, conversion by sequential removal of two alpha1,6-linked and alpha1,3-linked mannose residues from the alpha-1,6-branch of the substrate
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 H2O
Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
-
alpha-mannosidase IIx, M6Gn2 is the primary target in vivo, integral part of N-glycan biosynthesis
-
?
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 H2O
Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
GlcNAc(Man)5GlcNAc + 2 H2O
GlcNAc(Man)3GlcNAc + 2 alpha-D-mannose
-
natural substrate, involved in the processing of N-linked oligosaccharides
-
?
GlcNAc(Man)5GlcNAc + 2 H2O
GlcNAc(Man)3GlcNAc + 2 alpha-D-mannose
-
natural substrate, involved in the processing of N-linked oligosaccharides
-
-
?
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 H2O
Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
-
N-glycosylation pathway
-
?
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 H2O
Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
-
alpha-mannosidase II, biosynthesis of N-glycans
-
?
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 H2O
Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
-
involved in N-glycan maturation, acts after GlcNAc transferase I to remove 2 mannose residues to form GlcNAc(Man)3(GlcNAc)2 prior to extension into complex N-glycans
-
?
additional information
?
-
-
Golgi alpha-mannosidase II is a key enzyme in the formation of complex N-glycans in plants
-
-
-
additional information
?
-
Golgi alpha-mannosidase II is a key enzyme in the formation of complex N-glycans in plants
-
-
-
additional information
?
-
-
asparagine-linked glycoprotein biosynthesis
-
-
-
additional information
?
-
-
asparagine-linked glycoprotein biosynthesis
-
-
-
additional information
?
-
-
GMII is involved in the creation of glycoproteins that contain complex carbohydrates. It is responsible for the formation of the core trimannose structure to which all complex carbohydrates are appended. It catalyses the hydrolysis of an alpha(1,6)- and an alpha(1,3)-linked mannose from GlcNAc-Man5-GlcNAc2 to form GlcNAc-Man3-GlcNAc2-Asn-X
-
-
-
additional information
?
-
-
Co2+ regulates the substrate specificity, overview
-
-
-
additional information
?
-
-
Man II catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures
-
-
-
additional information
?
-
-
involved in trimming reactions in N-glycan maturation in the Golgi complex
-
-
-
additional information
?
-
-
Bt1769, Bt3858 and Bt3991 are alpha-1,3-mannosidases that display particularly high activity against alpha-1,3-mannobiose
-
-
-
additional information
?
-
Man II catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures
-
-
-
additional information
?
-
-
involved in trimming reactions in N-glycan maturation in the Golgi complex
-
-
-
additional information
?
-
-
MII and alpha-mannosidase IIx function in N-glycan processing in a similar manner
-
-
-
additional information
?
-
-
involved in asparagine-linked oligosaccharide processing
-
-
-
additional information
?
-
-
required in the maturation of asparagine-linked oligosaccharides in the Golgi complex
-
-
-
additional information
?
-
-
biosynthesis of complex-type N-linked oligosaccharides of glycoproteins
-
-
-
additional information
?
-
-
function in Golgi membranes: presumably glycopolymer metabolism
-
-
-
additional information
?
-
-
Man II catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures
-
-
-
additional information
?
-
-
asparagine-linked glycoprotein biosynthesis
-
-
-
additional information
?
-
-
alpha-mannosidase III probably provides an alternate N-glycan processing pathway in Sf-9 cells
-
-
-
additional information
?
-
-
asparagine-linked glycoprotein biosynthesis
-
-
-
additional information
?
-
-
study of biosynthesis and processing of alpha-mannosidase III
-
-
-
additional information
?
-
higher eukaryotic GH38 alpha-mannosides play a key role in the modification and diversification of hybrid N-glycans, processes with strong cellular links to cancer and autoimmune disease
-
-
-
additional information
?
-
-
the exo-type cytosolic class II enzyme cleaves off alpha-1,2-, alpha-1,3-, and alpha-1,6-mannose residues
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Fe2+
Mn2+
Zn2+
additional information
Zn2+
the recombinant GMII contains zinc in a stoichiometric amount
Zn2+
-
GMII contains a Zn atom which forms contacts with substrate analogues, stabilizes catalytic intermediates, and other inhibitors observed in the active site
Zn2+
-
is involved in the catalytic activity of the enzyme and in the strong binding of inhibitors
Zn2+
-
di-epi-swainsonine has only a single hydroxyl group at C-8 interacting with the zinc ion of the enzyme
additional information
no effect on recombinant GMII through Ca2+, Co2+, Mn2+, Ni2+, and Zn2+
additional information
-
not activated by Ba2+; not activated by Mg2+, Mn2+; not activated by Zn2+
additional information
-
does not need Ca2+ or any other metal cofactor of those tested
additional information
-
no metal ion requirement; not activated by Ca2+; not activated by Mg2+, Mn2+
additional information
-
no metal ion requirement; not activated by Ca2+; not activated by Mg2+, Mn2+
additional information
-
no metal ion requirement; not activated by Ca2+; not activated by Co2+; not activated by Mg2+, Mn2+; not activated by Sr2+; not activated by Zn2+
additional information
-
no metal ion requirement; not activated by Ca2+; not activated by Co2+; not activated by Mg2+, Mn2+; not activated by Zn2+
additional information
-
no metal ion requirement; not activated by Ca2+; not activated by Mg2+, Mn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2R,3R,4R,5S)-1-(methylthio)-2,3,4-trihydroxy-5-(N-(p-allyl-ester-benzyl)amino)cyclopentane
-
-
(1R,2R,3R,4R,5S)-1-(methylthio)-2,3,4-trihydroxy-5-(N-(p-bromo-benzyl)amino)cyclopentane
-
-
(1R,2R,3R,4R,5S)-1-(methylthio)-2,3,4-trihydroxy-5-(N-(p-chloro-benzyl)amino)cyclopentane
-
-
(1R,2R,3R,4R,5S)-1-(methylthio)-2,3,4-trihydroxy-5-(N-(p-fluoro-benzyl)amino)cyclopentane
-
-
(1R,2R,3R,4R,5S)-1-(methylthio)-2,3,4-trihydroxy-5-(N-(p-methoxy-benzyl)amino)cyclopentane
-
-
(1R,2R,3R,4R,5S)-1-(methylthio)-2,3,4-trihydroxy-5-(N-benzylamino)cyclopentane
-
-
(1R,2R,3R,4S,5S)-1,2,3,4-tetrahydroxy-5-(N-(p-allyl ester benzyl)amino)cyclopentane
-
-
(1R,2R,3R,4S,5S)-1,2,3,4-tetrahydroxy-5-(N-(p-bromo-benzyl)amino)cyclopentane
-
-
(1R,2R,3R,4S,5S)-1,2,3,4-tetrahydroxy-5-(N-(p-chloro-benzyl)amino)cyclopentane
-
-
(1R,2R,3R,4S,5S)-1,2,3,4-tetrahydroxy-5-(N-(p-fluoro-benzyl)amino)cyclopentane
-
-
(1R,2R,3R,4S,5S)-1,2,3,4-tetrahydroxy-5-(N-(p-methoxy-benzyl)amino)cyclopentane
-
-
(1R,2S,8aS)-1,2-dihydroxyoctahydrothieno[1,2-a]thiopyranium chloride
-
good inhibitor, lacks a hydroxyl group at C-5, more than 140fold better inhibitor of GMII than di-epi-swainsonine
(1R,6R,7R,8S)-7,8-dihydroxy-5-thia-1-thioniabicyclo[4.3.0]nonane chloride
-
synthetic inhibitor, selective and potent inhibition at 1 mM, 97% inhibition of the activity of the liver lysosomal fraction at pH 4.0, 100% at pH 6.5
(1S,2R,5R,8R,8aR)-5-[2-(4-tert-butylphenyl)ethyl]octahydroindolizine-1,2,8-triol
-
-
(1S,2R,5S,8R,8aR)-5-[2-(4-tert-butylphenyl)ethyl]octahydroindolizine-1,2,8-triol
-
-
(1S,2R,6R,7R,8S,8aS)-octahydroindolizine-1,2,6,7,8-pentol
-
most active
(2R,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
-
(2R,3R,4S)-2-([[(1S)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
-
(2R,3R,4S)-2-[[((1R)-2-hydroxy-1-[4'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl]ethyl)amino] methyl]pyrrolidine-3,4-diol
-
inhibits the proliferation of primary cells and cell lines of different origins, irrespective of Bcl-2 expression levels, inducing a G2/Mcell cycle arrest and by modification of genes involved in cell cycle progression and survival, IC50 in vivo and cytotoxic effects in different cell lines, overview
(2R,3R,4S)-2[([(1R)-2-hydroxy-1-(4-methoxyphenyl)ethyl]amino)-methyl]pyrrolidine-3,4-diol
-
-
(2R,3R,4S)-2[[((1R)-1-[1,1'-biphenyl]-4-yl-2-hydroxyethyl)amino]-methyl]pyrrolidine-3,4-diol
-
-
(2R,3R,4S)-2[[((1R)-2-hydroxy-1-(4-(phenylmethoxy)phenyl)ethyl)amino]methyl]pyrrolidine-3,4-diol
-
-
(2R,3R,4S)-2[[((1R)-2-hydroxy-1-[4-(2-thienyl)phenyl]ethyl)-amino]methyl]pyrrolidine-3,4-diol
-
-
(2R,3R,4S)-2[[((1R)-2-hydroxy-1-[4-(prop-2-enyloxy)phenyl]-ethyl)amino]methyl] pyrrolidine-3,4-diol
-
-
(2R,3R,4S,5R)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-5-methylpyrrolidine-3,4-diol
-
-
(2R,3R,4S,5S)-6-amino-2-(hydroxymethyl)-2,3,4,5-tetrahydropyridine-3,4,5-triol
-
-
(2R,3S,4S)-1-[(2S,3S)-2,4-dihydroxy-3-(sulfooxy)butyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
-
-
(2S,3R,4S)-2-[([(1R)-2-[(4-bromophenyl)(hydroxy)methoxy]-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
-
(3R,4R,5R)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
-
-
(3R,4R,5R)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
-
-
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
(3R,4R,5S)-5-[([(1R)-2-[(4-bromophenyl)(hydroxy)methoxy]-1-phenylethyl]amino)methyl]-3,4-dihydroxy-1-methylpyrrolidin-2-one
-
-
(3R,4R,5S)-5-[([(1R)-2-[(4-bromophenyl)(hydroxy)methoxy]-1-phenylethyl]amino)methyl]-3,4-dihydroxypyrrolidin-2-one
-
-
(3S,4S,5R,6R,E)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-one O-4-chlorophenylcarbamoyl oxime
-
(5R,6R,7S,8R)-5-methyl-1,5,6,7,8,8a-hexahydrotetrazolo[1,5-a]pyridine-6,7,8-triol
-
-
(5R,6R,7S,8S)-5-(hydroxymethyl)-1,5,6,7,8,8a-hexahydroimidazo[1,2-a]pyridine-6,7,8-triol
-
-
1-(4-methylphenyl)-2-[(1S,2R,5R,8R,8aR)-1,2,8-trihydroxyoctahydroindolizin-5-yl]ethanone
-
-
1-(4-tert-butylphenyl)-2-[(1S,2R,5R,8R,8aR)-1,2,8-trihydroxyoctahydroindolizin-5-yl]ethanone
-
-
1-(4-tert-butylphenyl)-2-[(1S,2R,5S,8R,8aR)-1,2,8-trihydroxyoctahydroindolizin-5-yl]ethanone
-
-
1-phenyl-2-[(1S,2R,5R,8R,8aR)-1,2,8-trihydroxyoctahydroindolizin-5-yl]ethanone
-
-
2-deoxy-2-fluoro-alpha-D-mannosyl fluoride
-
reversible, D341N mutant GMII
2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
-
in decreasing order of efficiency: alpha1,2, alpha 1,3 and alpha1,6-mannosylmannose
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
-
in decreasing order of efficiency: alpha1,2, alpha 1,3 and alpha1,6-mannosylmannose
5-fluoro-beta-L-gulosyl fluoride
-
reversible, wild-type and D341N mutant GMII, inhibits only at low assay temperatures, acts as slow substrate at 37°C
6-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
-
in decreasing order of efficiency: alpha1,2, alpha 1,3 and alpha1,6-mannosylmannose
EGTA
-
ethylene glycol-bis(beta-aminoethylether)-N,N,N',N'-tetraacetic acid
guanidinium hydrochloride
-
the enzyme loses 54% and 70% of the original activity in 0.5 M and 1.0 M guanidinium hydrochloride, respectively. Irreversible denaturation at higher concentration of 6 M of guanidinium hydrochloride, kinetics, overview. The protein almost completely unfolds in 4.0 M guanidinium hydrochloride
Mannosyl-mannose disaccharide
-
in decreasing order of efficiency: alpha1,2, alpha 1,3 and alpha1,6-mannosylmannose
-
N-benzyl mannostatin A
-
structural basis of the inhibition of Golgi alpha-mannosidase II and the role of the thiomethyl moiety in ligand-protein interactions, overview
[[(3S,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-ylidene]amino] N-(4-chlorophenyl)carbamate
-
(2S,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
-
(2S,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
-
(2S,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
-
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
-
competitive inhibitor
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
-
competitive inhibitor
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
-
-
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
-
competitve inhibitor
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
-
competitve inhibitor
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
-
competitve inhibitor
1-deoxyaminocyclopentitetrol
-
structural basis of the inhibition of Golgi alpha-mannosidase II and the role of the thiomethyl moiety in ligand-protein interactions, overview
1-deoxymannojirimycin
-
more inhibitory than kifunensine, mode of binding
1-deoxymannojirimycin
-
61% inhibition of the activity of the liver lysosomal fraction at pH 4.0, 37% at pH 6.5, at 1 mM
Cu2+
-
0.1 mM, 90% inhibition of GlcNAc(Man)5(GlcNAc)2 hydrolysis, 0.01 mM, 50% inhibition of 4-nitrophenyl alpha-D-mannoside hydrolysis; strong
D-mannonolactam amidrazone
-
broad spectrum mannosidase inhibitor, strong; IC50: 400 nM
D-mannonolactam amidrazone
-
broad spectrum mannosidase inhibitor, strong; equally as effective as mannostatin A, IC50: 90-100 nM
EDTA
-
alpha-mannosidase III, 1 mM, 90% inhibition of 4-nitrophenyl alpha-D-mannoside hydrolysis, 5 mM, complete inhibition of (Man)5(GlcNAc)2-PA hydrolysis
Mannostatin A
-
cyclopentanol structure containing thiomethyl and amino functional groups, in vivo and in vitro
Mannostatin A
-
; structural basis of the inhibition of Golgi alpha-mannosidase II and the role of the thiomethyl moiety in ligand-protein interactions, overview
Mannostatin A
-
cyclopentanol structure containing thiomethyl and amino functional groups, in vivo and in vitro
Mannostatin A
-
cyclopentanol structure containing thiomethyl and amino functional groups, in vivo and in vitro; potent inhibitor, equally effective as D-mannonolactam amidrazone
Mannostatin A
-
cyclopentanol structure containing thiomethyl and amino functional groups, in vivo and in vitro; very potent inhibitor, competitive, IC50: about 10 nM with 4-nitrophenyl alpha-D-mannoside as substrate, about 90 nM with GlcNAc(Man)5GlcNAc as substrate, equally potent as swainsonine
swainsonine
-
-
swainsonine
-
inhibits both alpha-mannosidase II and IIx, the latter is less sensitive
swainsonine
-
potent inhibition at 1 mM, 100% inhibition of the activity of the liver lysosomal fraction at pH 4.0, 95% at pH 6.5
swainsonine
-
disrupts enzyme activity, whereby inducing a novel class of hybrid-type glycosylation containing a partially processed mannose moiety
swainsonine
-
200 nM, 50% inhibition; i.e. (1S,2R,8R,8aR)-1,2,8-trihydroxyoctahydroindolizidine; very strong
swainsonine
-
200 nM, 50% inhibition; kinetics, in vivo and in vitro, partially reversible depending on inhibitor concentration
additional information
no inhibition of recombinant GMII by EDTA
-
additional information
-
inhibitor design and synthesis, and cytototxic effect in vivo, overview. 2-[(Benzylamino)methyl]pyrrolidine-3,4-diol derivatives as alpha-mannosidase inhibitors and with antitumor activities against hematological and solid malignancies
-
additional information
-
not inhibited by Co2+, Zn2+; not inhibited by EDTA; not inhibited by Tris-Cl, iodoacetamide, alpha-methylmannoside; not inhibited by Tris-maleate
-
additional information
-
not inhibited by chelating agents, 0.1 mM 1,10-phenanthroline, 1 mM 2,2'-dipyridyl, 250 mM glucose, 250 mM galactose; not inhibited by EDTA; not inhibited by Mn2+, Mg2+
-
additional information
-
effect of tunicamycin and castanospermine on the production of the 3 forms of alpha-mannosidase III
-
additional information
-
not inhibited by castanospermine, deoxynojirimycin; not inhibited by deoxymannojirimycin
-
additional information
-
not inhibited by Co2+, Zn2+; not inhibited by deoxymannojirimycin; not inhibited by EDTA; not inhibited by EGTA, 6-epicastanospermine, 2-episwainsonine, a trisaccharide of mannose residues linked in alpha-1,2-linkages, a tetrasaccharide of mannose with the nonreducing mannose linked in alpha-1,3-linkage to an alpha-1,2-linked trisaccharide of mannose; not inhibited by Mn2+, Mg2+
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not activated by glucose, galactose, AMP, ADP, GMP, GDP, GTP, CDP, CTP, UMP, UDP, UTP, cAMP, cGMP
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
alpha-Mannosidosis
Golgi alpha-mannosidase II deficiency in vertebrate systems: implications for asparagine-linked oligosaccharide processing in mammals.
Anemia
A human embryonic kidney 293T cell line mutated at the Golgi alpha-mannosidase II locus.
Anemia
Golgi alpha-mannosidase II deficiency in vertebrate systems: implications for asparagine-linked oligosaccharide processing in mammals.
Anemia, Dyserythropoietic, Congenital
A human embryonic kidney 293T cell line mutated at the Golgi alpha-mannosidase II locus.
Anemia, Dyserythropoietic, Congenital
Golgi alpha-mannosidase II deficiency in vertebrate systems: implications for asparagine-linked oligosaccharide processing in mammals.
Carcinoma
Swainsonine, an inhibitor of glycoprotein processing, enhances cytotoxicity of large granular lymphocytes.
Carcinoma, Hepatocellular
Processing by endoplasmic reticulum mannosidases partitions a secretion-impaired glycoprotein into distinct disposal pathways.
Diabetes Mellitus, Type 2
Variants in KCNQ1, AP3S1, MAN2A1, and ALDH7A1 and the risk of type 2 diabetes in the Chinese Northern Han population: a case-control study and meta-analysis.
Infections
Antibody-independent, complement-mediated enhancement of HIV-1 infection by mannosidase I and II inhibitors.
Infertility, Male
The in vivo role of alpha-mannosidase IIx and its role in processing of N-glycans in spermatogenesis.
Leukemia
Sensitivity to alpha/beta-interferon is independent of N-linked complex-type oligosaccharides on cell-surface-membrane glycoproteins.
Leukemia
The presence of concanavalin-A(Con-A)-like molecules on natural-killer (NK)-sensitive target cells: their possible role in swainsonine-augmented human NK cytotoxicity.
Lysosomal Storage Diseases
A swainsonine survey of North American Astragalus and Oxytropis taxa implicated as locoweeds.
Lysosomal Storage Diseases
Fungicide treatment and clipping of Oxytropis sericea does not disrupt swainsonine concentrations.
Lysosomal Storage Diseases
Golgi alpha-mannosidase II deficiency in vertebrate systems: implications for asparagine-linked oligosaccharide processing in mammals.
Lysosomal Storage Diseases
Swainsonine-containing plants and their relationship to endophytic fungi.
mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase deficiency
Golgi alpha-mannosidase II deficiency in vertebrate systems: implications for asparagine-linked oligosaccharide processing in mammals.
Neoplasm Metastasis
The inhibition of platelet aggregation of metastatic H-ras-transformed 10T1/2 fibroblasts with castanospermine, an N-linked glycoprotein processing inhibitor.
Neoplasms
MAN2A1-FER Fusion Gene Is Expressed by Human Liver and Other Tumor Types and Has Oncogenic Activity in Mice.
Neoplasms
Morphological changes in the Golgi complex correlate with actin cytoskeleton rearrangements.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Genome-wide association study of childhood acute lymphoblastic leukemia in Korea.
Vesicular Stomatitis
A novel glycosylation phenotype expressed by Lec23, a Chinese hamster ovary mutant deficient in alpha-glucosidase I.
Vesicular Stomatitis
Morphological and functional association of Sec22b/ERS-24 with the pre-Golgi intermediate compartment.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
25
2-deoxy-2-fluoro-alpha-D-mannosyl fluoride
-
pH 5.6, 37°C, above, wild-type GMII
3.6
4-methylumbelliferyl alpha-D-mannopyranoside
pH 6.8, 37°C, recombinant enzyme
0.2
D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-Asn
-
i.e. glycopeptide III
0.05
2,4-dinitrophenyl alpha-D-mannoside
-
pH 5.6, 37°C, D341N mutant GMII
5.5
2,4-dinitrophenyl alpha-D-mannoside
-
pH 5.6, 37°C, wild-type GMII
27
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose
pH 6.8, 37°C, recombinant enzyme
0.55
4-methylumbelliferyl-alpha-D-mannopyranoside
-
extracted from endothelial cells HCEC
0.65
4-methylumbelliferyl-alpha-D-mannopyranoside
-
extracted from human glioblastoma cells LNZ308
1.065
4-methylumbelliferyl-alpha-D-mannopyranoside
-
extracted from human glioblastoma cells LN18
40
4-nitrophenyl alpha-D-mannoside
-
intact 124 kDa Man II and chymotrypsin-cleaved 110 kDa catalytic subunit
1.25
Manalpha(1,6)(Manalpha(1,3))Manbeta(1,4)GlcNAcbeta(1,4)GlcNAc
-
NaBH4 reduced; pH 5, 37°C
1.25
Manalpha(1,6)(Manalpha(1,3))Manbeta(1,4)GlcNAcbeta(1,4)GlcNAc
-
NaBH4 reduced
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
4-methylumbelliferyl alpha-D-mannopyranoside
pH 6.8, 37°C, recombinant enzyme
0.0051
5-fluoro-beta-L-gulosyl fluoride
-
pH 5.6, 37°C, wild-type GMII
0.048
2,4-dinitrophenyl alpha-D-mannoside
-
pH 5.6, 37°C, D341N mutant GMII
8.6
2,4-dinitrophenyl alpha-D-mannoside
-
pH 5.6, 37°C, wild-type GMII
6.4
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose
pH 6.8, 37°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
2,4-dinitrophenyl alpha-D-mannopyranoside
-
pH 6.8, 37°C, recombinant enzyme
0.24
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose
-
pH 6.8, 37°C, recombinant enzyme
54
4-nitrophenyl alpha-D-mannoside
-
recombinant enzyme, in 50 mM sodium phosphate buffer, pH 6.5, at 65°C
351
4-nitrophenyl alpha-D-mannoside
-
native enzyme, in 50 mM sodium phosphate buffer, pH 6.5, at 65°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00322
(1R,2R,3R,4R,5S)-1-(methylthio)-2,3,4-trihydroxy-5-(N-(p-allyl ester benzyl)amino)cyclopentane
-
reaction volume containing 4-methylumbelliferyl alpha-D-mannopyranoside, sodium acetate pH 5.6 and ZnCl at 37°C
0.00051
(1R,2R,3R,4R,5S)-1-(methylthio)-2,3,4-trihydroxy-5-(N-(p-bromo-benzyl)amino)cyclopentane
-
reaction volume containing 4-methylumbelliferyl alpha-D-mannopyranoside, sodium acetate pH 5.6 and ZnCl at 37°C
0.00091
(1R,2R,3R,4R,5S)-1-(methylthio)-2,3,4-trihydroxy-5-(N-(p-chloro-benzyl)amino)cyclopentane
-
reaction volume containing 4-methylumbelliferyl alpha-D-mannopyranoside, sodium acetate pH 5.6 and ZnCl at 37°C
0.00053
(1R,2R,3R,4R,5S)-1-(methylthio)-2,3,4-trihydroxy-5-(N-(p-fluoro-benzyl)amino)cyclopentane
-
reaction volume containing 4-methylumbelliferyl alpha-D-mannopyranoside, sodium acetate pH 5.6 and ZnCl at 37°C
0.00052
(1R,2R,3R,4R,5S)-1-(methylthio)-2,3,4-trihydroxy-5-(N-(p-methoxy-benzyl)amino)cyclopentane
-
reaction volume containing 4-methylumbelliferyl alpha-D-mannopyranoside, sodium acetate pH 5.6 and ZnCl at 37°C
0.00088
(1R,2R,3R,4R,5S)-1-(methylthio)-2,3,4-trihydroxy-5-(N-benzylamino)cyclopentane
-
reaction volume containing 4-methylumbelliferyl alpha-D-mannopyranoside, sodium acetate pH 5.6 and ZnCl at 37°C
0.000076
(1R,2R,3R,4S,5R)-4-amino-5-methoxycyclopentane-1,2,3-triol
-
;
0.0044
(1R,2R,3R,4S,5S)-1,2,3,4-tetrahydroxy-5-(N-(p-allyl ester benzyl)amino)cyclopentane
-
reaction volume containing 4-methylumbelliferyl alpha-D-mannopyranoside, sodium acetate pH 5.6 and ZnCl at 37°C
0.0076
(1R,2R,3R,4S,5S)-1,2,3,4-tetrahydroxy-5-(N-(p-bromo-benzyl)amino)cyclopentane
-
reaction volume containing 4-methylumbelliferyl alpha-D-mannopyranoside, sodium acetate pH 5.6 and ZnCl at 37°C
0.0081
(1R,2R,3R,4S,5S)-1,2,3,4-tetrahydroxy-5-(N-(p-chloro-benzyl)amino)cyclopentane
-
reaction volume containing 4-methylumbelliferyl alpha-D-mannopyranoside, sodium acetate pH 5.6 and ZnCl at 37°C
0.006
(1R,2R,3R,4S,5S)-1,2,3,4-tetrahydroxy-5-(N-(p-fluoro-benzyl)amino)cyclopentane
-
reaction volume containing 4-methylumbelliferyl alpha-D-mannopyranoside, sodium acetate pH 5.6 and ZnCl at 37°C
0.0066
(1R,2R,3R,4S,5S)-1,2,3,4-tetrahydroxy-5-(N-(p-methoxy-benzyl)amino)cyclopentane
-
reaction volume containing 4-methylumbelliferyl alpha-D-mannopyranoside, sodium acetate pH 5.6 and ZnCl at 37°C
0.01
(1R,2R,3R,4S,5S)-1,2,3,4-tetrahydroxy-5-(N-benzylamino)cyclopentane
-
reaction volume containing 4-methylumbelliferyl alpha-D-mannopyranoside, sodium acetate pH 5.6 and ZnCl at 37°C
0.067
(2R,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
20C, pH 6.8
0.000135 - 0.067
(2S,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
0.001
(3R,4R,5R)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
-
20C, pH 6.8
0.022
(3R,4R,5R)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
-
20C, pH 6.8
0.000206 - 0.0032
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
0.004 - 0.022
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
0.52
(3S,4S,5R,6R,E)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-one O-4-chlorophenylcarbamoyl oxime
-
0.0027
1-(4-methylphenyl)-2-[(1S,2R,5R,8R,8aR)-1,2,8-trihydroxyoctahydroindolizin-5-yl]ethanone
-
pH 5.75, 25°C
0.0027
1-(4-tert-butylphenyl)-2-[(1S,2R,5R,8R,8aR)-1,2,8-trihydroxyoctahydroindolizin-5-yl]ethanone
-
pH 5.75, 25°C
0.0028
1-phenyl-2-[(1S,2R,5R,8R,8aR)-1,2,8-trihydroxyoctahydroindolizin-5-yl]ethanone
-
pH 5.75, 25°C
7.5
2-deoxy-2-fluoro-alpha-D-mannosyl fluoride
-
pH 5.6, 37°C, D341N mutant GMII
0.6
5-fluoro-beta-L-gulosyl fluoride
-
pH 5.6, 37°C, D341N mutant GMII
0.00021
mannostatin
-
reaction volume containing 4-methylumbelliferyl alpha-D-mannopyranoside, sodium acetate pH 5.6 and ZnCl at 37°C
50
meso-aminocyclopentitretrol
-
reaction volume containing 4-methylumbelliferyl alpha-D-mannopyranoside, sodium acetate pH 5.6 and ZnCl at 37°C
0.52
[[(3S,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-ylidene]amino] N-(4-chlorophenyl)carbamate
pH 5.6
additional information
additional information
-
although too weak for full Ki analyses with the amounts of material available, all analogues with salacinol-like stereochemistry at positions 2 and 3 proved to be weak inhibitors of the enzyme with IC50 values of approximately 7.5 mM
-
0.000135
(2S,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
-
0.0233
(2S,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
extracted from endothelial cells HCEC
0.0325
(2S,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
extracted from human glioblastoma cells LN18
0.0415
(2S,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
extracted from human glioblastoma cells LNZ308
0.067
(2S,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
-
0.000206
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
-
-
0.00055
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
-
extracted from human glioblastoma cells LNZ308
0.00067
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
-
extracted from endothelial cells HCEC
0.001
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
-
-
0.0032
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
-
extracted from human glioblastoma cells LN18
0.004
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
-
-
0.022
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
-
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00025
(1S,2R,5R,8R,8aR)-5-[2-(4-tert-butylphenyl)ethyl]octahydroindolizine-1,2,8-triol
Drosophila melanogaster
-
pH 5.75, 25°C
0.000044
(1S,2R,5S,8R,8aR)-5-[2-(4-tert-butylphenyl)ethyl]octahydroindolizine-1,2,8-triol
Drosophila melanogaster
-
pH 5.75, 25°C
0.8
(2R,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
Drosophila melanogaster
-
-
0.72
(2R,3R,4S)-2-([[(1S)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
Drosophila melanogaster
-
-
1
(2R,3R,4S,5R)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-5-methylpyrrolidine-3,4-diol
Drosophila melanogaster
-
-
0.025 - 0.05
(2S,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
0.075 - 0.2
(2S,3R,4S)-2-[([(1R)-2-[(4-bromophenyl)(hydroxy)methoxy]-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
0.0005 - 0.002
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
0.05 - 0.35
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
0.00075 - 0.075
(3R,4R,5S)-5-[([(1R)-2-[(4-bromophenyl)(hydroxy)methoxy]-1-phenylethyl]amino)methyl]-3,4-dihydroxy-1-methylpyrrolidin-2-one
0.075 - 0.75
(3R,4R,5S)-5-[([(1R)-2-[(4-bromophenyl)(hydroxy)methoxy]-1-phenylethyl]amino)methyl]-3,4-dihydroxypyrrolidin-2-one
2.5
(RS)-2-phenylethyl alpha-D-mannopyranosyl sulfoxide
Homo sapiens
-
in 50 mM sodium acetate buffer pH 5.8, at 37°C
0.000029
1-(4-methylphenyl)-2-[(1S,2R,5R,8R,8aR)-1,2,8-trihydroxyoctahydroindolizin-5-yl]ethanone
Drosophila melanogaster
-
pH 5.75, 25°C
0.000029
1-(4-tert-butylphenyl)-2-[(1S,2R,5R,8R,8aR)-1,2,8-trihydroxyoctahydroindolizin-5-yl]ethanone
Drosophila melanogaster
-
pH 5.75, 25°C
0.00025
1-(4-tert-butylphenyl)-2-[(1S,2R,5S,8R,8aR)-1,2,8-trihydroxyoctahydroindolizin-5-yl]ethanone
Drosophila melanogaster
-
pH 5.75, 25°C
0.00003
1-phenyl-2-[(1S,2R,5R,8R,8aR)-1,2,8-trihydroxyoctahydroindolizin-5-yl]ethanone
Drosophila melanogaster
-
pH 5.75, 25°C
1.5
2-phenylethyl alpha-D-mannopyranosyl sulfone
Homo sapiens
-
in 50 mM sodium acetate buffer pH 5.8, at 37°C
2
benzyl alpha-D-mannopyranosyl sulfone
Homo sapiens
-
in 50 mM sodium acetate buffer pH 5.8, at 37°C
0.025
(2S,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
Homo sapiens
-
extracted from endothelial cells HCEC
0.05
(2S,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
Homo sapiens
-
extracted from human glioblastoma cells LN18; extracted from human glioblastoma cells LNZ308
0.075
(2S,3R,4S)-2-[([(1R)-2-[(4-bromophenyl)(hydroxy)methoxy]-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
Homo sapiens
-
extracted from endothelial cells HCEC; extracted from human glioblastoma cells LNZ308
0.2
(2S,3R,4S)-2-[([(1R)-2-[(4-bromophenyl)(hydroxy)methoxy]-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
Homo sapiens
-
extracted from human glioblastoma cells LN18
0.0005
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
Homo sapiens
-
extracted from endothelial cells HCEC; extracted from human glioblastoma cells LNZ308
0.002
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
Homo sapiens
-
extracted from human glioblastoma cells LN18
0.05
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
Homo sapiens
-
extracted from human glioblastoma cells LNZ308
0.075
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
Homo sapiens
-
extracted from endothelial cells HCEC
0.35
(3R,4R,5S)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
Homo sapiens
-
extracted from human glioblastoma cells LN18
0.00075
(3R,4R,5S)-5-[([(1R)-2-[(4-bromophenyl)(hydroxy)methoxy]-1-phenylethyl]amino)methyl]-3,4-dihydroxy-1-methylpyrrolidin-2-one
Homo sapiens
-
extracted from endothelial cells HCEC
0.0075
(3R,4R,5S)-5-[([(1R)-2-[(4-bromophenyl)(hydroxy)methoxy]-1-phenylethyl]amino)methyl]-3,4-dihydroxy-1-methylpyrrolidin-2-one
Homo sapiens
-
extracted from human glioblastoma cells LNZ308
0.075
(3R,4R,5S)-5-[([(1R)-2-[(4-bromophenyl)(hydroxy)methoxy]-1-phenylethyl]amino)methyl]-3,4-dihydroxy-1-methylpyrrolidin-2-one
Homo sapiens
-
extracted from human glioblastoma cells LN18
0.075
(3R,4R,5S)-5-[([(1R)-2-[(4-bromophenyl)(hydroxy)methoxy]-1-phenylethyl]amino)methyl]-3,4-dihydroxypyrrolidin-2-one
Homo sapiens
-
extracted from endothelial cells HCEC
0.15
(3R,4R,5S)-5-[([(1R)-2-[(4-bromophenyl)(hydroxy)methoxy]-1-phenylethyl]amino)methyl]-3,4-dihydroxypyrrolidin-2-one
Homo sapiens
-
extracted from human glioblastoma cells LNZ308
0.75
(3R,4R,5S)-5-[([(1R)-2-[(4-bromophenyl)(hydroxy)methoxy]-1-phenylethyl]amino)methyl]-3,4-dihydroxypyrrolidin-2-one
Homo sapiens
-
extracted from human glioblastoma cells LN18
0.00009 - 0.0001
D-mannonolactam amidrazone
Vigna radiata
-
equally as effective as mannostatin A, IC50: 90-100 nM
0.00001
Mannostatin A
Vigna radiata
-
very potent inhibitor, competitive, IC50: about 10 nM with 4-nitrophenyl alpha-D-mannoside as substrate, about 90 nM with GlcNAc(Man)5GlcNAc as substrate, equally potent as swainsonine
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.38
purified recombinant GMII expressed in insect cells, substrate 4-nitrophenyl alpha-mannoside
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
5.75
5.8
6 - 6.5
additional information
5.5
-
endogenous enzyme in 3T3 cells and recombinant enzyme expressed in COS cells
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 6
-
pH 3.5: more than 70% of maximal activity, pH 6: about half-maximal activity
4.2 - 6
-
pH 4.2: about half-maximal activity, pH 6: about 80% of maximal activity
4.2 - 6.6
pH 4.2: about 20% of maximal activity, pH 6.6: about 85% of maximal activity
5.5 - 6.7
-
alpha-mannosidase III activity is negligible at pH 5.5, increases at pH 5.7-5.9, decreases at pH 6.1 and rises to a plateau at pH 6.5-6.7
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
30°C: about 40% of maximal activity, 55°C: about 40% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
brenda
-
646574, 646625, 646631, 646639, 664599, 664603, 672706, 679856, 680041, 696732, 707745, 709035, 710037, 714909, 731660, 751356
-
-
brenda
-
-
-
brenda
at least 3 different forms of ManIII; Sf-9, alpha-mannosidase III
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the enzyme is lowly expressed in the molecular layer of the cerebral cortex and hippocampal layers, and highly expressed in other areas of the brain
brenda
-
clear cells in all epdididymal regions, not in principal cells
brenda
-
cells selectively express alpha-mannosidase II, with minimal expression of its isozyme, alpha-mannosidase IIx
brenda
-
freeze-dried mixture of mycelium and its culture medium, commercially available as Morushin
brenda
-
mutant HEK293T cell line called Lec36, which displays sensitivity to ricin that lies between the parental HEK 293T cells, in which the secreted and membrane-expressed proteins are dominated by complex-type glycosylation, and 293S Lec1 cells, which produce only oligomannose-type N-linked glycans. Lec36 cells are dominated by hybrid-type glycosylation. Wild-type and mutant enzyme expression analysis, overview
brenda
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
hepatocytes cultured in dexamethason-supplemented medium
brenda
-
at least 3 forms of alpha-mannosidase III, the smallest form accumulates in the extracellular fraction
-
brenda
SpGH38 may be intracellular, absence of any classical signal peptide
brenda
-
hepatocytes cultured in colchicine-containing medium
brenda
additional information
-
2 enzymes: a membrane-bound microsomal and a soluble cytoplasmic one
brenda
Golgi alpha-mannosidase II, the enzyme has a transmembrane domain and a cytoplasmic tail sufficient for localisation of the enzyme to the Golgi complex, retention by lumenal sequences is not involved, retention mechanism
brenda
-
-
brenda
-
type II membrane protein, alpha-mannosidase II and IIx
brenda
-
type II transmembrane protein with short cytoplasmic tail, single transmembrane domain and large C-terminal catalytic domain
brenda
-
integral membrane protein, hydrophilic catalytic domain is anchored to the lumenal face of Golgi membranes through an NH2-terminal hydrophobic membrane-anchoring domain
brenda
-
-
brenda
-
topology study: integral membrane protein with lumenal orientation, hydrophilic catalytic domain is bound to an integral hydrophobic membrane anchoring domain through a proteolytically sensitive linkage
brenda
-
type II transmembrane enzyme, subcompartmental localization, mainly over medial saccules of the Golgi stack
brenda
-
alpha-mannosidase III, integral membrane glycoprotein with type II topology
brenda
Golgi alpha-mannosidase II is a type II membrane protein
brenda
-
type II transmembrane protein with short cytoplasmic tail, single transmembrane domain and large hydrophilic C-terminal domain
brenda
-
type II transmembrane protein with short cytoplasmic tail, single transmembrane domain and large hydrophilic C-terminal domain
brenda
-
2 enzymes: a membrane-bound microsomal and a soluble cytoplasmic one
brenda
-
2 enzymes: a membrane-bound microsomal and a soluble cytoplasmic one
-
brenda
additional information
-
AfAms1 contains no cleavable signal sequence or transmembrane domain
-
brenda
additional information
AfAms1 contains no cleavable signal sequence or transmembrane domain
-
brenda
additional information
-
AfAms1 contains no cleavable signal sequence or transmembrane domain
-
-
brenda
additional information
-
absent from the endoplasmic reticulum, lysosomes, and autophagosomes
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
alpha-mannosidase II deficiency has a minimal effect on N-glycan maturation in most cell types due to the compensation by alpha-mannosidase IIx, ablation of alpha-MII impairs the maturation of N-glycans in intestinal epithelial cells. alpha-mannosidase II (DELTA intestinal epithelial cell) mice are less susceptible to dextran sulfate sodium-induced colitis compared with control littermates. Neutrophil infiltration in the colonic mucosa is attenuated in alpha-mannosidase II (DELTA intestinal epithelial cell) mice. Gene expression levels of neutrophil-attracting chemokines are downregulated in the colonic tissue
physiological function
physiological function
-
key enzyme in removal of mannose residues from the maturing oligosaccharide by hydrolyzing the mannosyl glycosidic bond as part of the machinery of complex carbohydrate formation
physiological function
the Afams1 gene, in contrast to its homologues in Saccharomyces cerevisiae or Aspergillus nidulans, is required for morphogenesis and cellular function in Aspergillus fumigatus
physiological function
-
the enzyme is important for N-glycosylation of protein in the Golgi apparatus
physiological function
-
the enzyme is perhaps functioning in the subsequent degradation of extracellular host glycans following their initial digestion by secreted glycosidases
physiological function
key glycosyl hydrolase in the N-linked glycosylation pathway
physiological function
-
the enzyme plays a crucial, but not exclusive, role in the maturation of N-glycans. Intestinal epithelial cell alpha-mannosidase II promotes intestinal inflammation by facilitating chemokine expression
physiological function
-
the Afams1 gene, in contrast to its homologues in Saccharomyces cerevisiae or Aspergillus nidulans, is required for morphogenesis and cellular function in Aspergillus fumigatus
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
D5BNB0_PUNMI
Puniceispirillum marinum (strain IMCC1322)
378
1
41669
TrEMBL
F9ULI0_LACPL
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
899
0
101855
TrEMBL