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Information on EC 3.2.1.18 - exo-alpha-sialidase and Organism(s) Vibrio cholerae serotype O1 and UniProt Accession P0C6E9
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3.2.1.18 exo-alpha-sialidaseIUBMB 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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Word Map
- 3.2.1.18
- influenza
-
sialic
- viruses
- vaccine
- pandemic
- oseltamivir
- lectin
-
sialylated
- oligosaccharide
- subtype
- epitope
- erythrocyte
- gangliosides
- lymphocyte
-
reassortant
-
hemagglutination
-
anti-influenza
- chicken
- glycans
-
surveillance
- galactose
- cholera
-
desialylation
- hn
- glycoconjugates
-
outbreak
- cruzi
-
poultry
- virion
- bird
- pronase
- parainfluenza
-
epidemic
-
n-acetylneuraminic
- trypanosoma
- peanut
- mucin
-
n-linked
- newcastle
-
agglutination
- perfringens
- nucleoprotein
-
prophylaxis
-
concanavalin
- medicine
-
drift
-
sendai
- analysis
- n-acetylgalactosamine
- ferret
- nutrition
-
endoglycosidase
- molecular biology
- diagnostics
- gm3
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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-acylneuraminate glycohydrolase
-
-
-
-
NANase
-
-
-
-
neuraminidase
SA85-1.1 protein
-
-
-
-
SA85-1.2 protein
-
-
-
-
SA85-1.3 protein
-
-
-
-
sialidase
STNA
-
-
-
-
neuraminidase
-
-
-
-
sialidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
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
exo-glycosidase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
9001-67-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferol + alpha-D-N-acetylneuraminic acid
-
-
-
-
?
2-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + N-acetyl-alpha-D-neuraminic acid
-
-
-
-
?
2-(4-nitrophenyl)-alpha-D-N-acetylneuraminic acid + H2O
4-nitrophenol + alpha-D-N-acetylneuraminic acid
-
-
-
-
?
2-chloro-5-(4-methoxyspiro(1,2-dioxetane-3,29-(5-chloro)tricyclo[3.3.1.13,7]decan)-4-yl-phenyl-5-acetamido-3,5-dideoxy-alpha-D-glycero-D-galacto-2-nonulopyranoside)onate + H2O
?
-
-
-
-
?
4-methylumbelliferyl alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + N-acetylneuraminic acid
-
-
-
-
?
4-nitrophenyl O-(3,5-dideoxy-5-fluoro-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-3)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-(3,5-dideoxy-5-fluoro-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-6)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-(3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-3)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-(3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-6)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-(3-deoxy-5-O-methyl-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-3)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-(3-deoxy-5-O-methyl-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-6)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-(5-azido-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-3)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-(5-azido-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-6)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-[5-(2-azidoacetamido)-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid]-(2-3)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-[5-(2-azidoacetamido)-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid]-(2-6)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-[5-(2-fluoroacetamido)-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid]-(2-3)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-[5-(2-fluoroacetamido)-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid]-(2-6)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-[5-(2-methoxyacetamido)-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid]-(2-3)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-[5-(2-methoxyacetamido)-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid]-(2-6)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
N-(2,4,7,8,9-penta-O-acetyl-N-acetyl-beta-D-neuraminoyl)phenylalanine methylester + H2O
?
-
-
-
-
?
N-(4,7,8,9-tetra-O-acetyl-N-acetyl-2-O-benzyl-alpha-D-neuraminoyl)phenylalanine methylester + H2O
?
-
-
-
-
?
Neu5Gcalpha-(2-8)-Neu5Ac + H2O
Neu5Gc + Neu5Ac
-
preferred substrate
-
-
?
additional information
?
-
-
essential enzyme, enzyme containing culture filtrate possesses the ability to agglutinate 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
-
-
?
additional information
?
-
-
no activity with sialyl-alpha-(2-8)-sialic acid
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
essential enzyme, enzyme containing culture filtrate possesses the ability to agglutinate 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
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-deoxy-2,3-dehydro-N-acetylneuraminic acid
-
inhibition occurs in the micromolar range
5-acetamido-2-(4-N-5-dimethylaminonaphthalene-1-sulfonyl-2-difluoromethylphenyl)3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosonic acid
-
irreversible and competitive
asteropine A
-
a conotoxin-like peptide from the marine sponge Asteropus simplex, competitive 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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.9
5-acetamido-2-(4-N-5-dimethylaminonaphthalene-1-sulfonyl-2-difluoromethylphenyl)3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosonic acid
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
carbohydrate-binding module CBM40 of sialidase, showing high affinity for sialic acid and specificity to alpha(2,3), alpha(2,6), and alpha(2,8)-linked sialosides
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
subcloning of carbohydrate-binding module CBM40 of sialidase, showing high affinity for sialic acid and specificity to alpha(2,3), alpha(2,6), and alpha(2,8)-linked sialosides. Creation of polypeptides containing up to four CBM40 modules in tandem show increased affinities compared with the single module molecule. Variation in linker length has little effect on affinity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
subcloning of carbohydrate-binding module CBM40 of sialidase, showing high affinity for sialic acid and specificity to alpha(2,3), alpha(2,6), and alpha(2,8)-linked sialosides. Creation of polypeptides containing up to four CBM40 modules in tandem show increased affinities compared with the single module molecule. Variation in linker length has little effect on affinity
medicine
-
bacterial neuraminidases functions as the predominant neuraminidase when influenza virus neuraminidase is inhibited to promote the spread of infection and to inactivate the neutralization activity of saliva. Neuraminidase from bacterial flora in patients may reduce the efficacy of neuraminidase inhibitor drugs during influenza virus infection
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eschenfelder, V.; Brossmer, R.; Wachter, M.
On the specificity of sialidase: synthesis and properties of N5-acetyl-beta-D-neuraminoylpeptides - AcNeu-Gly-OH, AcNeu-Glu-OH, AcNeu-Phe-OH - and the corresponding alpha-ketosides
Hoppe-Seyler's Z. Physiol. Chem.
364
1411-1417
1983
Vibrio cholerae serotype O1
Gottschalk, A.
Neuraminidase
The Enzymes, 2nd Ed (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
4
461-473
1960
unidentified influenza virus, Vibrio cholerae serotype O1
-
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
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
-
Hinou, H.; Kurogochi, M.; Shimizu, H.; Nishimura, S.
Characterization of Vibrio cholerae neuraminidase by a novel mechanism-based fluorescent labeling reagent
Biochemistry
44
11669-11675
2005
Vibrio cholerae serotype O1
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
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
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
Nishikawa, T.; Shimizu, K.; Tanaka, T.; Kuroda, K.; Takayama, T.; Yamamoto, T.; Hanada, N.; Hamada, Y.
Bacterial neuraminidase rescues influenza virus replication from inhibition by a neuraminidase inhibitor
PLoS ONE
7
e45371
2012
Paenarthrobacter ureafaciens, Streptococcus pneumoniae, influenza A virus, Vibrio cholerae serotype O1, Streptococcus pneumoniae IID553
EXTERNAL LINKS (specific for EC-Number 3.2.1.18)
Transporter Classification Database (TCDB): 1.A.32.1.3
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