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Information on EC 3.2.1.18 - exo-alpha-sialidase and Organism(s) Homo sapiens and UniProt Accession Q9UQ49

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EC Tree
IUBMB Comments
The enzyme does not act on 4-O-acetylated sialic acids. endo-alpha-Sialidase activity is listed as EC 3.2.1.129, endo-alpha-sialidase. See also EC 4.2.2.15 anhydrosialidase.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q9UQ49
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
neuraminidase, sialidase, glycosyl hydrolase, trans-sialidase, hemagglutinin-neuraminidase, major surface antigen, alpha2,6-sialyltransferase, cytosolic sialidase, endosialidase, neuraminidase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-N-acylneuraminate glycohydrolase
-
exo-alpha-sialidase
-
exo-sialidase
-
Ganglioside sialidase
-
ganglioside-specific sialidase
-
glycosyl hydrolase
-
Membrane sialidase
-
N-acetyl-alpha-neuraminidase 3
-
neuramindase
-
neuraminidase
-
neuraminidase 3
-
sialidase-3
-
acetylneuraminidase
-
-
-
-
Acetylneuraminyl hydrolase
acid sialidase
-
-
acylneuraminyl glycohydrolase
-
-
-
-
alpha-N-acylneuraminate glycohydrolase
-
alpha-neuraminidase
-
-
-
-
Cytosolic sialidase
exo-alpha-sialidase
-
G9 sialidase
Ganglioside sialidase
-
-
-
-
ganglioside-specific sialidase
-
-
HsNEU2
-
-
Lysosomal sialidase
Major 85 kDa surface antigen
-
-
-
-
Major surface antigen
-
-
-
-
Membrane sialidase
-
-
-
-
Mouse skeletal muscle sialidase
-
-
-
-
MSS
-
-
-
-
MTS
-
-
-
-
mucopolysaccharide N-acetylneuraminylhydrolase
-
-
-
-
Murine thymic sialidase
-
-
-
-
N-acetyl-alpha-neuraminidase 1
-
N-acetyl-alpha-neuraminidase 2
-
N-acetyl-alpha-neuraminidase 4
-
N-acylneuraminate glycohydrolase
-
-
-
-
N-acylneuraminosyl glycohydrolase
-
NANase
-
-
-
-
NEU4 long
-
-
NEU4 short
-
-
NEU4L
-
-
Neu4L sialidase
-
-
neuraminidase
neuraminidase 2
-
-
neuraminidase-1
-
-
SA85-1.1 protein
-
-
-
-
SA85-1.2 protein
-
-
-
-
SA85-1.3 protein
-
-
-
-
sialidase
sialidase Neu2
-
sialidase-2
-
sialidase-4
-
STNA
-
-
-
-
trans-sialidase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates
show the reaction diagram
catalytic mechanism, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
acetylneuraminyl hydrolase
The enzyme does not act on 4-O-acetylated sialic acids. endo-alpha-Sialidase activity is listed as EC 3.2.1.129, endo-alpha-sialidase. See also EC 4.2.2.15 anhydrosialidase.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-67-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferol + alpha-D-N-acetylneuraminic acid
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + N-acetylneuraminic acid
show the reaction diagram
ganglioside GD1a + H2O
?
show the reaction diagram
-
-
-
?
ganglioside GD1a + H2O
sialic acid + ganglioside GM1
show the reaction diagram
-
-
-
?
ganglioside GD1b + H2O
?
show the reaction diagram
-
-
-
?
ganglioside GM1 + H2O
?
show the reaction diagram
-
-
-
?
ganglioside GM3 + H2O
?
show the reaction diagram
-
-
-
?
ganglioside GT1b + H2O
?
show the reaction diagram
-
-
-
?
lactosyl-ceramide + H2O
?
show the reaction diagram
-
-
-
?
octyl-ganglioside GM3 + H2O
?
show the reaction diagram
-
-
-
?
octyl-lactoside + H2O
?
show the reaction diagram
-
-
-
?
(N-glycolylneuraminic acid)(alpha2,3)Galbeta-p-nitrophenol + H2O
N-glycolylneuraminic acid + 4-nitrophenol + ?
show the reaction diagram
-
-
-
-
?
(N-glycolylneuraminic acid)(alpha2,6)Galbeta-p-nitrophenol + H2O
N-glycolylneuraminic acid + 4-nitrophenol + ?
show the reaction diagram
-
-
-
-
?
2'-(4-methyl-umbelliferyl) alpha-D-N-acetylneuraminic acid + H2O
4-methyl-umbelliferol + alpha-D-N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
2'-(4-methylumbelliferyl) 9-O-acetyl-alpha-D-N-acetylneuraminic acid + H2O
4-methyl-umbelliferone + 9-O-acetyl-alpha-D-N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
2'-(4-methylumbelliferyl) alpha-D-N-acetylneuraminic acid + H2O
4-methyl-umbelliferone + alpha-D-N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
2'-(4-methylumbelliferyl) alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
2'-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid + H2O
4-methyl-umbelliferone + alpha-D-N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
2-(3-methoxyphenyl)-N-acetylneuraminic acid + H2O
3-methoxyphenol + N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferol + alpha-D-N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + alpha-D-N-acetylneuraminic acid
show the reaction diagram
-
about 1% activity compared to ganglioside GD3
-
-
?
4-methylumbelliferyl alpha-N-acetylneuraminic acid + H2O
4-methylumbelliferone + alpha-N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl alpha-NeuAc + H2O
4-methylumbelliferone + alpha-neuAc
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferol + alpha-D-N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + alpha-D-N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + N-acetylneuraminic acid
show the reaction diagram
5-acetylneuraminic acid-(alpha2,3)Galbeta-4-nitrophenol + H2O
N-acetylneuraminic acid + 4-nitrophenol + ?
show the reaction diagram
-
-
-
-
?
5-acetylneuraminic acid-(alpha2,6)Galbeta-4-nitrophenol + H2O
N-acetylneuraminic acid + 4-nitrophenol + ?
show the reaction diagram
-
-
-
-
?
5-azidoacetylneuraminic acid-(alpha2,3)Galbeta-4-nitrophenol + H2O
N-azidoacetylneuraminic acid + 4-nitrophenol + ?
show the reaction diagram
-
-
-
-
?
5-azidoacetylneuraminic acid-(alpha2,6)Galbeta-4-nitrophenol + H2O
N-azidoacetylneuraminic acid + 4-nitrophenol + ?
show the reaction diagram
-
-
-
-
?
5-fluoroacetylneuraminic acid-(alpha2,3)Galbeta-4-nitrophenol + H2O
N-fluoroacetylneuraminic acid + 4-nitrophenol + ?
show the reaction diagram
-
-
-
-
?
5-fluoroacetylneuraminic acid-(alpha2,6)Galbeta-4-nitrophenol + H2O
N-fluoroacetylneuraminic acid + 4-nitrophenol + ?
show the reaction diagram
-
-
-
-
?
alpha(2-3)sialyl-lactose + H2O
?
show the reaction diagram
-
-
-
?
alpha(2-3)sialyllactose + H2O
sialic acid + lactose
show the reaction diagram
-
-
-
-
?
alpha(2-3)sialylparagloboside + H2O
?
show the reaction diagram
-
-
-
-
?
alpha(2-6)-sialyllactose + H2O
sialic acid + lactose
show the reaction diagram
-
-
-
-
?
alpha-acid glycoprotein + H2O
?
show the reaction diagram
-
-
-
-
?
alpha2,3-sialyllactose + H2O
sialic acid + lactose
show the reaction diagram
-
-
-
-
?
bovine gland submaxillary gland mucin + H2O
?
show the reaction diagram
-
-
-
-
?
colominic acid + H2O
?
show the reaction diagram
-
-
-
-
?
fetuin + H2O
?
show the reaction diagram
ganglioside GD1a + H2O
?
show the reaction diagram
-
-
-
-
?
ganglioside GD1a + H2O
ganglioside GM1 + sialic acid
show the reaction diagram
ganglioside GD1a + H2O
sialic acid + ganglioside GM1
show the reaction diagram
-
-
-
?
ganglioside GD1b + H2O
?
show the reaction diagram
-
-
-
-
?
ganglioside GD3 + H2O
?
show the reaction diagram
-
-
-
-
?
ganglioside GD3 + H2O
N-acetylneuraminate + ganglioside GM3
show the reaction diagram
-
100% activity
-
-
?
ganglioside GM1 + H2O
?
show the reaction diagram
-
-
-
-
?
ganglioside GM2 + H2O
?
show the reaction diagram
-
-
-
-
?
ganglioside GM3 + H2O
?
show the reaction diagram
-
-
-
-
?
ganglioside GM3 + H2O
N-acetylneuraminate + beta-D-galactosyl-(1->4)-beta-D-glucosylceramide
show the reaction diagram
ganglioside GT1 + H2O
?
show the reaction diagram
-
-
-
-
?
ganglioside GT1b + H2O
?
show the reaction diagram
-
-
-
-
?
monosialoganglioside GM3 + H2O
?
show the reaction diagram
-
-
-
?
N-acetylneuraminic acid-alpha-2,3-lactose + H2O
N-acetylneuraminic acid + lactose
show the reaction diagram
-
-
-
-
?
N-acetylneuraminic acid-alpha-2,6-lactose + H2O
N-acetylneuraminic acid + lactose
show the reaction diagram
-
-
-
-
?
N-acetylneuraminyllactose + H2O
N-acetylneuraminic acid + lactose
show the reaction diagram
-
-
-
-
?
N-glycoloylneuraminic acid-alpha-2,3-lactose + H2O
?
show the reaction diagram
-
-
-
-
?
Neu5(4-[(2,4-dinitrophenoxy)methyl]-1H-1,2,3-triazol-1-yl)Ac-alpha-(2->3)-Gal-beta--(1->4)-Glc-beta-n-octyl + H2O
?
show the reaction diagram
-
-
-
-
?
Neu5(azido)Ac-alpha-(2->3)-Gal-beta--(1->4)-Glc-beta-n-octyl + H2O
?
show the reaction diagram
-
-
-
-
?
Neu5Ac-alpha-(2->3)-Gal-beta--(1->4)-Glc-beta-(CH2)8COOCH3 + H2O
?
show the reaction diagram
-
-
-
-
?
Neu5Ac-alpha-(2->3)-Gal-beta--(1->4)-Glc-beta-CH2(CH3)CH2CH2CH3 + H2O
?
show the reaction diagram
-
-
-
-
?
Neu5Ac-alpha-(2->3)-Gal-beta--(1->4)-Glc-beta-CH2Ph + H2O
?
show the reaction diagram
-
-
-
-
?
Neu5Ac-alpha-(2->3)-Gal-beta--(1->4)-Glc-beta-n-butyl + H2O
?
show the reaction diagram
-
-
-
-
?
Neu5Ac-alpha-(2->3)-Gal-beta--(1->4)-Glc-beta-n-octyl + H2O
?
show the reaction diagram
-
-
-
-
?
Neu5Ac-alpha-(2->3)-Gal-beta--(1->4)-Glc-beta-N3 + H2O
?
show the reaction diagram
-
-
-
-
?
Neu5Ac9(2,4-dinitrobenzoyl)N-alpha-(2->3)-Gal-beta--(1->4)-Glc-beta-n-octyl + H2O
?
show the reaction diagram
-
-
-
-
?
Neu5Ac9N-alpha-(2->3)-Gal-beta--(1->4)-Glc-beta-n-octyl + H2O
?
show the reaction diagram
-
-
-
-
?
Neu5Ac9N3-alpha-(2->3)-Gal-beta--(1->4)-Glc-beta-n-octyl + H2O
?
show the reaction diagram
-
-
-
-
?
Neu5Acalpha(2->3)Galbeta-4-nitrophenyl + H2O
?
show the reaction diagram
-
-
-
?
Neu5Acalpha(2->6)Galbeta4-nitrophenyl + H2O
?
show the reaction diagram
-
-
-
?
O-(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galactonon-2-ulopyranosylonic acid)-(2->3)-O-(beta-D-galactopyranosyl)-(1->4)-O-(beta-D-glucopyranosyl)-octanol + H2O
?
show the reaction diagram
-
-
-
-
?
O-(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galactonon-2-ulopyranosylonic acid)-(2->6)-O-(beta-D-galactopyranosyl)-(1->4)-O-(beta-D-glucopyranosyl)-octanol + H2O
?
show the reaction diagram
-
-
-
-
?
O-(5-acetamido-9-O-acetyl-3,5-dideoxy-D-glycero-alpha-D-galactonon-2-ulopyranosylonic acid)-(2->3)-O-(beta-D-galactopyranosyl)-(1->4)-O-(beta-D-glucopyranosyl)-octanol + H2O
?
show the reaction diagram
-
-
-
-
?
O-(5-acetamido-9-O-acetyl-3,5-dideoxy-D-glycero-alpha-D-galactonon-2-ulopyranosylonic acid)-(2->6)-O-(beta-D-galactopyranosyl)-(1->4)-O-(beta-D-glucopyranosyl)-octanol + H2O
?
show the reaction diagram
-
-
-
-
?
O-(5-glycolylamido-3,5,-dideoxy-D-glycero-alpha-D-galactonon-2-ulopyranosylonic acid)-(2->3)-O-(beta-D-galactopyranosyl)-(1->4)-O-(beta-D-glucopyranosyl)-octanol + H2O
?
show the reaction diagram
-
-
-
-
?
O-(5-glycolylamido-3,5,-dideoxy-D-glycero-alpha-D-galactonon-2-ulopyranosylonic acid)-(2->6)-O-(beta-D-galactopyranosyl)-(1-> 4)-O-(beta-D-glucopyranosyl)-octanol + H2O
?
show the reaction diagram
-
-
-
-
?
orosomucoid + H2O
?
show the reaction diagram
-
-
-
-
?
siallyllactose + H2O
?
show the reaction diagram
-
about 7% activity compared to ganglioside GD3
-
-
?
sialyl-alpha-2,3-lactose + H2O
?
show the reaction diagram
-
-
-
-
?
sialyl-alpha-2,6-lactose + H2O
?
show the reaction diagram
-
-
-
-
?
sialyloligosaccharides + H2O
?
show the reaction diagram
-
-
-
-
?
transferrin + H2O
?
show the reaction diagram
-
-
-
-
?
vesicular GM3 + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ganglioside GD1a + H2O
?
show the reaction diagram
-
-
-
?
ganglioside GM1 + H2O
?
show the reaction diagram
-
-
-
?
ganglioside GM3 + H2O
?
show the reaction diagram
-
-
-
?
lactosyl-ceramide + H2O
?
show the reaction diagram
-
-
-
?
alpha(2-3)sialyl-lactose + H2O
?
show the reaction diagram
-
-
-
?
alpha(2-6)-sialyllactose + H2O
sialic acid + lactose
show the reaction diagram
-
-
-
-
?
fetuin + H2O
?
show the reaction diagram
-
-
-
?
ganglioside GD1a + H2O
ganglioside GM1 + sialic acid
show the reaction diagram
-
i.e. NeuAcalpha(2-3)-Galbeta(1-3)-GalNAcbeta(1-4)-NeuAcalpha(2-3)-Galbeta(1-4)-Glcbeta(1-1)-Cer, isozyme Neu-3, no activity with Neu-1
-
-
?
monosialoganglioside GM3 + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Br-
-
activates
Ca2+
-
stimulates the activity of the enzyme
Cl-
-
activates up to 1 M
K+
-
slight activation up to 0.01 mM
Mg2+
-
required
Na+
-
slight activation up to 0.01 mM
NO3-
-
activates
S2O42-
-
activates
SO32-
-
activates
SO42-
-
activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-dehydro-2-deoxy-N-acetylneuraminic acid
competitive inhibitor
2-deoxy-2,3-dehydro-N-acetylneuraminic acid
4,5-diacetamido-2-fluorobenzoic acid
23% inhibition of isoform NEU3 at 1 mM
4-acetamido-5-(2-naphthamido)-2-fluorobenzoic acid
8% inhibition of isoform NEU3 at 1 mM
4-acetamido-5-(biphenyl-4-ylcarboxamido)-2-fluorobenzoic acid
8% inhibition of isoform NEU3 at 1 mM
4-acetamido-5-pentanamido-2-fluorobenzoic acid
13% inhibition of isoform NEU3 at 1 mM
(2R,3R,4S)-3-(acetylamino)-2-[(1S,2S)-3-(acetylamino)-1,2-dihydroxypropyl]-4-hydroxy-3,4-dihydro-2H-pyran-6-carboxylic acid
-
(2R,3R,4S)-3-(acetylamino)-2-[(1S,2S)-3-(benzoylamino)-1,2-dihydroxypropyl]-4-hydroxy-3,4-dihydro-2H-pyran-6-carboxylic acid
-
(2R,3R,4S)-3-(acetylamino)-2-[(1S,2S)-3-(butyrylamino)-1,2-dihydroxypropyl]-4-hydroxy-3,4-dihydro-2H-pyran-6-carboxylic acid
-
(2R,3R,4S)-3-(acetylamino)-2-[(1S,2S)-3-[(cyclopropylcarbonyl)amino]-1,2-dihydroxypropyl]-4-hydroxy-3,4-dihydro-2H-pyran-6-carboxylic acid
-
1,3,8-trihydroxy-6-methylanthracene-9,10-dione
-
-
1,8-dihydroxyanthracene-9,10-dione
-
-
2,3-dehydro-2-deoxy-N-acetylneuraminic acid
2,6-anhydro-3,5-dideoxy-5-glycolylamido-D-glycero-D-galactonon-2-enonic acid
-
-
2,6-anhydro-3-deoxy-D-glycero-D-galacto-non-2-enonic acid
-
-
2,6-anhydro-5-(2-azidoacetamido)-3,5-dideoxy-D-glycero-D-galacto-non-2-enonic acid
-
-
2,6-anhydro-9-azido-3,5,9-trideoxy-5-(2-hydroxyacetamido)-D-glycero-D-galacto-non-2-enonic acid
-
2,6-anhydro-9-azido-5-(2-azidoacetamido)-3,5,9-trideoxy-D-glycero-D-galacto-non-2-enonic acid
-
2-(3,4-dihydroxyphenyl)-3,5,7-trihydroxy-4H-chromen-4-one
-
-
2-(3,4-dihydroxyphenyl)-4H-chromene-3,5,7-triol
-
-
2-deoxy-2,3-dehydro-N-acetyl-D-neuraminic acid
-
-
2-deoxy-2,3-dehydro-N-acetylneuraminic acid
2-deoxy-2,3-didehydro-D-N-acetylneuraminic acid
-
induces morphological changes, showing megakaryocytic differentiation of K-562 cells, with expression of CD41b surface antigen
2-Deoxy-2,3-didehydro-N-acetylneuraminic acid
-
-
3,5,7-trihydroxy-2-(3,4,5-trihydroxyphenyl)-4H-chromen-4-one
-
-
3,5,7-trihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
-
-
4,5-diacetamido-2-fluorobenzoate
8% inhibition of isoform NEU4 at 1 mM
4,5-diacetamido-2-fluorobenzoic acid
37% inhibition of isoform NEU2 at 1 mM
4,5-dihydroxy-9,10-dioxo-9,10-dihydroanthracene-2-carboxylic acid
-
-
4-acetamido-5-(2-ethylbutanamido)-2-fluorobenzoic acid
4-acetamido-5-(2-methylbutanamido)-2-fluorobenzoic acid
7% inhibition of isoform NEU2 at 1 mM
4-acetamido-5-(2-naphthamido)-2-fluorobenzoic acid
4-acetamido-5-(biphenyl-4-ylcarboxamido)-2-fluorobenzoic acid
4-acetamido-5-benzamido-2-fluorobenzoic acid
17% inhibition of isoform NEU2 at 1 mM
4-acetamido-5-cyclohexanecarboxamido-2-fluorobenzoic acid
4-acetamido-5-cyclopropanecarboxamido-2-fluorobenzoic acid
4-acetamido-5-isobutyramido-2-fluorobenzoic acid
4-acetamido-5-pentanamido-2-fluorobenzoic acid
4-acetamido-5-pivalamido-2-fluorobenzoic acid
less than 5% inhibition of isoform NEU4 at 1 mM
5,6,7-trihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
-
-
5,6,7-trihydroxy-2-phenyl-4H-chromen-4-one
-
-
5,7-dihydroxy-2-(2-hydroxyphenyl)-4H-chromen-4-one
-
-
5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
-
-
5,7-dihydroxy-2-(4-methoxyphenyl)-4H-chromen-4-one
-
-
5,7-dihydroxy-2-phenyl-4H-chromen-4-one
-
-
5,7-dihydroxy-3-(4-hydroxyphenyl)-4H-chromen-4-one
-
-
5-(acetylamino)-2,6-anhydro-3,5,9-trideoxy-9-(pentanoylamino)-L-glycero-L-altro-non-2-enonic acid
-
5-(acetylamino)-2,6-anhydro-3,5,9-trideoxy-9-[(3-methylbutanoyl)amino]-L-glycero-L-altro-non-2-enonic acid
-
5-(acetylamino)-2,6-anhydro-9-[(cyclopentylcarbonyl)amino]-3,5,9-trideoxy-L-glycero-L-altro-non-2-enonic acid
-
5-acetamido-2,6-anhydro-3,5-dideoxy-9-O-methyl-D-glycero-D-galacto-non-2-enonic acid
-
5-acetamido-2,6-anhydro-3,5-dideoxy-D-glycero-D-galactonon-2-enonic acid
-
-
5-acetamido-2,6-anhydro-9-azido-3,5,9-trideoxy-D-glycero-D-galacto-non-2-enonic acid
-
5-acetamido-9-aminopropyl-2,6-anhydro-3,5,9-trideoxy-D-glycero-D-galacto-non-2-enonic acid
-
5-hydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
-
-
5-hydroxy-2-(4-hydroxyphenyl)-7-methoxy-4H-chromen-4-one
-
-
5-methyl-4-methylidene-2-phenyl-4H-chromene
-
-
6-chloro-9,10-dihydro-4,5,7-trihydroxy-9,10-dioxo-2-anthracenecarboxylic acid
-
-
7-hydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
-
-
9,10-dioxo-9,10-dihydroanthracene-2-carboxylic acid
-
-
Cd2+
-
-
Co2+
-
-
dihydroisoquinoline derivative
-
-
dithiothreitol
-
-
Fe3+
-
-
K+
-
above 1 mM
Li+
-
9% inhibition at 10 mM
mercaptoethanol
-
-
Mg2+
-
-
Mn2+
-
28% inhibition at 10 mM
myricetin
-
-
N-(4-nitrophenyl)-oxamic acid
-
-
Na+
-
above 1 mM
neuraminic acid
-
-
NH4+
-
-
p-chloromercuribenzoate
-
-
plant extract
-
extracts of Laminaria saccharina, Fucus vesiculosus, Achillea millefolium, Allium cepa and Hypericum perforatum decrease activity. Extracts of pollen and garlic powder (Allium sativum) produce maximum inhibitory effect, 2fold inhibition after preoral administration
-
zanamivir
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cholate
-
-
octyl glucoside
-
highest activation (1.3-2.2fold) at 0.08% w/v concentration
protective protein/cathepsin A
-
because of its association with protective protein/cathepsin A, which acts as a molecular chaperone, NEU1 is transported to the lysosomal compartment, catalytically activated, and stabilized
-
sodium deoxycholate
-
highest activation (1.1-1.8.5fold) at 0.03% w/v concentration
Triton X-100
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018 - 0.14
4-methylumbelliferyl alpha-D-N-acetylneuraminic acid
0.078
2'-(4-methylumbelliferyl) alpha-D-N-acetylneuraminic acid
-
in 50 mM Tris-HCl pH7.5, at 25°C
1.1
2-(3-methoxyphenyl)-N-acetylneuraminic acid
-
-
0.44
4-methylumbelliferyl alpha-NeuAc
-
37°C, pH 5.6 or 7.0
0.09 - 0.14
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid
0.31
alpha(2-3)sialyllactose
-
37°C, pH 5.6 or 7.0
0.28 - 0.43
alpha(2-3)sialylparagloboside
0.36 - 6.7
fetuin
-
0.14 - 0.91
ganglioside GD1a
0.1 - 0.59
ganglioside GD1b
0.24 - 0.4
ganglioside GM3
0.38 - 0.62
ganglioside GT1b
0.11 - 0.25
GD1a
0.04
GM2
-
-
0.15
GM3
-
-
0.09
GT1
-
-
7.9
N-acetylneuraminic acid-alpha-2,3-lactose
-
-
5.6
N-acetylneuraminic acid-alpha-2,6-lactose
-
-
3
N-acetylneuraminyllactose
-
-
4.8
N-glycoloylneuraminic acid-alpha-2,3-lactose
-
-
1.67
sialyl-alpha-2,3-lactose
-
-
1.81
sialyl-alpha-2,6-lactose
-
-
2.39
transferrin
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8 - 51
4-methylumbelliferyl alpha-D-N-acetylneuraminic acid
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5
4-acetamido-5-(biphenyl-4-ylcarboxamido)-2-fluorobenzoic acid
Homo sapiens
IC50 above 5 mM, isoform NEU3
0.058
(2R,3R,4S)-3-(acetylamino)-2-[(1S,2S)-3-(acetylamino)-1,2-dihydroxypropyl]-4-hydroxy-3,4-dihydro-2H-pyran-6-carboxylic acid
Homo sapiens
-
0.013
(2R,3R,4S)-3-(acetylamino)-2-[(1S,2S)-3-(benzoylamino)-1,2-dihydroxypropyl]-4-hydroxy-3,4-dihydro-2H-pyran-6-carboxylic acid
Homo sapiens
-
0.032
(2R,3R,4S)-3-(acetylamino)-2-[(1S,2S)-3-(butyrylamino)-1,2-dihydroxypropyl]-4-hydroxy-3,4-dihydro-2H-pyran-6-carboxylic acid
Homo sapiens
-
0.68
(2R,3R,4S)-3-(acetylamino)-2-[(1S,2S)-3-[(cyclopropylcarbonyl)amino]-1,2-dihydroxypropyl]-4-hydroxy-3,4-dihydro-2H-pyran-6-carboxylic acid
Homo sapiens
-
0.76
1,3,8-trihydroxy-6-methylanthracene-9,10-dione
Homo sapiens
-
in 50 mM Tris-HCl pH 7.5, at 25°C
1
1,8-dihydroxyanthracene-9,10-dione
Homo sapiens
-
IC50 above 1.0 mM, in 50 mM Tris-HCl pH 7.5, at 25°C
0.034
2,6-anhydro-3,5-dideoxy-5-glycolylamido-D-glycero-D-galactonon-2-enonic acid
Homo sapiens
-
pH 5.5, 37°C
2.1
2,6-anhydro-3-deoxy-D-glycero-D-galacto-non-2-enonic acid
Homo sapiens
-
pH 5.5, 37°C
0.0083
2,6-anhydro-5-(2-azidoacetamido)-3,5-dideoxy-D-glycero-D-galacto-non-2-enonic acid
Homo sapiens
-
pH 5.5, 37°C
0.15 - 0.19
2,6-anhydro-9-azido-3,5,9-trideoxy-5-(2-hydroxyacetamido)-D-glycero-D-galacto-non-2-enonic acid
0.013
2,6-anhydro-9-azido-5-(2-azidoacetamido)-3,5,9-trideoxy-D-glycero-D-galacto-non-2-enonic acid
0.13 - 0.16
2-(3,4-dihydroxyphenyl)-3,5,7-trihydroxy-4H-chromen-4-one
1
2-(3,4-dihydroxyphenyl)-4H-chromene-3,5,7-triol
Homo sapiens
-
IC50 above 1.0 mM, in 50 mM Tris-HCl pH 7.5, at 25°C
0.018 - 0.143
2-deoxy-2,3-dehydro-N-acetylneuraminic acid
0.13
3,5,7-trihydroxy-2-(3,4,5-trihydroxyphenyl)-4H-chromen-4-one
Homo sapiens
-
in 50 mM Tris-HCl pH 7.5, at 25°C
0.23
3,5,7-trihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
Homo sapiens
-
in 50 mM Tris-HCl pH 7.5, at 25°C
0.13
4,5-dihydroxy-9,10-dioxo-9,10-dihydroanthracene-2-carboxylic acid
Homo sapiens
-
in 50 mM Tris-HCl pH 7.5, at 25°C
0.552 - 5
4-acetamido-5-(biphenyl-4-ylcarboxamido)-2-fluorobenzoic acid
0.055
5,6,7-trihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
Homo sapiens
-
in 50 mM Tris-HCl pH 7.5, at 25°C
0.13
5,6,7-trihydroxy-2-phenyl-4H-chromen-4-one
Homo sapiens
-
in 50 mM Tris-HCl pH 7.5, at 25°C
0.07
5,7-dihydroxy-2-(2-hydroxyphenyl)-4H-chromen-4-one
Homo sapiens
-
in 50 mM Tris-HCl pH 7.5, at 25°C
0.57
5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
Homo sapiens
-
in 50 mM Tris-HCl pH 7.5, at 25°C
1
5,7-dihydroxy-2-(4-methoxyphenyl)-4H-chromen-4-one
Homo sapiens
-
IC50 above 1.0 mM, in 50 mM Tris-HCl pH 7.5, at 25°C
0.89
5,7-dihydroxy-2-phenyl-4H-chromen-4-one
Homo sapiens
-
in 50 mM Tris-HCl pH 7.5, at 25°C
0.38
5,7-dihydroxy-3-(4-hydroxyphenyl)-4H-chromen-4-one
Homo sapiens
-
in 50 mM Tris-HCl pH 7.5, at 25°C
0.01
5-(acetylamino)-2,6-anhydro-3,5,9-trideoxy-9-(pentanoylamino)-L-glycero-L-altro-non-2-enonic acid
Homo sapiens
-
0.565
5-(acetylamino)-2,6-anhydro-3,5,9-trideoxy-9-[(3-methylbutanoyl)amino]-L-glycero-L-altro-non-2-enonic acid
Homo sapiens
-
0.135
5-(acetylamino)-2,6-anhydro-9-[(cyclopentylcarbonyl)amino]-3,5,9-trideoxy-L-glycero-L-altro-non-2-enonic acid
Homo sapiens
-
0.041 - 1.1
5-acetamido-2,6-anhydro-3,5-dideoxy-9-O-methyl-D-glycero-D-galacto-non-2-enonic acid
0.018
5-acetamido-2,6-anhydro-3,5-dideoxy-D-glycero-D-galactonon-2-enonic acid
Homo sapiens
-
pH 5.5, 37°C
0.031 - 0.043
5-acetamido-2,6-anhydro-9-azido-3,5,9-trideoxy-D-glycero-D-galacto-non-2-enonic acid
2.4 - 10
5-acetamido-9-aminopropyl-2,6-anhydro-3,5,9-trideoxy-D-glycero-D-galacto-non-2-enonic acid
1
5-hydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
Homo sapiens
-
IC50 above 1.0 mM, in 50 mM Tris-HCl pH 7.5, at 25°C
0.89 - 1
5-hydroxy-2-(4-hydroxyphenyl)-7-methoxy-4H-chromen-4-one
1
5-methyl-4-methylidene-2-phenyl-4H-chromene
Homo sapiens
-
IC50 above 1.0 mM, in 50 mM Tris-HCl pH 7.5, at 25°C
0.1
6-chloro-9,10-dihydro-4,5,7-trihydroxy-9,10-dioxo-2-anthracenecarboxylic acid
Homo sapiens
-
IC50 above 0.1 mM, in 50 mM Tris-HCl pH 7.5, at 25°C
0.47
7-hydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
Homo sapiens
-
in 50 mM Tris-HCl pH 7.5, at 25°C
0.8
9,10-dioxo-9,10-dihydroanthracene-2-carboxylic acid
Homo sapiens
-
in 50 mM Tris-HCl pH 7.5, at 25°C
0.15
myricetin
Homo sapiens
-
in 50 mM Tris-HCl pH 7.5, at 25°C
0.0053
zanamivir
Homo sapiens
-
pH 5.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0005
-
leukocytes
0.0024
-
liver
0.04
-
-
additional information
-
quantification by RT-PCR
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
assay at
4 - 4.5
-
-
4 - 5
-
-
4.1
-
ganglioside mixture as substrate
4.2 - 4.6
-
-
4.4
-
sialyllactose as substrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 5.8
-
-
3.5 - 5
-
pH 3.5: about 30% of maximal activity, pH 5.0: about 60% of maximal activity
4.5 - 6.5
-
activity range, almost inactive at pH 4.0 and pH 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
37
-
assay at
37.5
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
only lysosomal Neu1 and plasma membrane-associated Neu3 are detected in freshly isolated and activated human T lymphocytes. Activity of Neu3 changes minimally in activated lymphocytes. Sialidase activity in activated T lymphocytes contributes to the hyposialylation of specific cell surface glycoconjugates and to the production of IFN-gamma
Manually annotated by BRENDA team
-
aortic smooth muscle
Manually annotated by BRENDA team
-
low expression of Neu-2 and Neu-3
Manually annotated by BRENDA team
-
low amount of Neu-1
Manually annotated by BRENDA team
-
aortic smooth muscle
Manually annotated by BRENDA team
-
CD4+ T-cells,low expression of Neu-2
Manually annotated by BRENDA team
additional information
-
tissue distribution of the 3 isozymes, Neu-1 is ubiquitously expressed at higher level, except for neutrophils
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
intracellular distribution, enzyme contains a signal for internalization in form of a C-terminal tetrapeptide Y412GTL415, Y412 and L415 are essential for endocytosis of the enzyme, mechanism, targeting from lysosomal membrane to endosomes via clathrin-coated pits, enzyme pattern in AP3-deficient cells
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
mutations of residues expected to interact directly with the sialic acid N5-acetyl (A160, M87, I105) and C7-C9 glycerol side-chain (E113, Y179, Y181) reduce enzymatic activity. Truncations at the N- or C-terminus of more than 10 residues abolish enzyme activity
metabolism
NEU3 regulates the detergent resistant membranes ganglioside content and is as a modulator of Akt phosphorylation
malfunction
mutations in the NEU1 gene are causative of sialidosis, a severe lysosomal storage disorder showing autosomal recessive mode of inheritance
metabolism
-
NEU4 long is a downstream component of the PI3K/Akt signaling pathway required for retinoic acid-induced differentiation of neuroblastoma SK-N-BE cells
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NEUR3_HUMAN
428
0
48252
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
-
gel filtration
42000
-
-
46000
x * 46000, SDS-PAGE
48000
48252
-
x * 48252, calculated from sequence
70000
-
analytical gel electrophoresis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of three-dimensional structures of NEU3 based on the crystal structure of NEU2 using a homology modeling program
hanging drop method, high resolution X-ray structures of human sialidase Neu2, in its apo form and in complex with the inhibitor 2-deoxy-2,3-dehydro-N-acetylneuraminic acid. The structure shows the canonical six-blade beta-propeller observed in viral and bacterial sialidases with its active site in a shallow crevice. In the complex structure, the inhibitor lies in the catalytic crevice surrounded by ten amino acids
modeling of three-dimensional structures of NEU1, NEU3 and NEU4 based on the crystal structure of NEU2 using a homology modeling program
modeling of three-dimensional structures of NEU4 based on the crystal structure of NEU2 using a homology modeling program
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A160G
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
A160G/M87G/I105G
site-directed mutagenesis, inactive mutant
D50S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E113A
site-directed mutagenesis, inactive mutant
E225S
site-directed mutagenesis, almost inactive mutant
E51D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E51S
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
G162A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
G419STOP
site-directed mutagenesis, the C-terminal 10-residue truncation leads to an increase in activity compared to the wild-type enzyme
H277F
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
I105G
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
I407STOP
site-directed mutagenesis, almost inactive mutant
L408STOP
site-directed mutagenesis, the large deletion leads to inactivation of the mutant
M87G
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
M87G/I105G
site-directed mutagenesis, inactive mutant
N88D
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R114A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R114Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R245A
site-directed mutagenesis, inactive mutant
R25H
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R340A
site-directed mutagenesis, almost inactive mutant
R45V
site-directed mutagenesis, inactive mutant
T403STOP
site-directed mutagenesis, inactive mutant
V107M
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y179F
site-directed mutagenesis, inactive mutant
Y181F
site-directed mutagenesis, inactive mutant
Y370C
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y370F
D234N
the mutation results in significantly lower levels of sialidase activity (25%) compared to the wild type and is associated with sialosis
D46A
inactive
E218A
inactive
E218Q
inactive
G413A
-
site-directed mutagenesis, activity and localization in the cell similar to the wild-type enzyme
K45A
the mutant shows about 3fold increased activity towards 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid compared to the wild type
L415A
-
site-directed mutagenesis, 30-50% reduced activity compared to the wild-type enzyme, no internalization due to impaired endocytosis, location in the plasma membrane and the cytosol
Q112A
the mutant shows nearly 4fold increased activity towards 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid compared to the wild type
Q270A
the mutant shows about 4fold increased activity towards 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid compared to the wild type
Q270E
the mutant shows about wild type activity
V217A
the mutation results in significantly lower levels of sialidase activity (44%) compared to the wild type and is associated with sialosis
V217M/G243R
-
the mutation is associated with sialidosis type I phenotype
Y412A
-
site-directed mutagenesis, 55-70% reduced activity compared to the wild-type enzyme, no internalization due to impaired endocytosis, location in the plasma membrane and the cytosol
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
24 h, 50% loss of activity
45
-
5 min, 60% loss in activity
50
-
30 min, complete inactivation
52
-
inactivated
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
labile towards freezing and thrawing
-
stable to freezing
-
the enzyme is unstable upon freezing at -20°C, 50% loss of activity after one cycle of freezing-thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, one week, 20% loss in activity
-
-20°C, pellet no loss in activity up to a month
-
-70°C, after 48 h inactivated
-
-80°C, stable for 1 year
-
-80°C, storage of liver over a year, no loss in activity
-
4°C, 24 h, 30 to 40% loss in activity
-
4°C, 50% loss of activity after 24 h
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes as MBP-fusion proteins from Escherichia coli strain TB1 by amylose affinity chromatography, the tag is cleaved off by Factor Xa
glutathione-Sepharose 4B column chromatography
Ni-NTA column chromatography, and Superdex 200 gel filtration
-
octyl-Sepharose chromatography and Toyopearl HW-55F column chromatography
-
recombinant
-
recombinant enzyme
-
recombinant His-tagged protein
-
SP Sepharose column chromatography, His-Trap HP column chromatography, and Superdex 200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
adenoviral-mediated gene transfer is used to overexpress hNeu3 in the livers of male mice. hepatic Neu3 overexpression improves insulin sensitivity and glucose tolerance through modification of ganglioside composition and peroxisome proliferator-activated receptor gamma signaling
overexpression in mouse aortic vascular smooth muscle cells. Overexpression of this gene has no effect on DNA synthesis and ERK phosphorylation in cultured vascular smooth muscle cells in the presence of TNF-alpha. The expression of the Neu3 gene leads to the inhibition of TNF-alpha induced matrix metalloproteinase-9 (MMP-9) expression in vascular smooth muscle cells. Neu3 gene expression strongly decreases MMP-9 promoter activity in response to TNF-alpha
recombinant expression of wild-type and mutant A160G, E51S, H277F, R48N, R48S, M87G, D50S, and Y370F enzymes as MBP-fusion proteins in Escherichia coli strain TB1
expressed as GST-fusion protein in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli strain JM109
-
expressed in HEK-293 T cells
-
expressed in Sf9 insect cells
-
expressed in SK-N-BE neuroblastoma cells
-
expression in COS-7 cells
-
expression in Escherichia coli
-
gene neu-1 located in the major histocompatibility complex locus, expression of wild-type and mutant in COS-7 cells
-
isozyme NEU2, DNA and amino acid sequence determination and analysis, overexpression as soluble active enzyme in Escherichia coli
-
isozymes Neu-1 and Neu-3, DNA sequence determination and analysis, expression of the enzymes in COS-7 cells, stably in JURKAT cells, and as His-tagged proteins in Spodoptera frugiperda Sf9 insect cells
-
transfection in COS7 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme activity is increased in serum of prostate cancer patients
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schauer, R.; Wember, M.
Isolation and characterization of a sialidase from the starfish Asterias rubens
Biol. Chem. Hoppe-Seyler
370
183-190
1989
Asterias rubens, Homo sapiens
Manually annotated by BRENDA team
Lieser, M.; Harms, E.; Kern, H.; Bach, G.; Cantz, M.
Ganglioside GM3 sialidase activity in fibroblasts of normal individuals and of patients with sialidosis and mucolipidosis IV
Biochem. J.
260
69-74
1989
Homo sapiens
Manually annotated by BRENDA team
Hiraiwa, M.; Uda, Y.; Nishizawa, M.; Miyatake, T.
Human placental sialidase: partial purification and characterization
J. Biochem.
101
1273-1279
1987
Homo sapiens
Manually annotated by BRENDA team
Michalski, J.C.; Corfield, A.P.; Schauer, R.
Properties of human liver lysosomal sialidase
Biol. Chem. Hoppe-Seyler
367
715-722
1986
Homo sapiens
Manually annotated by BRENDA team
Hiraiwa, M.; Uda, Y.; Nishizawa, M.; Uda, Y.; Nakajima, T.; Miyatake, T.
Human placental sialidase: further purification and characterization
J. Biochem.
103
86-90
1988
Homo sapiens
Manually annotated by BRENDA team
Verheuen, F.W.; Palmeri, S.; Galjaard, H.
Purification and partial characterization of lysosomal neuraminidase from human placenta
Eur. J. Biochem.
162
63-67
1987
Homo sapiens
Manually annotated by BRENDA team
Schauer, R.; Wember, M.; Tschetsche, H.
Isolation and characterization of an oligosaccharide- and glycoprotein-specific sialidase from human leucocytes
Hoppe-Seyler's Z. Physiol. Chem.
365
419-426
1984
Homo sapiens
Manually annotated by BRENDA team
Michalski, J.C.; Corfield, A.P.; Schauer, R.
Solubilization and affinity chromatography of a sialidase from human liver
Hoppe-Seyler's Z. Physiol. Chem.
363
1097-1102
1982
Homo sapiens
Manually annotated by BRENDA team
Meyer, D.M.; Lemmonier, M.; Bourrillon, R.
Human liver neuraminidase
Biochem. Biophys. Res. Commun.
103
1302-1309
1981
Homo sapiens
Manually annotated by BRENDA team
Thomas, G.H.; Reynolds, L.W.; Miller, C.S.
Characterization of neuraminidase activity of cultured human fibroblasts
Biochim. Biophys. Acta
568
39-48
1979
Homo sapiens
Manually annotated by BRENDA team
Ray, P.K.
Bacterial neuraminidase and altered immunological behavior of treated mammalian cells
Adv. Appl. Microbiol.
21
227-267
1977
Bos taurus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Tallman J.F.; Brady, R.O.
The purification and properties of a mammalian neuraminidase (sialidase)
Biochim. Biophys. Acta
293
434-443
1973
Homo sapiens
Manually annotated by BRENDA team
Waters, P.J.; Corfield, A.P.; Eisenthal, R.; Pennok, C.A.
Freeze-stable sialidase activity in human leucocytes: substrate specificity, inhibitor susceptibility, detergent requirements and subcellular localization
Biochem. J.
301
777-784
1994
Homo sapiens
-
Manually annotated by BRENDA team
Hiraiwa, M.; Uda, Y.; Tsuji, S.; Miyatake, T.; Martin, B.M.; Tayama, M.; O. Brien, J.S.; Kishimoto, Y.
Human placental sialidase complex: characterization of the 60 kda protein that cross-reacts with anti-saposin antibodies
Biochem. Biophys. Res. Commun.
177
1211-1216
1991
Homo sapiens
Manually annotated by BRENDA team
Martinez-Zorzano, V.S.; Feijoo, C.; de la Cadena, M.P.; Butron, M.; Fernandez-Briera, A.; Rodriguez-Berrocal, F.J.
Human colon sialidase: characterization and activity levels in normal mucosa and colonic adenocarcinoma
Enzyme Protein
48
282-290
1996
Homo sapiens
Manually annotated by BRENDA team
Wang, P.; Zhang, J.; Bian, H.; Wu, P.; Kuvelkar, R.; Kung, T.T.; Crawley, Y.; Egan, R.W.; Billah, M.M.
Induction of lysosomal and plasma membrane-bound sialidases in human T-cells via T-cell receptor
Biochem. J.
380
425-433
2004
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Nagaoka, M.; Shiraishi, T.; Furuhata, K.; Uda, Y.
Effects of inorganic anions on the activation of acid sialidases
Biol. Pharm. Bull.
26
295-298
2003
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Lukong, K.E.; Seyrantepe, V.; Landry, K.; Trudel, S.; Ahmad, A.; Gahl, W.A.; Lefrancois, S.; Morales, C.R.; Pshezhetsky, A.V.
Intracellular distribution of lysosomal sialidase is controlled by the internalization signal in its cytoplasmic tail
J. Biol. Chem.
276
46172-46181
2001
Homo sapiens
Manually annotated by BRENDA team
Monti, E.; Bassi, M.T.; Bresciani, R.; Civini, S.; Croci, G.L.; Papini, N.; Riboni, M.; Zanchetti, G.; Ballabio, A.; Preti, A.; Tettamanti, G.; Venerando, B.; Borsani, G.
Molecular cloning and characterization of NEU4, the fourth member of the human sialidase gene family
Genomics
83
445-453
2004
Homo sapiens
Manually annotated by BRENDA team
Tringali, C.; Papini, N.; Fusi, P.; Croci, G.; Borsani, G.; Preti, A.; Tortora, P.; Tettamanti, G.; Venerando, B.; Monti, E.
Properties of recombinant human cytosolic sialidase HsNEU2: The enzyme hydrolyzes monomerically dispersed GM1 ganglioside molecules
J. Biol. Chem.
279
3169-3179
2004
Homo sapiens
Manually annotated by BRENDA team
Chavas, L.M.; Tringali, C.; Fusi, P.; Venerando, B.; Tettamanti, G.; Kato, R.; Monti, E.; Wakatsuki, S.
Crystal structure of the human cytosolic sialidase Neu2. Evidence for the dynamic nature of substrate recognition
J. Biol. Chem.
280
469-475
2005
Homo sapiens (Q9Y3R4), Homo sapiens
Manually annotated by BRENDA team
Ha, K.; Cho, S.; Kang, S.; Kim, Y.; Kim, J.; Kim, C.
Cloning of human liver cytosolic sialidase from genomic DNA using splicing by overlap extension and its characterization
J. Microbiol. Biotechnol.
15
722-727
2005
Homo sapiens
-
Manually annotated by BRENDA team
Ha, K.T.; Lee, Y.C.; Cho, S.H.; Kim, J.K.; Kim, C.H.
Molecular characterization of membrane type and ganglioside-specific sialidase (Neu3) expressed in E. coli
Mol. Cell
17
267-273
2004
Homo sapiens
Manually annotated by BRENDA team
Yamaguchi, K.; Hata, K.; Wada, T.; Moriya, S.; Miyagi, T.
Epidermal growth factor-induced mobilization of a ganglioside-specific sialidase (NEU3) to membrane ruffles
Biochem. Biophys. Res. Commun.
346
484-490
2006
Homo sapiens (Q9UQ49), Homo sapiens
Manually annotated by BRENDA team
Moon, S.K.; Cho, S.H.; Kim, K.W.; Jeon, J.H.; Ko, J.H.; Kim, B.Y.; Kim, C.H.
Overexpression of membrane sialic acid-specific sialidase Neu3 inhibits matrix metalloproteinase-9 expression in vascular smooth muscle cells
Biochem. Biophys. Res. Commun.
356
542-547
2007
Homo sapiens (Q9UQ49)
Manually annotated by BRENDA team
Magesh, S.; Moriya, S.; Suzuki, T.; Miyagi, T.; Ishida, H.; Kiso, M.
Design, synthesis, and biological evaluation of human sialidase inhibitors. Part 1: selective inhibitors of lysosomal sialidase (NEU1)
Bioorg. Med. Chem. Lett.
18
532-537
2008
Homo sapiens (Q99519), Homo sapiens
Manually annotated by BRENDA team
Aksenov, D.V.; Kaplun, V.V.; Tertov, V.V.; Sobenin, I.A.; Orekhov, A.N.
Effect of plant extracts on trans-sialidase activity in human blood plasma
Bull. Exp. Biol. Med.
143
46-50
2007
Homo sapiens
Manually annotated by BRENDA team
Hasegawa, T.; Sugeno, N.; Takeda, A.; Matsuzaki-Kobayashi, M.; Kikuchi, A.; Furukawa, K.; Miyagi, T.; Itoyama, Y.
Role of Neu4L sialidase and its substrate ganglioside GD3 in neuronal apoptosis induced by catechol metabolites
FEBS Lett.
581
406-412
2007
Homo sapiens
Manually annotated by BRENDA team
Nan, X.; Carubelli, I.; Stamatos, N.M.
Sialidase expression in activated human T lymphocytes influences production of IFN-gamma
J. Leukoc. Biol.
81
284-296
2007
Homo sapiens (Q99519), Homo sapiens (Q9UQ49), Homo sapiens
Manually annotated by BRENDA team
Magesh, S.; Suzuki, T.; Miyagi, T.; Ishida, H.; Kiso, M.
Homology modeling of human sialidase enzymes NEU1, NEU3 and NEU4 based on the crystal structure of NEU2: hints for the design of selective NEU3 inhibitors
J. Mol. Graph. Model.
25
196-207
2006
Homo sapiens (Q8WWR8), Homo sapiens (Q9UQ49), Homo sapiens (Q9Y3R4), Homo sapiens
Manually annotated by BRENDA team
Yoshizumi, S.; Suzuki, S.; Hirai, M.; Hinokio, Y.; Yamada, T.; Yamada, T.; Tsunoda, U.; Aburatani, H.; Yamaguchi, K.; Miyagi, T.; Oka, Y.
Increased hepatic expression of ganglioside-specific sialidase, NEU3, improves insulin sensitivity and glucose tolerance in mice
Metab. Clin. Exp.
56
420-429
2007
Homo sapiens (Q9UQ49)
Manually annotated by BRENDA team
Hinek, A.; Bodnaruk, T.D.; Bunda, S.; Wang, Y.; Liu, K.
Neuraminidase-1, a subunit of the cell surface elastin receptor, desialylates and functionally inactivates adjacent receptors interacting with the mitogenic growth factors PDGF-BB and IGF-2
Am. J. Pathol.
173
1042-1056
2008
Clostridium perfringens, Homo sapiens
Manually annotated by BRENDA team
Jin, U.H.; Ha, K.T.; Kim, K.W.; Chang, Y.C.; Lee, Y.C.; Ko, J.H.; Kim, C.H.
Membrane type sialidase inhibits the megakaryocytic differentiation of human leukemia K562 cells
Biochim. Biophys. Acta
1780
757-763
2008
Homo sapiens
Manually annotated by BRENDA team
Shiozaki, K.; Yamaguchi, K.; Sato, I.; Miyagi, T.
Plasma membrane-associated sialidase (NEU3) promotes formation of colonic aberrant crypt foci in azoxymethane-treated transgenic mice
Cancer Sci.
100
588-594
2009
Homo sapiens
Manually annotated by BRENDA team
Piagnerelli, M.; Boudjeltia, K.Z.; Rapotec, A.; Richard, T.; Brohee, D.; Babar, S.; Bouckaert, V.; Simon, A.C.; Toko, J.P.; Walravens, T.; Vincent, J.L.; Vanhaeverbeek, M.
Neuraminidase alters red blood cells in sepsis
Crit. Care Med.
37
1244-1250
2009
Clostridium perfringens, Homo sapiens
Manually annotated by BRENDA team
Yogalingam, G.; Bonten, E.J.; van de Vlekkert, D.; Hu, H.; Moshiach, S.; Connell, S.A.; dAzzo, A.
Neuraminidase 1 is a negative regulator of lysosomal exocytosis
Dev. Cell
15
74-86
2008
Mus musculus (O35657), Homo sapiens (Q99519), Homo sapiens
Manually annotated by BRENDA team
Gadhoum, S.Z.; Sackstein, R.
CD15 expression in human myeloid cell differentiation is regulated by sialidase activity
Nat. Chem. Biol.
4
751-757
2008
Homo sapiens
Manually annotated by BRENDA team
Uchihara, T.; Ohashi, K.; Kitagawa, M.; Kurata, M.; Nakamura, A.; Hirokawa, K.; Kasuga, T.; Kobayashi, T.
Sialidosis type I carrying V217M/G243R mutations in lysosomal sialidase: an autopsy study demonstrating terminal sialic acid in lysosomal lamellar inclusions and cerebellar dysplasia
Acta Neuropathol.
119
135-145
2010
Homo sapiens
Manually annotated by BRENDA team
Magesh, S.; Savita, V.; Moriya, S.; Suzuki, T.; Miyagi, T.; Ishida, H.; Kiso, M.
Human sialidase inhibitors: design, synthesis, and biological evaluation of 4-acetamido-5-acylamido-2-fluoro benzoic acids
Bioorg. Med. Chem.
17
4595-4603
2009
Homo sapiens (Q8WWR8), Homo sapiens (Q99519), Homo sapiens (Q9UQ49), Homo sapiens (Q9Y3R4), Homo sapiens
Manually annotated by BRENDA team
Arioka, S.; Sakagami, M.; Uematsu, R.; Yamaguchi, H.; Togame, H.; Takemoto, H.; Hinou, H.; Nishimura, S.
Potent inhibitor scaffold against Trypanosoma cruzi trans-sialidase
Bioorg. Med. Chem.
18
1633-1640
2010
Homo sapiens, Trypanosoma cruzi
Manually annotated by BRENDA team
Bigi, A.; Morosi, L.; Pozzi, C.; Forcella, M.; Tettamanti, G.; Venerando, B.; Monti, E.; Fusi, P.
Human sialidase NEU4 long and short are extrinsic proteins bound to outer mitochondrial membrane and the endoplasmic reticulum, respectively
Glycobiology
20
148-157
2010
Homo sapiens
Manually annotated by BRENDA team
Bonten, E.J.; Campos, Y.; Zaitsev, V.; Nourse, A.; Waddell, B.; Lewis, W.; Taylor, G.; dAzzo, A.
Heterodimerization of the sialidase NEU1 with the chaperone protective protein/cathepsin A prevents its premature oligomerization
J. Biol. Chem.
284
28430-28441
2009
Homo sapiens
Manually annotated by BRENDA team
Wang, J.; Wu, G.; Miyagi, T.; Lu, Z.H.; Ledeen, R.W.
Sialidase occurs in both membranes of the nuclear envelope and hydrolyzes endogenous GD1a
J. Neurochem.
111
547-554
2009
Homo sapiens (Q99519), Homo sapiens (Q9UQ49)
Manually annotated by BRENDA team
Sandbhor, M.S.; Soya, N.; Albohy, A.; Zheng, R.B.; Cartmell, J.; Bundle, D.R.; Klassen, J.S.; Cairo, C.W.
Substrate recognition of the membrane-associated sialidase NEU3 requires a hydrophobic aglycone
Biochemistry
50
6753-6762
2011
Homo sapiens
Manually annotated by BRENDA team
Albohy, A.; Li, M.D.; Zheng, R.B.; Zou, C.; Cairo, C.W.
Insight into substrate recognition and catalysis by the human neuraminidase 3 (NEU3) through molecular modeling and site-directed mutagenesis
Glycobiology
20
1127-1138
2010
Homo sapiens (Q9UQ49), Homo sapiens
Manually annotated by BRENDA team
Li, Y.; Cao, H.; Yu, H.; Chen, Y.; Lau, K.; Qu, J.; Thon, V.; Sugiarto, G.; Chen, X.
Identifying selective inhibitors against the human cytosolic sialidase NEU2 by substrate specificity studies
Mol. Biosyst.
7
1060-1072
2011
Homo sapiens
Manually annotated by BRENDA team
Bigi, A.; Tringali, C.; Forcella, M.; Mozzi, A.; Venerando, B.; Monti, E.; Fusi, P.
A proline-rich loop mediates specific functions of human sialidase NEU4 in SK-N-BE neuronal differentiation
Glycobiology
23
1499-1509
2013
Homo sapiens
Manually annotated by BRENDA team
Albohy, A.; Richards, M.R.; Cairo, C.W.
Mapping substrate interactions of the human membrane-associated neuraminidase, NEU3, using STD NMR
Glycobiology
25
284-293
2015
Homo sapiens (Q9UQ49), Homo sapiens
Manually annotated by BRENDA team
Cross, A.S.; Hyun, S.W.; Miranda-Ribera, A.; Feng, C.; Liu, A.; Nguyen, C.; Zhang, L.; Luzina, I.G.; Atamas, S.P.; Twaddell, W.S.; Guang, W.; Lillehoj, E.P.; Puche, A.C.; Huang, W.; Wang, L.X.; Passaniti, A.; Goldblum, S.E.
NEU1 and NEU3 sialidase activity expressed in human lung microvascular endothelia: NEU1 restrains endothelial cell migration, whereas NEU3 does not
J. Biol. Chem.
287
15966-15980
2012
Homo sapiens (Q99519), Homo sapiens (Q9UQ49), Homo sapiens
Manually annotated by BRENDA team
Khedri, Z.; Li, Y.; Cao, H.; Qu, J.; Yu, H.; Muthana, M.M.; Chen, X.
Synthesis of selective inhibitors against V. cholerae sialidase and human cytosolic sialidase NEU2
Org. Biomol. Chem.
10
6112-6120
2012
Streptococcus pneumoniae, Vibrio cholerae (P0C6E9), Vibrio cholerae, Clostridium perfringens (P10481), Salmonella enterica subsp. enterica serovar Typhimurium (P29768), Homo sapiens (Q9Y3R4), Homo sapiens
Manually annotated by BRENDA team
Bonardi, D.; Ravasio, V.; Borsani, G.; dAzzo, A.; Bresciani, R.; Monti, E.; Giacopuzzi, E.
In silico identification of new putative pathogenic variants in the NEU1 sialidase gene affecting enzyme function and subcellular localization
PLoS ONE
9
e104229
2014
Homo sapiens (Q99519), Homo sapiens
Manually annotated by BRENDA team
Bonardi, D.; Papini, N.; Pasini, M.; Dileo, L.; Orizio, F.; Monti, E.; Caimi, L.; Venerando, B.; Bresciani, R.
Sialidase NEU3 dynamically associates to different membrane domains specifically modifying their ganglioside pattern and triggering Akt phosphorylation
PLoS ONE
9
e99405
2014
Homo sapiens (Q9UQ49)
Manually annotated by BRENDA team
Mozzi, A.; Mazzacuva, P.; Zampella, G.; Forcella, M.E.; Fusi, P.A.; Monti, E.
Molecular insight into substrate recognition by human cytosolic sialidase NEU2
Proteins
80
1123-1132
2012
Homo sapiens (Q9Y3R4), Homo sapiens
Manually annotated by BRENDA team
Hunter, C.D.; Khanna, N.; Richards, M.R.; Rezaei Darestani, R.; Zou, C.; Klassen, J.S.; Cairo, C.W.
Human neuraminidase isoenzymes show variable activities for 9-O-acetyl-sialoside substrates
ACS Chem. Biol.
13
922-932
2018
Homo sapiens
Manually annotated by BRENDA team
Paolini, L.; Orizio, F.; Busatto, S.; Radeghieri, A.; Bresciani, R.; Bergese, P.; Monti, E.
Exosomes secreted by hela cells shuttle on their surface the plasma membrane-associated sialidase NEU3
Biochemistry
56
6401-6408
2017
Homo sapiens
Manually annotated by BRENDA team
Hata, K.; Tochigi, T.; Sato, I.; Kawamura, S.; Shiozaki, K.; Wada, T.; Takahashi, K.; Moriya, S.; Yamaguchi, K.; Hosono, M.; Miyagi, T.
Increased sialidase activity in serum of cancer patients Identification of sialidase and inhibitor activities in human serum
Cancer Sci.
106
383-389
2015
Homo sapiens
Manually annotated by BRENDA team