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(Man)3GlcNAc + H2O
?
-
poor substrate
-
-
?
(Man)6GlcNAc + H2O
?
-
rate at 2% of GlcNAc(Man)5GlcNAc hydrolysis
-
-
?
(Man)7GlcNAc + H2O
?
-
rate at 3% of GlcNAc(Man)5GlcNAc hydrolysis
-
-
?
(Man)8GlcNAc + H2O
?
-
rate at 5% of GlcNAc(Man)5GlcNAc hydrolysis
-
-
?
(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
-
-
?
(Man)9GlcNAc + H2O
?
-
rate at 6.4% of GlcNAc(Man)5GlcNAc hydrolysis
-
-
?
2,4-dinitrophenyl alpha-D-mannopyranoside + H2O
2,4-dinitrophenol + alpha-D-mannopyranose
-
-
-
?
2,4-dinitrophenyl alpha-D-mannopyranoside + H2O
?
-
-
-
?
2,4-dinitrophenyl alpha-D-mannoside + H2O
2,4-dinitrophenol + alpha-D-mannose
2,4-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
-
-
?
2,5-dinitrophenyl-alpha-D-mannopyranoside + H2O
2,5-dinitrophenol + D-mannose
-
-
-
?
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
-
-
?
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose + H2O
alpha-D-mannopyranose
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-mannopyranoside + H2O
?
-
-
-
?
4-methylumbelliferyl alpha-D-mannoside + H2O
4-methylumbelliferol + 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 + D-mannopyranose
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
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
-
-
?
alpha-D-Man-(1,6)-D-Man + H2O
alpha-D-mannopyranose
-
-
-
-
?
alpha-D-Manp-(1,3)-D-Manp + H2O
alpha-D-mannopyranose
-
-
-
-
?
alpha-D-Manp-(1,6)-D-Manp + H2O
alpha-D-mannopyranose
-
-
-
-
?
baker's yeast mannan + H2O
?
-
-
-
-
?
D-Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + H2O
?
-
NaBH4 reduced, poor substrate
-
-
?
D-Manalpha(1-3)Manbeta(1-4)GlcNAc + H2O
D-Manbeta(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-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
?
GlcNAc(Man)5GlcNAc + 2 H2O
GlcNAc(Man)3GlcNAc + 2 alpha-D-mannose
GlcNAc(Man)5GlcNAc2 + H2O
GlcNAc(Man)3GlcNAc2 + D-mannose
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
-
-
?
GlcNAcMan5GlcNAc2 + H2O
?
-
-
-
-
?
GlcNAcMan5GlcNAc2 + H2O
? + alpha-D-mannose
-
-
-
?
high mannose chains of thyroglobulin and phytohemagglutinin-P + H2O
? + D-mannose
-
thyroglobulin: 70% of alpha1,2-mannose residues accessible
-
-
?
high mannose N-glycan + H2O
?
-
-
-
?
Man5GlcNAc2 + H2O
Man3GlcNAc2 + 2 alpha-D-mannopyranose
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
-
-
-
-
?
ovalbumin + H2O
?
-
-
-
-
?
ovalbumin glycopeptide + H2O
? + D-mannose
-
glycopeptide IV
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
-
-
-
-
?
pyridylaminated (Man)5(GlcNAc)2 + H2O
pyridylaminated (Man)3(GlcNAc)2 + 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
R-Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
?
-
-
-
-
?
yeast mannan + H2O
?
-
-
-
-
?
additional information
?
-
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
-
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
-
-
-
?
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
-
-
-
-
?
GlcNAc(Man)5GlcNAc2 + H2O
GlcNAc(Man)3GlcNAc2 + D-mannose
-
alpha-mannosidase IIx protein
-
-
?
Man5GlcNAc2 + H2O
Man3GlcNAc2 + 2 alpha-D-mannopyranose
-
-
-
-
?
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
?
-
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
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: 4-nitrophenyl alpha-mannoside
-
-
?
additional information
?
-
-
not: 4-nitrophenyl alpha-mannoside
-
-
?
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
?
-
-
not: (Man)5(GlcNAc)2
-
-
?
additional information
?
-
-
not: (Man)5(GlcNAc)2
-
-
?
additional information
?
-
-
asparagine-linked glycoprotein biosynthesis
-
-
?
additional information
?
-
-
-
-
-
?
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
?
-
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
?
-
-
substrate specificity, overview
-
-
?
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
?
-
-
-
-
-
?
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
?
-
-
-
-
-
?
additional information
?
-
domain structure
-
-
?
additional information
?
-
-
domain structure
-
-
?
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
?
-
-
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
?
-
-
-
-
-
?
additional information
?
-
-
domain structure
-
-
?
additional information
?
-
-
domain structure
-
-
?
additional information
?
-
-
not: (Man)9GlcNAc
-
-
?
additional information
?
-
-
not: GlcNAc(Man)3GlcNAc
-
-
?
additional information
?
-
-
not: (Man)5GlcNAc
-
-
?
additional information
?
-
-
not: (Man)5GlcNAc
-
-
?
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
?
-
-
not: (Man)5(GlcNAc)2
-
-
?
additional information
?
-
-
not: (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 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
?
-
-
not: (Man)5(GlcNAc)2
-
-
?
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
?
-
-
-
-
-
?
additional information
?
-
-
not: Glc3(Man)9GlcNAc
-
-
?
additional information
?
-
-
not: Glc3(Man)9GlcNAc
-
-
?
additional information
?
-
-
not: (Man)9GlcNAc
-
-
?
additional information
?
-
-
not: (Man)9GlcNAc
-
-
?
additional information
?
-
-
not: (Man)5GlcNAc
-
-
?
additional information
?
-
-
not: (Man)5GlcNAc
-
-
?
additional information
?
-
-
asparagine-linked glycoprotein biosynthesis
-
-
?
additional information
?
-
-
no hydrolysis of alpha1,6-linkages
-
-
?
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(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,5R)-4-amino-5-methoxycyclopentane-1,2,3-triol
-
(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,2R,3R,4S,5S)-1,2,3,4-tetrahydroxy-5-(N-benzylamino)cyclopentane
-
-
(1R,2R,3S,4R,5R)-5-aminocyclopentane-1,2,3,4-tetrol
-
(1R,2S,3R,4R,5R)-5-aminocyclopentane-1,2,3,4-tetraol
-
(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
(1S,2R,8R,8aR)-octahydroindolizine-1,2,8-triol
-
(2R,3R,4R,5R)-2-(hydroxymethyl)piperidine-3,4,5-triol
-
(2R,3R,4R,5R)-5-amino-2-(hydroxymethyl)piperidine-3,4-diol
-
(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,4R)-2-[(1R)-1-hydroxyethyl]pyrrolidine-3,4-diol
most active
(2R,3S,4S)-1-[(2S,3S)-2,4-dihydroxy-3-(sulfooxy)butyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
-
(2S,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
(2S,3R,4S)-2-[([(1R)-2-[(4-bromophenyl)(hydroxy)methoxy]-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
-
(3R,4R)-4-aminopyrrolidin-3-ol
-
(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)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-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
-
(RS)-2-phenylethyl alpha-D-mannopyranosyl sulfoxide
-
-
1,4-Dideoxy-1,4-imino-D-mannitol
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-deoxyamino-cyclopentitetrol
-
-
1-deoxyaminocyclopentitetrol
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
2-phenylethyl alpha-D-mannopyranosyl sulfone
-
-
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
5-thio-alpha-D-mannopyranosylamine
-
6-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
-
in decreasing order of efficiency: alpha1,2, alpha 1,3 and alpha1,6-mannosylmannose
8,8a-di-epi-swainsonine
-
-
alpha-1,6-linked trisaccharide of mannose
-
1.5 mM, 40% inhibition
BAPTA
-
i.e. 1,2-bis(2-aminophenoxy) ethane N,N,N',N'-tetraacetic acid
benzyl alpha-D-mannopyranosyl sulfone
-
-
D-mannonolactam amidrazone
di-epi-swainsonine
weak inhibitor
diastereomer of salacinol
-
diastereomer of seleno-salacinol
-
EGTA
-
ethylene glycol-bis(beta-aminoethylether)-N,N,N',N'-tetraacetic acid
Fe3+
-
less potent inhibitor than Fe2+ and Cu2+, 1 mM, 24-30% inhibition
gluco-hydroxyiminolactam
-
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
mannose
-
250 mM, 30% inhibition
mannostatin B
strong inhibitor, reversible, competitive
Mannosyl-mannose disaccharide
-
in decreasing order of efficiency: alpha1,2, alpha 1,3 and alpha1,6-mannosylmannose
-
meso-aminocyclopentitretrol
-
-
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
N-octyl-6-epi-valienamine
-
N-[(R)-amino(phenyl)methyl]-5-thio-alpha-D-mannopyranosylamine
-
p-chloromercuriphenylsulfonate
phosphatidylinositol
-
CaCl2 or NaCl restores
[[(3S,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-ylidene]amino] N-(4-chlorophenyl)carbamate
-
(2R,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
(2R,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
-
(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
1,4-Dideoxy-1,4-imino-D-mannitol
-
-
1,4-Dideoxy-1,4-imino-D-mannitol
-
-
1,4-Dideoxy-1,4-imino-D-mannitol
-
-
1,4-Dideoxy-1,4-imino-D-mannitol
-
-
1,4-Dideoxy-1,4-imino-D-mannitol
-
-
1,4-Dideoxy-1,4-imino-D-mannitol
-
much less effective than swainsonine
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-deoxyaminocyclopentitetrol
poor inhibitor
1-deoxymannojirimycin
-
more inhibitory than kifunensine, mode of binding
1-deoxymannojirimycin
-
complete inhibition at 0.5 mM
1-deoxymannojirimycin
-
61% inhibition of the activity of the liver lysosomal fraction at pH 4.0, 37% at pH 6.5, at 1 mM
1-deoxymannojirimycin
-
-
1-deoxymannojirimycin
-
0.4 mM, 50% inhibition
Co2+
2 mM, strong inhibition
Cu2+
over 97% inhibition of the recombinant GMII at 1 mM
Cu2+
-
1 mM, 50% inhibition
Cu2+
-
20 mM, 90% inhibition
Cu2+
2 mM, strong inhibition
Cu2+
-
complete inhibition at 1 mM
Cu2+
-
completely inhibits
Cu2+
-
1 mM, 91-93% inhibition; strong
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
Cu2+
-
0.2 mM CuCl2, 75% inhibition
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
deoxymannojirimycin
-
EDTA
-
10 mM
EDTA
-
20 mM, 20% inhibition
EDTA
2 mM, strong inhibition
EDTA
-
26% inhibition at 1 mM
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
Fe2+
-
1 mM, 70-76% inhibition; strong
kifunensine
-
weak, mode of binding
kifunensine
-
complete inhibition at 0.5 mM
mannostatin
-
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
strong inhibitor, reversible, competitive
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
Mn2+
-
-
noeuromycin
-
-
p-chloromercuriphenylsulfonate
-
-
p-chloromercuriphenylsulfonate
-
1 mM, 80% inhibition
swainsonine
50% inhibition of recombinant GMII at 18 nM
swainsonine
-
30 nM, 85% inhibition
swainsonine
-
competitve inhibitor
swainsonine
-
mode of binding; very strong
swainsonine
competitve inhibitor
swainsonine
most powerful inhibitor
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
-
competitve inhibitor
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
swainsonine
-
20 nM, 50% inhibition
swainsonine
-
alpha-mannosidase III, IC50: 10 nM
swainsonine
binding structure, overview
swainsonine
-
i.e. (1S,2R,8R,8aR)-trihydroxyindolizidine; very strong
swainsonine
-
very strong
Zn2+
-
9% inhibition at 1 mM
Zn2+
-
10 mM: 40% inhibition, 2.5 mM: no inhibition
Zn2+
-
alpha-mannosidase III
additional information
no inhibition of recombinant GMII by EDTA
-
additional information
-
no inhibition of recombinant GMII by EDTA
-
additional information
-
not inhibited by EDTA
-
additional information
-
not inhibited by Ca2+; not inhibited by Mn2+, Mg2+
-
additional information
-
not inhibited by N-acetylmannostatin A
-
additional information
-
simulations of ligand/inhibitor binding
-
additional information
inhibitor synthesis, overview
-
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 alpha-D-mannose
-
additional information
-
no inhibition by Mg2+
-
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
-
not inhibited by N-acetylmannostatin A
-
additional information
-
not inhibited by Tris-maleate
-
additional information
-
-
-
additional information
-
not inhibited by EDTA
-
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+
-
additional information
-
not inhibited by N-acetylmannostatin A
-
additional information
-
not inhibited by Mn2+, Mg2+
-
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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
0.0003
(1R,2R,3S,4R,5R)-5-aminocyclopentane-1,2,3,4-tetrol
-
0.0003
(1R,2S,3R,4R,5R)-5-aminocyclopentane-1,2,3,4-tetraol
-
0.00002
(1S,2R,8R,8aR)-octahydroindolizine-1,2,8-triol
20C, pH 6.8
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
0.265
1-deoxyamino-cyclopentitetrol
-
-
0.265
1-deoxyaminocyclopentitetrol
0.4 - 0.75
1-deoxymannojirimycin
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
0.02
8,8a-di-epi-swainsonine
-
liver lysosomal fraction
0.75
8a-epi-swainsonine
-
liver lysosomal fraction
0.4
deoxymannojirimycin
pH 5.6
0.07
gluco-hydroxyiminolactam
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
0.000249
N-benzyl mannostatin A
-
-
0.000249
N-benzyl-mannostatin
-
-
0.017
N-octyl-6-epi-valienamine
0.0000105 - 0.018
swainsonine
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
-
0.265
1-deoxyaminocyclopentitetrol
-
-
0.265
1-deoxyaminocyclopentitetrol
-
0.4
1-deoxymannojirimycin
-
0.75
1-deoxymannojirimycin
-
pH 5.5, liver lysosomal fraction
0.07
gluco-hydroxyiminolactam
-
0.07
gluco-hydroxyiminolactam
pH 5.6
0.013
glucoimidazole
-
0.013
glucoimidazole
pH 5.6
5
kifunensine
pH 5.6
5.2
kifunensine
-
pH 5.75, 37°C
0.002
mannoimidazole
-
0.002
mannoimidazole
pH 5.6
0.000036
Mannostatin A
-
-
0.017
N-octyl-6-epi-valienamine
-
0.017
N-octyl-6-epi-valienamine
pH 5.6
0.02
noeuromycin
-
0.0000105
swainsonine
-
pH 5.75, 37°C
0.00002
swainsonine
pH 5.6
0.003
swainsonine
pH 5.75, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.014
8-epi-lentiginosine
Drosophila melanogaster
-
2
benzyl alpha-D-mannopyranosyl sulfone
Homo sapiens
-
in 50 mM sodium acetate buffer pH 5.8, at 37°C
0.00009 - 0.0004
D-mannonolactam amidrazone
2
di-epi-swainsonine
Drosophila melanogaster
-
0.00001 - 0.00013
Mannostatin A
0.000005 - 0.00005
swainsonine
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
0.05
(2S,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
Homo sapiens
-
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
0.075
(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 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
0.0005
(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 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
0.0004
D-mannonolactam amidrazone
Canis lupus familiaris
-
IC50: 400 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
0.00013
Mannostatin A
Homo sapiens
-
in 50 mM sodium acetate buffer pH 5.8, at 37°C
0.000005
swainsonine
Homo sapiens
-
in 50 mM sodium acetate buffer pH 5.8, at 37°C
0.00001
swainsonine
Spodoptera frugiperda
-
alpha-mannosidase III, IC50: 10 nM
0.00001
swainsonine
Homo sapiens
-
extracted from endothelial cells HCEC
0.000017
swainsonine
Drosophila melanogaster
-
0.00002
swainsonine
Homo sapiens
-
extracted from human glioblastoma cells LNZ308
0.000037
swainsonine
Drosophila melanogaster
pH 5.75, 25°C
0.00005
swainsonine
Homo sapiens
-
extracted from human glioblastoma cells LN18
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Moremen, K.W.; Touster, O.; Robbins, P.W.
Novel purification of the catalytic domain of golgi alpha-mannosidase II. Characterization and comparison with the intact enzyme
J. Biol. Chem.
266
16876-16885
1991
Rattus norvegicus
brenda
Tulsiani, D.R.P.; Hubbard, S.C.; Robbins, P.W.; Touster, O.
alpha-D-Mannosidases of rat liver Golgi membranes. Mannosidase II is the GlcNAcMAN5-cleaving enzyme in glycoprotein biosynthesis and mannosidases Ia and IB are the enzymes converting Man9 precursors to Man5 intermediates
J. Biol. Chem.
257
3660-3668
1982
Rattus norvegicus
brenda
Tulsiani, D.R.P.; Opheim, D.J.; Touster, O.
Purification and characterization of alpha-D-mannosidase from rat liver golgi membranes
J. Biol. Chem.
252
3227-3233
1977
Rattus norvegicus
brenda
Amano, J.; Kobata, A.
Purification and characterization of a novel alpha-mannosidase from Aspergillus saitoi
J. Biochem.
99
1645-1654
1986
Aspergillus phoenicis
brenda
Chandrasekaran, E.V.; Savila, M.; Nixon, D.; Mendicino, J.
Purification and properties of alpha-D-mannose:beta-1,2-N-acetylglucosaminyl-transferases and alpha-D-mannosidases from human adenocarcinoma
Cancer Res.
44
4059-4068
1984
Homo sapiens
brenda
Forsee, W.T.
Characterization of microsomal and cytosolic alpha-1,2-mannosidases from mung bean hypocotyls
Arch. Biochem. Biophys.
242
48-57
1985
Vigna radiata var. radiata
brenda
Palamarczyk, G.; Mitchell, M.; Smith, P.W.; Fleet, G.W.; Elbein, A.D.
1,4-Dideoxy-1,4-imino-D-mannitol inhibits glycoprotein processing and mannosidase
Arch. Biochem. Biophys.
243
35-45
1985
Canis lupus familiaris
brenda
Kobata, A.; Amano, J.
alpha-Mannosidases I and II from Aspergillus saitoi
Methods Enzymol.
138
779-785
1987
Aspergillus phoenicis
brenda
Kaushal, G.P.; Elbein, A.D.
Glycoprotein processing enzymes of plants
Methods Enzymol.
179
452-475
1989
Vigna radiata
brenda
Forsee, W.T.; Palmer, C.F.; Schutzbach, J.S.
Purification and characterization of an alpha-1,2-mannosidase involved in processing asparagine-linked oligosaccharides
J. Biol. Chem.
264
3869-3876
1989
Oryctolagus cuniculus
brenda
Elbein, A.D.
Glycosidase inhibitors: inhibitors of N-linked oligosaccharide processing
FASEB J.
5
3055-3063
1991
plant, 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
Canis lupus familiaris, Vigna radiata
brenda
Shah, N.; Kuntz, D.A.; Rose, D.R.
Comparison of kifunensine and 1-deoxymannojirimycin binding to class I and II alpha-mannosidases demonstrates different saccharide distortions in inverting and retaining catalytic mechanisms
Biochemistry
42
13812-13816
2003
Drosophila melanogaster
brenda
Harpaz, N.; Schachter, H.
Control of glycoprotein synthesis. Processing of asparagine-linked oligosaccharides by one or more rat liver Golgi alpha-D-mannosidases dependent on the prior action of UDP-N-acetylglucosamine: alpha-D-mannoside beta 2-N-acetylglucosaminyltransferase I
J. Biol. Chem.
255
4894-4902
1980
Rattus norvegicus
brenda
Tulsiani, D.R.P.; Harris, T.M.; Touster, O.
Swainsonine inhibits the biosynthesis of complex glycoproteins by inhibition of Golgi mannosidase II
J. Biol. Chem.
257
7936-7939
1982
Rattus norvegicus
brenda
Tulsiani, D.R.P.; Broquist, H.P.; Touster, O.
Marked differences in the swainsonine inhibition of rat liver lysosomal alpha-D-mannosidase, rat liver Golgi mannosidase II, and jack bean alpha-D-mannosidase
Arch. Biochem. Biophys.
236
427-434
1985
Rattus norvegicus
brenda
Moremen, K.W.; Touster, O.
Topology of mannosidase II in rat liver Golgi membranes and release of the catalytic domain by selective proteolysis
J. Biol. Chem.
261
10945-10951
1986
Rattus norvegicus
brenda
Moremen, K.W.; Touster, O.
Biosynthesis and modification of Golgi mannosidase II in HeLa and 3T3 cells
J. Biol. Chem.
260
6654-6662
1985
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Kaushal, G.P.; Szumilo, T.; Pastuszak, I.; Elbein, A.D.
Purification to homogeneity and properties of mannosidase II from mung bean seedlings
Biochemistry
29
2168-2176
1990
Vigna radiata
brenda
Tropea, J.E.; Kaushal, G.P.; Pastuszak, I.; Mitchell, M.; Aoyagi, T.; Molyneux, R.J.; Elbein, A.D.
Mannostatin A, a new glycoprotein-processing inhibitor
Biochemistry
29
10062-10069
1990
Canis lupus familiaris, Vigna radiata
brenda
Baron, M.D.; Garoff, H.
Mannosidase II and the 135-kDa Golgi-specific antigen recognized monoclonal antibody 53FC3 are the same dimeric protein
J. Biol. Chem.
265
19928-19931
1990
Rattus norvegicus
brenda
Moremen, K.W.; Robbins, P.W.
Isolation, characterization, and expression of cDNAs encoding murine alpha-mannosidase II, a Golgi enzyme that controls conversion of high mannose to complex N-glycans
J. Cell Biol.
115
1521-1534
1991
Homo sapiens, Mus musculus (P27046), Mus musculus, Rattus norvegicus
brenda
Foster, J.M.; Yudkin, B.; Lockyer, A.E.; Roberts, D.B.
Cloning and sequence analysis of GmII, a Drosophila melanogaster homologue of the cDNA encoding murine Golgi alpha-mannosidase II
Gene
154
183-186
1995
Mus musculus, Drosophila melanogaster (Q24451), Drosophila melanogaster
brenda
Altmann, F.; Mrz, L.
Processing of asparagine-linked oligosaccharides in insect cells: evidence for alpha-mannosidase II
Glycoconj. J.
12
150-155
1995
Bombyx mori, Mamestra brassicae, Vigna radiata, Spodoptera frugiperda, Xenopus laevis, Spodoptera frugiperda Sf-21, Bombyx mori Bm-N, Mamestra brassicae Mb-0503
brenda
Ren, J.; Castellino, F.J.; Bretthauer, R.K.
Purification and properties of alpha-mannosidase II from Golgi-like membranes of baculovirus-infected Spodoptera frugiperda (IPLB-SF-21AE) cells
Biochem. J.
324
951-956
1997
Spodoptera frugiperda
brenda
Numao, S.; Kuntz, D.A.; Withers, S.G.; Rose, D.R.
Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural analysis of covalent reaction intermediates
J. Biol. Chem.
278
48074-48083
2003
Drosophila melanogaster (Q24451)
brenda
Moremen, K.W.
Golgi alpha-mannosidase II deficiency in vertebrate systems: implications for asparagine-linked oligosaccharide processing in mammals
Biochim. Biophys. Acta
1573
225-235
2002
Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Igdoura, S.A.; Herscovics, A.; Lal, A.; Moremen, K.W.; Morales, C.R.; Hermo, L.
alpha-Mannosidases involved in N-glycan processing show cell specificity and distinct subcompartmentalization within the Golgi apparatus of cells in the testis and epididymis
Eur. J. Cell Biol.
78
441-452
1999
Rattus norvegicus
brenda
Oh-Eda, M.; Nakagawa, H.; Akama, T.O.; Lowitz, K.; Misago, M.; Moremen, K.W.; Fukuda, M.N.
Overexpression of the Golgi-localized enzyme alpha-mannosidase IIx in Chinese hamster ovary cells results in the conversion of hexamannosyl-N-acetylchitobiose to tetramannosyl-N-acetylchitobiose in the N-glycan-processing pathway
Eur. J. Biochem.
268
1280-1288
2001
Homo sapiens
brenda
Francis, B.R.; Paquin, L.; Weinkauf, C.; Jarvis, D.L.
Biosynthesis and processing of Spodoptera frugiperda alpha-mannosidase III
Glycobiology
12
369-377
2002
Spodoptera frugiperda
brenda
Kawar, Z.; Karaveg, K.; Moremen, K.W.; Jarvis, D.L.
Insect cells encode a class II alpha-mannosidase with unique properties
J. Biol. Chem.
276
16335-16340
2001
Spodoptera frugiperda
brenda
Nakajima, M.; Fushinobu, S.; Imamura, H.; Shoun, H.; Wakagi, T.
Crystallization and preliminary X-ray analysis of cytosolic alpha-mannosidase from Thermotoga maritima
Acta Crystallogr. Sect. F
62
104-105
2006
Thermotoga maritima
brenda
Woo, K.K.; Miyazaki, M.; Hara, S.; Kimura, M.; Kimura, Y.
Purification and characterization of a co(II)-sensitive alpha-mannosidase from Ginkgo biloba seeds
Biosci. Biotechnol. Biochem.
68
2547-2556
2004
Ginkgo biloba
brenda
Woo, K.K.; Kimura, Y.
Regulation of substrate specificity of plant alpha-mannosidase by cobalt ion: in vitro hydrolysis of high-mannose type N-glycans by Co2+-activated Ginkgo alpha-mannosidase
Biosci. Biotechnol. Biochem.
69
1111-1119
2005
Ginkgo biloba
brenda
Athanasopoulos, V.I.; Niranjan, K.; Rastall, R.A.
The production, purification and characterization of two novel alpha-D-mannosidases from Aspergillus phoenicis
Carbohydr. Res.
340
609-617
2005
Aspergillus phoenicis
brenda
Li, B.; Kawatkar, S.P.; George, S.; Strachan, H.; Woods, R.J.; Siriwardena, A.; Moremen, K.W.; Boons, G.J.
Inhibition of Golgi mannosidase II with mannostatin A analogues: synthesis, biological evaluation, and structure-activity relationship studies
Chembiochem
5
1220-1227
2004
Homo sapiens
brenda
Siriwardena, A.; Strachan, H.; El-Daher, S.; Way, G.; Winchester, B.; Glushka, J.; Moremen, K.; Boons, G.
Potent and selective inhibition of class II alpha-D-mannosidase activity by a bicyclic sulfonium salt
ChemBioChem
6
845-848
2005
Homo sapiens
brenda
Kawatkar, S.P.; Kuntz, D.A.; Woods, R.J.; Rose, D.R.; Boons, G.J.
Structural basis of the inhibition of Golgi alpha-mannosidase II by mannostatin A and the role of the thiomethyl moiety in ligand-protein interactions
J. Am. Chem. Soc.
128
8310-8319
2006
Drosophila melanogaster
brenda
Strasser, R.; Schoberer, J.; Jin, C.; Gloessl, J.; Mach, L.; Steinkellner, H.
Molecular cloning and characterization of Arabidopsis thaliana Golgi alpha-mannosidase II, a key enzyme in the formation of complex N-glycans in plants
Plant J.
45
789-803
2006
Arabidopsis thaliana (Q9LFR0), Arabidopsis thaliana
brenda
Kuntz, D.A.; Ghavami, A.; Johnston, B.D.; Pinto, B.M.; Rose, D.R.
Crystallographic analysis of the interactions of Drosophila melanogaster Golgi alpha-mannosidase II with the naturally occurring glycomimetic salacinol and its analogues
Tetrahedron Asymmetry
16
25-32
2005
Drosophila melanogaster (Q24451)
-
brenda
Ferrara, C.; Bruenker, P.; Suter, T.; Moser, S.; Puentener, U.; Umana, P.
Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous beta1,4-N-acetylglucosaminyltransferase III and Golgi alpha-mannosidase II
Biotechnol. Bioeng.
93
851-861
2006
Homo sapiens
brenda
Kuntz, D.A.; Liu, H.; Bols, M.; Rose, D.R.
The role of the active site Zn in the catalytic mechanism of the GH38 Golgi alpha -mannosidase II: implications from noeuromycin inhibition
Biocatal. Biotransform.
24
55-61
2006
Drosophila melanogaster
-
brenda
Crispin, M.; Aricescu, A.R.; Chang, V.T.; Jones, E.Y.; Stuart, D.I.; Dwek, R.A.; Davis, S.J.; Harvey, D.J.
Disruption of alpha-mannosidase processing induces non-canonical hybrid-type glycosylation
FEBS Lett.
581
1963-1968
2007
Homo sapiens
brenda
Kuokkanen, E.; Smith, W.; Maekinen, M.; Tuominen, H.; Puhka, M.; Jokitalo, E.; Duvet, S.; Berg, T.; Heikinheimo, P.
Characterization and subcellular localization of human neutral class II alpha-mannosidase cytosolic enzymes/free oligosaccharides/glycosidehydrolase family 38/M2C1/N-glycosylation
Glycobiology
17
1084-1093
2007
Homo sapiens
brenda
Akama, T.O.; Fukuda, M.N.
N-Glycan structure analysis using lectins and an alpha-mannosidase activity assay
Methods Enzymol.
416
304-314
2006
Mus musculus
brenda
Akama, T.O.; Nakagawa, H.; Wong, N.K.; Sutton-Smith, M.; Dell, A.; Morris, H.R.; Nakayama, J.; Nishimura, S.; Pai, A.; Moremen, K.W.; Marth, J.D.; Fukuda, M.N.
Essential and mutually compensatory roles of {alpha}-mannosidase II and {alpha}-mannosidase IIx in N-glycan processing in vivo in mice
Proc. Natl. Acad. Sci. USA
103
8983-8988
2006
Mus musculus
brenda
Englebienne, P.; Fiaux, H.; Kuntz, D.A.; Corbeil, C.R.; Gerber-Lemaire, S.; Rose, D.R.; Moitessier, N.
Evaluation of docking programs for predicting binding of Golgi alpha-mannosidase II inhibitors: a comparison with crystallography
Proteins
69
160-176
2007
Drosophila melanogaster (Q24451)
brenda
Kumar, N.S.; Kuntz, D.A.; Wen, X.; Pinto, B.M.; Rose, D.R.
Binding of sulfonium-ion analogues of di-epi-swainsonine and 8-epi-lentiginosine to Drosophila Golgi alpha-mannosidase II: The role of water in inhibitor binding
Proteins
71
1484-1496
2008
Drosophila melanogaster (Q24451)
brenda
Chida, K.; Taguchi, M.
Change in localization of alkaline phosphatase and mannosidase II by colchicine treatment of primary cultures of fetal rat hepatocytes
Acta Histochem. Cytochem.
41
1-5
2008
Rattus norvegicus
brenda
Kuntz, D.A.; Tarling, C.A.; Withers, S.G.; Rose, D.R.
Structural analysis of Golgi alpha-mannosidase II inhibitors identified from a focused glycosidase inhibitor screen
Biochemistry
47
10058-10068
2008
Drosophila melanogaster (Q24451)
brenda
Fiaux, H.; Kuntz, D.A.; Hoffman, D.; Janzer, R.C.; Gerber-Lemaire, S.; Rose, D.R.; Juillerat-Jeanneret, L.
Functionalized pyrrolidine inhibitors of human type II alpha-mannosidases as anti-cancer agents: optimizing the fit to the active site
Bioorg. Med. Chem.
16
7337-7346
2008
Canavalia ensiformis, Drosophila melanogaster, Drosophila melanogaster (Q24451), Homo sapiens
brenda
Kuntz, D.A.; Zhong, W.; Guo, J.; Rose, D.R.; Boons, G.J.
The molecular basis of inhibition of Golgi alpha-mannosidase II by mannostatin A
ChemBioChem
10
268-277
2009
Drosophila melanogaster, Drosophila melanogaster (Q24451)
brenda
Zhong, W.; Kuntz, D.A.; Ember, B.; Singh, H.; Moremen, K.W.; Rose, D.R.; Boons, G.J.
Probing the substrate specificity of Golgi alpha-mannosidase II by use of synthetic oligosaccharides and a catalytic nucleophile mutant
J. Am. Chem. Soc.
130
8975-8983
2008
Drosophila melanogaster, Drosophila melanogaster (Q24451)
brenda
Shah, N.; Kuntz, D.A.; Rose, D.R.
Golgi alpha-mannosidase II cleaves two sugars sequentially in the same catalytic site
Proc. Natl. Acad. Sci. USA
105
9570-9575
2008
Drosophila melanogaster (Q24451), Drosophila melanogaster
brenda
Bello, C.; Cea, M.; Bello, G.D.; Garuti, A.; Rocco, I.; Cirmena, G.; Moran, E.; Nahimana, A.; Duchosal, M.A.; Fruscione, F.; Pronzato, P.; Grossi, F.; Patrone, F.; Ballestrero, A.; Dupuis, M.; Sordat, B.; Nencioni, A.; Vogel, P.
Novel 2-[(benzylamino)methyl]pyrrolidine-3,4-diol derivatives as alpha-mannosidase inhibitors and with antitumor activities against hematological and solid malignancies
Bioorg. Med. Chem.
18
3320-3334
2010
Homo sapiens
brenda
Kuntz, D.A.; Nakayama, S.; Shea, K.; Hori, H.; Uto, Y.; Nagasawa, H.; Rose, D.R.
Structural investigation of the binding of 5-substituted swainsonine analogues to Golgi alpha-mannosidase II
ChemBioChem
11
673-680
2010
Drosophila melanogaster (Q24451)
brenda
Li, Y.; Fang, W.; Zhang, L.; Ouyang, H.; Zhou, H.; Luo, Y.; Jin, C.
Class IIC alpha-mannosidase AfAms1 is required for morphogenesis and cellular function in Aspergillus fumigatus
Glycobiology
19
624-632
2009
Aspergillus fumigatus (Q5I5K3), Aspergillus fumigatus, Aspergillus fumigatus YJ-407 (Q5I5K3)
brenda
Crispin, M.; Chang, V.T.; Harvey, D.J.; Dwek, R.A.; Evans, E.J.; Stuart, D.I.; Jones, E.Y.; Lord, J.M.; Spooner, R.A.; Davis, S.J.
A human embryonic kidney 293T cell line mutated at the Golgi alpha-mannosidase II locus
J. Biol. Chem.
284
21684-21695
2009
Homo sapiens
brenda
Shashidhara, K.S.; Gaikwad, S.M.
Conformational and functional transitions in class II alpha-mannosidase from Aspergillus fischeri
J. Fluoresc.
20
827-836
2010
Aspergillus fischeri
brenda
Zhu, Y.; Suits, M.D.; Thompson, A.J.; Chavan, S.; Dinev, Z.; Dumon, C.; Smith, N.; Moremen, K.W.; Xiang, Y.; Siriwardena, A.; Williams, S.J.; Gilbert, H.J.; Davies, G.J.
Mechanistic insights into a Ca2+-dependent family of alpha-mannosidases in a human gut symbiont
Nat. Chem. Biol.
6
125-132
2010
Homo sapiens
brenda
Suits, M.D.; Zhu, Y.; Taylor, E.J.; Walton, J.; Zechel, D.L.; Gilbert, H.J.; Davies, G.J.
Structure and kinetic investigation of Streptococcus pyogenes family GH38 alpha-mannosidase
PLoS ONE
5
e9006
2010
Streptococcus pyogenes M1 GAS (Q99YP5)
brenda
Polakova, M.; Sestak, S.; Lattova, E.; Petrus, L.; Mucha, J.; Tvaroska, I.; Kona, J.
alpha-D-mannose derivatives as models designed for selective inhibition of Golgi alpha-mannosidase II
Eur. J. Med. Chem.
46
944-952
2011
Homo sapiens
brenda
Petersen, L.; Ardevol, A.; Rovira, C.; Reilly, P.J.
Molecular mechanism of the glycosylation step catalyzed by Golgi alpha-mannosidase II: a QM/MM metadynamics investigation
J. Am. Chem. Soc.
132
8291-8300
2010
Drosophila melanogaster (Q24451)
brenda
Cheng, T.; Chan, T.; Tsou, E.; Chang, S.; Yun, W.; Yang, P.; Wu, Y.; Cheng, W.
From natural product-inspired pyrrolidine scaffolds to the development of new human Golgi alpha-mannosidase II inhibitors
Chemistry
8
2600-2604
2013
Homo sapiens
-
brenda
Rose, D.R.
Structure, mechanism and inhibition of Golgi alpha-mannosidase II
Curr. Opin. Struct. Biol.
22
558-562
2012
Drosophila melanogaster
brenda
Lu, H.; Wang, S.S.; Wang, W.L.; Zhang, L.; Zhao, B.Y.
Effect of swainsonine in Oxytropis kansuensis on Golgi alpha-mannosidase II expression in the brain tissues of Sprague-Dawley rats
J. Agric. Food Chem.
62
7407-7412
2014
Rattus norvegicus
brenda
Li, J.; Zhang, J.; Lai, B.; Zhao, Y.; Li, Q.
Cloning, expression, and characterization of Capra hircus Golgi alpha-mannosidase II
Appl. Biochem. Biotechnol.
177
1241-1251
2015
Capra hircus (V9XY47)
brenda
Suzuki, K.; Yamada, T.; Yamazaki, K.; Hirota, M.; Ishihara, N.; Sakamoto, M.; Takahashi, D.; Iijima, H.; Hase, K.
Intestinal epithelial cell-specific deletion of alpha-mannosidase II ameliorates experimental colitis
Cell Struct. Funct.
43
25-39
2018
Mus musculus (P27046)
brenda
Bobovska, A.; Tvaro?ka, I.; Kona, J.
Using DFT methodology for more reliable predictive models Design of inhibitors of Golgi alpha-mannosidase II
J. Mol. Graph. Model.
66
47-57
2016
Homo sapiens
brenda