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Information on EC 3.2.1.18 - exo-alpha-sialidase and Organism(s) Clostridium perfringens and UniProt Accession Q59310

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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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This record set is specific for:
Clostridium perfringens
UNIPROT: Q59310
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The taxonomic range for the selected organisms is: Clostridium perfringens
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, lysosomal sialidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylneuraminidase
-
-
-
-
Acetylneuraminyl hydrolase
-
-
-
-
acylneuraminyl glycohydrolase
-
-
-
-
alpha-neuraminidase
-
-
-
-
Cytosolic sialidase
-
-
-
-
G9 sialidase
-
-
-
-
Ganglioside sialidase
-
-
-
-
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-acetylneuraminosyl glycohydrolase
-
-
N-acylneuraminate glycohydrolase
-
-
-
-
NANase
-
-
-
-
neuraminidase
SA85-1.1 protein
-
-
-
-
SA85-1.2 protein
-
-
-
-
SA85-1.3 protein
-
-
-
-
sialidase
STNA
-
-
-
-
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
exo-glycosidase, the active center contains essential cysteine residues
-
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
2-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferol + alpha-D-N-acetylneuraminic acid
show the reaction diagram
-
-
-
?
2-deoxy-2,3-dehydro-N-acetylneuraminic acid + H2O
N-acetylneuraminic acid
show the reaction diagram
-
reaction deduced from crystal structures and confirmed by NMR study
-
?
(N-glycolylneuraminic acid)(alpha2,3)Galbeta-p-nitrophenol + H2O
(N-glycolylneuraminic acid)(alpha2,3)Gal + p-nitrophenol
show the reaction diagram
-
-
-
-
?
(N-glycolylneuraminic acid)(alpha2,6)Galbeta-p-nitrophenol + H2O
(N-glycolylneuraminic acid)(alpha2,6)Gal + p-nitrophenol
show the reaction diagram
-
low activity
-
-
?
(N-glycolylneuraminic acid)(alpha2,6)GalNAcbeta-p-nitrophenol + H2O
(N-glycolylneuraminic acid)(alpha2,6)GalNAc + p-nitrophenol
show the reaction diagram
-
low activity
-
-
?
2'-(4-methyl-umbelliferyl) 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-methylumbelliferol + alpha-D-N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
2-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + N-acetyl-alpha-D-neuraminic acid
show the reaction diagram
-
-
-
-
?
2-(4-nitrophenyl)-alpha-D-N-acetylneuraminic acid + H2O
4-nitrophenol + alpha-D-N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
2-O-(3-methoxyphenyl)neuraminic acid + H2O
?
show the reaction diagram
-
-
-
-
?
3'-sialyllactose + H2O
sialic acid + lactose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
4-nitrophenyl O-(3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-3)-O-beta-D-galactopyranoside + H2O
?
show the reaction diagram
-
about 30% cleavage
-
-
?
4-nitrophenyl O-(3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-6)-O-beta-D-galactopyranoside + H2O
?
show the reaction diagram
-
about 5% cleavage
-
-
?
4-nitrophenyl O-[5-(2-azidoacetamido)-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid]-(2-3)-O-beta-D-galactopyranoside + H2O
?
show the reaction diagram
-
less than 10% cleavage
-
-
?
4-nitrophenyl O-[5-(2-azidoacetamido)-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid]-(2-6)-O-beta-D-galactopyranoside + H2O
?
show the reaction diagram
-
less than 5% cleavage
-
-
?
4-nitrophenyl O-[5-(2-fluoroacetamido)-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid]-(2-3)-O-beta-D-galactopyranoside + H2O
?
show the reaction diagram
-
about 50% cleavage
-
-
?
4-nitrophenyl O-[5-(2-fluoroacetamido)-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid]-(2-6)-O-beta-D-galactopyranoside + H2O
?
show the reaction diagram
-
about 35% cleavage
-
-
?
5-bromo-4-chloro-3-indolyl-alpha-D-N-acetylneuraminic acid + H2O
5-bromo-4-chloro-3-hydroxyindole + N-acetylneuraminic acid
show the reaction diagram
-
-
-
-
?
5-bromo-4-chloro-3-indolyl-alpha-D-N-acetylneuraminic acid + H2O
?
show the reaction diagram
-
-
-
-
?
6'-sialyllactose + H2O
sialic acid + lactose
show the reaction diagram
-
-
-
-
?
alpha(2-6)-sialyllactose + H2O
sialic acid + lactose
show the reaction diagram
-
-
-
-
?
alpha-sialyllactose + H2O
sialic acid + lactose
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-D-galactose + H2O
N-acetylneuraminic acid + D-galactose
show the reaction diagram
-
-
-
-
?
N-acetylneuraminic acid-alpha-2,6-lactose + H2O
N-acetylneuraminic acid + lactose
show the reaction diagram
-
-
-
-
?
Neu5,9Ac2(alpha2,3)Galbeta-p-nitrophenol + H2O
Neu5,9Ac2(alpha2,3)Gal + p-nitrophenol
show the reaction diagram
-
low activity
-
-
?
Neu5,9Ac2(alpha2,6)Galbeta-p-nitrophenol + H2O
Neu5,9Ac2(alpha2,6)Gal + p-nitrophenol
show the reaction diagram
-
low activity
-
-
?
Neu5,9Ac2(alpha2,6)GalNAcbeta-p-nitrophenol + H2O
Neu5,9Ac2(alpha2,6)GalNAc + p-nitrophenol
show the reaction diagram
-
low activity
-
-
?
Neu5,9Ac2alpha2,6Galbeta-p-nitrophenol + H2O
Neu5,9Ac2alpha2,6Gal + p-nitrophenol
show the reaction diagram
-
low activity
-
-
?
Neu5Ac(alpha2,3)Galbeta-p-nitrophenol + H2O
Neu5Ac(alpha2,3)Gal + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
Neu5Ac(alpha2,6)GalNAcbeta-p-nitrophenol + H2O
Neu5Ac(alpha2,6)GalNAc + p-nitrophenol
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
-
-
-
?
Neu5Acalpha2,6Galbeta-p-nitrophenol + H2O
Neu5Acalpha2,6Galbeta + p-nitrophenol
show the reaction diagram
-
-
-
-
?
Neu5Gcalpha-(2-5)-O-glycolylNeu5Gc + H2O
2 Neu5Gcalpha
show the reaction diagram
-
-
-
-
?
Neu5Gcalpha-(2-8)-Neu5Ac + H2O
Neu5Gc + Neu5Ac
show the reaction diagram
-
preferred substrate
-
-
?
Neu5Gcalpha-(2-8)-Neu5Gc + H2O
Neu5Gc + Neu5Gc
show the reaction diagram
-
low activity
-
-
?
poly-alpha-2,8-lactose + H2O
?
show the reaction diagram
-
-
-
-
?
sialyl-alpha-2,3-lactose + H2O
?
show the reaction diagram
-
-
-
-
?
sialyl-alpha-2,6-lactose + 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
additional information
?
-
-
essential enzyme, enzyme containing culture filtrate possesses the ability to aggluinate and virus and shows receptor properties for erythrocytes, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
110% activity at 10 mM
Mg2+
-
115% activity at 10 mM
Mn2+
-
110% activity at 10 mM
additional information
-
not influenced by Fe2+ and Ni2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3,6,7-tetrahydroxy-2-(3-methylbut-2-enyl)-8-(2-methylbut-3-en-2-yl)-9H-xanthen-9-one
competitive
cudratricusxanthone
competitive
cudraxanthone L
competitive
cudraxanthone M
competitive
macluraxanthone
competitive
(6aS,12aS)-6a,12a-dihydro-6H-[1,3]dioxolo[5,6][1]benzofuro[3,2-c]chromen-3-ol
-
noncompetitive
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-(cyclohexylamino)ethanesulfonic acid
-
-
2-deoxy-2,3-dehydro-N-acetylneuraminic 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-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
-
asteropine A
-
a conotoxin-like peptide from the marine sponge Asteropus simplex, competitive inhibition
-
Berberine
-
reversible non-competitive inhibition
Ca2+
-
90% residual activity at 10 mM
calopocarpin
-
noncompetitive inhibition
cristacarpin
-
noncompetitive inhibition
dehydrocorybulbine
-
-
demethylmedicarpin
-
noncompetitive inhibition
erystagallin A
-
noncompetitive inhibition
erysubin D
-
competitive inhibitor
erysubin E
-
noncompetitive inhibition
erythribyssin D
-
i.e. 3-hydroxy-[2',2'-(3'-hydroxy)-dimethylpyrano]-(5',6':10,9)-(6aR,11aR)pterocarpan
erythribyssin L
-
i.e. 9-hydroxy-10-prenyl-[2',2'-(3'-hydroxy)-dimethylpyrano]-(5',6':2,3)-(6aR,11aR)pterocarpan
erythribyssin M
-
3-hydroxy-[2',2'-(3'-hydroxy)-dimethylpyrano]-(5',6':10,9)-(6aS,11aS)pterocarpan
erythribyssin O
-
noncompetitive inhibition
eryvarin D
-
noncompetitive inhibition
Fe3+
-
56% residual activity at 10 mM
isoneorautenol
-
noncompetitive inhibition
Jatrorrhizine
-
-
N-acetyl-2,3-dehydro-2-deoxyneuraminic acid
-
-
neorautenol
-
noncompetitive inhibition
p-chloromercuribenzoate
-
18% residual activity at 10 mM
palmatine
-
reversible non-competitive inhibition
phaseollin
-
competitive inhibitor
pseudocoptisine
-
-
pseudodehydrocorydaline
-
-
pterocarpin
-
noncompetitive
sophorapterocarpan A
-
noncompetitive inhibition
tetrahydrocoptisine
-
-
Zn2+
-
61% residual activity at 10 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Trypsin
-
isoform NanI activity is enhanced by trypsin pretreatment and then only for substrates with an alpha-2,3- or alpha-2,6-sialic acid linkage
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
2-O-(3-methoxyphenyl)neuraminic acid
-
-
3.3
3'-sialyllactose
-
at pH 5.0 and 37°C
0.08 - 1.8
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid
2
6'-sialyllactose
-
at pH 5.0 and 37°C
1.6
N-acetylneuraminic acid-alpha-2,3-lactose
-
-
0.8
N-acetylneuraminic acid-alpha-2,6-galactose
-
-
1.2
N-acetylneuraminic acid-alpha-2,6-lactose
-
-
0.36 - 0.5
poly-alpha-2,8-lactose
-
0.53 - 1.9
sialyl-alpha-2,3-lactose
1.7 - 3.5
sialyl-alpha-2,6-lactose
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000058
1,3,6,7-tetrahydroxy-2-(3-methylbut-2-enyl)-8-(2-methylbut-3-en-2-yl)-9H-xanthen-9-one
pH 5.0, 37°C
0.000136
cudratricusxanthone
pH 5.0, 37°C
0.000138
cudraxanthone L
pH 5.0, 37°C
0.000098
cudraxanthone M
pH 5.0, 37°C
0.000103
macluraxanthone
pH 5.0, 37°C
0.0021
(6aS,12aS)-6a,12a-dihydro-6H-[1,3]dioxolo[5,6][1]benzofuro[3,2-c]chromen-3-ol
-
-
0.0000367
asteropine A
-
-
-
0.00209
calopocarpin
-
-
0.00031
cristacarpin
-
-
0.00383
demethylmedicarpin
-
-
0.0018
erystagallin A
-
-
0.0152
erysubin D
-
-
0.00024
erysubin E
-
-
0.00413
erythribyssin L
-
-
0.00121
erythribyssin O
-
-
0.00255
eryvarin D
-
-
0.01096
isoneorautenol
-
-
0.02174
neorautenol
-
-
0.00484
phaseollin
-
-
0.0017
pterocarpin
-
-
0.00178
sophorapterocarpan A
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00008
1,3,6,7-tetrahydroxy-2-(3-methylbut-2-enyl)-8-(2-methylbut-3-en-2-yl)-9H-xanthen-9-one
Clostridium perfringens
pH 5.0, 37°C
0.000245
cudratricusxanthone
Clostridium perfringens
pH 5.0, 37°C
0.000228
cudraxanthone L
Clostridium perfringens
pH 5.0, 37°C
0.000186
cudraxanthone M
Clostridium perfringens
pH 5.0, 37°C
0.000186
macluraxanthone
Clostridium perfringens
pH 5.0, 37°C
0.0032
(6aS,12aS)-6a,12a-dihydro-6H-[1,3]dioxolo[5,6][1]benzofuro[3,2-c]chromen-3-ol
Clostridium perfringens
-
-
1.4 - 1.9
2,6-anhydro-9-azido-3,5,9-trideoxy-5-(2-hydroxyacetamido)-D-glycero-D-galacto-non-2-enonic acid
1.2 - 1.6
2,6-anhydro-9-azido-5-(2-azidoacetamido)-3,5,9-trideoxy-D-glycero-D-galacto-non-2-enonic acid
0.013 - 0.02
2-deoxy-2,3-dehydro-N-acetylneuraminic acid
0.31 - 0.46
5-acetamido-2,6-anhydro-3,5-dideoxy-9-O-methyl-D-glycero-D-galacto-non-2-enonic acid
0.04 - 0.059
5-acetamido-2,6-anhydro-9-azido-3,5,9-trideoxy-D-glycero-D-galacto-non-2-enonic acid
1
5-acetamido-9-aminopropyl-2,6-anhydro-3,5,9-trideoxy-D-glycero-D-galacto-non-2-enonic acid
0.0135
Berberine
Clostridium perfringens
-
in 50 mM sodium acetate buffer (pH 5.0), at 22°C
0.00157
calopocarpin
Clostridium perfringens
-
-
0.0251
coptisine
Clostridium perfringens
-
in 50 mM sodium acetate buffer (pH 5.0), at 22°C
0.00228
cristacarpin
Clostridium perfringens
-
-
0.006
curcumin
Clostridium perfringens
-
in 50 mM sodium acetate buffer (pH 5.0), at 22°C
0.0413
dehydrocorybulbine
Clostridium perfringens
-
in 50 mM sodium acetate buffer (pH 5.0), at 22°C
0.00639
demethylmedicarpin
Clostridium perfringens
-
-
0.00204
erystagallin A
Clostridium perfringens
-
-
0.02639
erysubin D
Clostridium perfringens
-
-
0.0013
erysubin E
Clostridium perfringens
-
-
0.0771
erythribyssin D
Clostridium perfringens
-
-
0.00279
erythribyssin L
Clostridium perfringens
-
-
0.2054
erythribyssin M
Clostridium perfringens
-
-
0.00132
erythribyssin O
Clostridium perfringens
-
-
0.00209
eryvarin D
Clostridium perfringens
-
-
0.0969
glaucine
Clostridium perfringens
-
in 50 mM sodium acetate buffer (pH 5.0), at 22°C
0.01412
isoneorautenol
Clostridium perfringens
-
-
0.037
Jatrorrhizine
Clostridium perfringens
-
in 50 mM sodium acetate buffer (pH 5.0), at 22°C
0.0189
N-acetyl-2,3-dehydro-2-deoxyneuraminic acid
Clostridium perfringens
-
at pH 7.2 and 37°C
0.01982
neorautenol
Clostridium perfringens
-
-
0.0128
palmatine
Clostridium perfringens
-
in 50 mM sodium acetate buffer (pH 5.0), at 22°C
0.03355
phaseollin
Clostridium perfringens
-
-
0.0652
pseudocoptisine
Clostridium perfringens
-
in 50 mM sodium acetate buffer (pH 5.0), at 22°C
0.0326
pseudodehydrocorydaline
Clostridium perfringens
-
in 50 mM sodium acetate buffer (pH 5.0), at 22°C
0.0014
pterocarpin
Clostridium perfringens
-
-
0.02534
quercetin
Clostridium perfringens
-
-
0.0422
siastatin B
Clostridium perfringens
-
at pH 7.2 and 37°C
0.00201
sophorapterocarpan A
Clostridium perfringens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.03
-
A99, small sialidase
390
-
A99, large sialidase
570
-
DSM 756, large sialidase
615
-
sialyllactose as substrate
740
-
A99, small sialidase, cloned
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 4.8
-
potassium acetate buffer
4.5 - 7
-
wild type, K1 and K2
5.6
-
citrate-phosphate or Tris-maleate buffer
6.1
-
small sialidase
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
-
at pH 9.0, the activity of all three sialidase isoforms has decreased by about 50%
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43
-
isoform NanH
48
-
isoform NanI sialidase activity steadily increases with temperature until 48°C
51 - 55
-
higher molecular mass sialidase
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 55
-
small sialidase
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q59310_CLOPF
694
0
77327
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
129000
-
x * 129000, isoform NanJ, SDS-PAGE
32000
-
gel filtration, small sialidase
43000
-
x * 43000, isoform NanH, SDS-PAGE
56000
-
gel filtration
60000 - 69000
-
gel filtration, ultracentrifugation, SDS-PAGE
63000
-
gel filtration, higher molecular mass sialidase
65000
-
gel filtration
77000
-
x * 77000, isoform NanI, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain of isoform NanI, to 0.97 A resolution, and complexes with its substrate sialic acid to 0.97A resolution, with transition-state analogue 2-deoxy-2,3-dehydro-N-acetylneuraminic acid to 1.5 A resolution, and with a covalent intermediate formed using a fluorinated sialic acid analogue to 1.2 A resolution
crystallization of the catalytic domain by sitting-drop vapour-diffusion. Crystals belong to space group P2(1)2(1)2(1) with unit-cell parameters a = 96.98, b = 69.41, c = 72.69 A and one monomer per asymmetric unit. The crystals diffract to at least 0.92 A
-
in complex with 2-(cyclohexylamino)ethanesulfonic acid, hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 and 0.2 M ammonium sulfate
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
a mutant strain, with cysteine residue of the active site being exchanged for other amino acids, is insensitive to inhibition by mercury ions
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 8
-
-
171159
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
the NanI sialidase shows no loss of activity after a 10 min incubation at 50°C in Tris-HCl buffer, pH 7.2
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
albumin 0.3 mg/ml protects the enzyme, 50-85% (NH4)2SO4 fraction is stable for at least three years to freezing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.1 M KCN, six months
-
4°C, more than two years in albumin
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 200 gel filtration
-
recombinantly expressed catalytic domain
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 CodonPlus (DE3) cells
-
expression in Escherichia coli
overexpression of the catalytic domain of NAN1 in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bouwstra, J.B.; Deyl, C.M.; Vliegenthart, J.F.G.
Purification and kinetic properties of sialidase from Clostridium perfringens
Biol. Chem. Hoppe-Seyler
368
269-275
1987
Clostridium perfringens
Manually annotated by BRENDA team
Schauer, R.; Nhle, U.
Sialidase (neuraminidase)
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
4
195-208
1984
Actinomyces viscosus, Clostridium perfringens
-
Manually annotated by BRENDA team
Nees, S.; Veh, R.W.; Schauer, R.; Ehrlich, K.
Purification and characterization of neuraminidase from Clostridium perfringens
Hoppe-Seyler's Z. Physiol. Chem.
356
1027-1042
1975
Clostridium perfringens
Manually annotated by BRENDA team
Tanenbaum, S.W.; Sun, S.C.
Some molecular properties of pneumococcal neuraminidase isoenzymes
Biochim. Biophys. Acta
229
824-828
1971
Clostridium perfringens, Streptococcus pneumoniae
Manually annotated by BRENDA team
Cassidy, J.T.; Jourdian, G.W.; Roseman, S.
Sialidase from Clostridium perfringens
Methods Enzymol.
8
680-685
1966
Clostridium perfringens
-
Manually annotated by BRENDA team
Roggentin, P.; Kleineidam, R.G.; Schauer, R.
Diversity in the properties of two sialidase isoenzymes produced by Clostridium perfringens spp.
Biol. Chem. Hoppe-Seyler
376
569-575
1995
Clostridium perfringens
Manually annotated by BRENDA team
Roggentin, T.; Kleineidam, R.G.; schauer, R.; Roggentin, P.
Effects of site-specific mutations on the enzymatic properties of a sialidase from Clostridium perfringens
Glycoconj. J.
9
235-240
1992
Clostridium perfringens
Manually annotated by BRENDA team
Inoue, S.; Lin, S.L.; Inoue, Y.; Groves, D.R.; Thomson, R.J.; von Itzstein, M.; Pavlova, N.V.; Li, S.C.; Li, Y.T.
A unique sialidase that cleaves the Neu5Gcalpha2->5-OglycolylNeu5Gc linkage: comparison of its specificity with that of three microbial sialidases toward four sialic acid dimers
Biochem. Biophys. Res. Commun.
280
104-109
2001
Paenarthrobacter ureafaciens, Clostridium perfringens, Crassostrea virginica, Vibrio cholerae serotype O1
Manually annotated by BRENDA team
Abrashev, I.; Dulguerova, G.
Neuraminidases (sialidases) from bacterial origin
Exp. Pathol. Parasitol.
4
35-40
2000
Glutamicibacter nicotianae, Arthrobacter sp., Paenarthrobacter ureafaciens, Clostridium chauvoei, Clostridium perfringens, Paeniclostridium sordellii, Corynebacterium diphtheriae, Corynebacterium ulcerans, Pasteurella multocida, Streptococcus sp., Trichomonas vaginalis, Micromonospora viridifaciens, Erysipelothrix rhusiopathiae, Vibrio cholerae serotype O1, Paeniclostridium sordellii G12
-
Manually annotated by BRENDA team
Newstead, S.; Chien, C.H.; Taylor, M.; Taylor, G.
Crystallization and atomic resolution X-ray diffraction of the catalytic domain of the large sialidase, nanI, from Clostridium perfringens
Acta Crystallogr. Sect. D
60
2063-2066
2004
Clostridium perfringens
Manually annotated by BRENDA team
Takada, K.; Hamada, T.; Hirota, H.; Nakao, Y.; Matsunaga, S.; van Soest, R.W.; Fusetani, N.
Asteropine A, a sialidase-inhibiting conotoxin-like peptide from the marine sponge Asteropus simplex
Chem. Biol.
13
569-574
2006
Clostridium perfringens, Salmonella enterica subsp. enterica serovar Typhimurium, influenza A virus, Vibrio cholerae serotype O1
Manually annotated by BRENDA team
Chokhawala, H.A.; Yu, H.; Chen, X.
High-throughput substrate specificity studies of sialidases by using chemoenzymatically synthesized sialoside libraries
ChemBioChem
8
194-201
2007
Clostridium perfringens, Paenarthrobacter ureafaciens, Salmonella enterica subsp. enterica serovar Typhimurium, Streptococcus pneumoniae, Streptococcus sp.
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
Kuroiwa, A.; Hisatsune, A.; Isohama, Y.; Katsuki, H.
Bacterial neuraminidase increases IL-8 production in lung epithelial cells via NF-kappaB-dependent pathway
Biochem. Biophys. Res. Commun.
379
754-759
2009
Clostridium perfringens
Manually annotated by BRENDA team
Ryu, Y.B.; Curtis-Long, M.J.; Kim, J.H.; Jeong, S.H.; Yang, M.S.; Lee, K.W.; Lee, W.S.; Park, K.H.
Pterocarpans and flavanones from Sophora flavescens displaying potent neuraminidase inhibition
Bioorg. Med. Chem. Lett.
18
6046-6049
2008
Clostridium perfringens
Manually annotated by BRENDA team
Ryu, Y.B.; Curtis-Long, M.J.; Lee, J.W.; Kim, J.H.; Kim, J.Y.; Kang, K.Y.; Lee, W.S.; Park, K.H.
Characteristic of neuraminidase inhibitory xanthones from Cudrania tricuspidata
Bioorg. Med. Chem.
17
2744-2750
2009
Clostridium perfringens (Q59310)
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
Newstead, S.L.; Potter, J.A.; Wilson, J.C.; Xu, G.; Chien, C.H.; Watts, A.G.; Withers, S.G.; Taylor, G.L.
The structure of Clostridium perfringens NanI sialidase and its catalytic intermediates
J. Biol. Chem.
283
9080-9088
2008
Clostridium perfringens (Q59310), Clostridium perfringens
Manually annotated by BRENDA team
Frank, J.E.; Thompson, V.P.; Brown, M.P.; Sandy, J.D.
Removal of O-linked and N-linked oligosaccharides is required for optimum detection of NITEGE neoepitope on ADAMTS4-digested fetal aggrecans: implications for specific N-linked glycan-dependent aggrecanolysis at Glu373-Ala374
Osteoarthritis Cartilage
17
777-781
2008
Clostridium perfringens (P10481)
Manually annotated by BRENDA team
Nguyen, P.H.; Nguyen, T.N.; Kang, K.W.; Ndinteh, D.T.; Mbafor, J.T.; Kim, Y.R.; Oh, W.K.
Prenylated pterocarpans as bacterial neuraminidase inhibitors
Bioorg. Med. Chem.
18
3335-3344
2010
Clostridium perfringens, Vibrio cholerae serotype O1
Manually annotated by BRENDA team
Chiarezza, M.; Lyras, D.; Pidot, S.J.; Flores-Diaz, M.; Awad, M.M.; Kennedy, C.L.; Cordner, L.M.; Phumoonna, T.; Poon, R.; Hughes, M.L.; Emmins, J.J.; Alape-Giron, A.; Rood, J.I.
The NanI and NanJ sialidases of Clostridium perfringens are not essential for virulence
Infect. Immun.
77
4421-4428
2009
Clostridium perfringens, Clostridium perfringens type A
Manually annotated by BRENDA team
Cao, H.; Li, Y.; Lau, K.; Muthana, S.; Yu, H.; Cheng, J.; Chokhawala, H.A.; Sugiarto, G.; Zhang, L.; Chen, X.
Sialidase substrate specificity studies using chemoenzymatically synthesized sialosides containing C5-modified sialic acids
Org. Biomol. Chem.
7
5137-5145
2009
Clostridium perfringens, Streptococcus pneumoniae, Pasteurella multocida, Salmonella enterica subsp. enterica serovar Typhimurium, Vibrio cholerae serotype O1
Manually annotated by BRENDA team
Li, J.; McClane, B.A.
The sialidases of Clostridium perfringens type D strain CN3718 differ in their properties and sensitivities to inhibitors
Appl. Environ. Microbiol.
80
1701-1709
2014
Clostridium perfringens, Clostridium perfringens CN3718
Manually annotated by BRENDA team
Kim, J.H.; Ryu, Y.B.; Lee, W.S.; Kim, Y.H.
Neuraminidase inhibitory activities of quaternary isoquinoline alkaloids from Corydalis turtschaninovii rhizome
Bioorg. Med. Chem.
22
6047-6052
2014
Clostridium perfringens
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
Gattu, S.; Crihfield, C.L.; Holland, L.A.
Microscale measurements of Michaelis-Menten constants of neuraminidase with nanogel capillary electrophoresis for the determination of the sialic acid linkage
Anal. Chem.
89
929-936
2017
Clostridium perfringens
Manually annotated by BRENDA team
Lee, Y.; Youn, H.S.; Lee, J.G.; An, J.Y.; Park, K.R.; Kang, J.Y.; Ryu, Y.B.; Jin, M.S.; Park, K.H.; Eom, S.H.
Crystal structure of the catalytic domain of Clostridium perfringens neuraminidase in complex with a non-carbohydrate-based inhibitor, 2-(cyclohexylamino)ethanesulfonic acid
Biochem. Biophys. Res. Commun.
486
470-475
2017
Clostridium perfringens
Manually annotated by BRENDA team