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Information on EC 3.2.1.18 - exo-alpha-sialidase and Organism(s) Pasteurella multocida and UniProt Accession Q9EZV7
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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 taxonomic range for the selected organisms is: Pasteurella multocida
The enzyme appears in selected viruses and cellular organisms
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
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
alpha(2-6')-sialyllactose + H2O
sialic acid + lactose
the nanB encoded enzyme hydrolyzes both (2-3')- and (2-6')-sialyllactose, the latter substrate is preferred
-
-
?
colominic acid + H2O
sialic acid + lactose
i.e. (2-8')-sialyllactose
-
-
?
2-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferol + alpha-D-N-acetylneuraminic acid
-
-
-
-
?
2-(4-nitrophenyl)-alpha-D-N-acetylneuraminic acid + H2O
4-nitrophenol + alpha-D-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
?
-
-
-
-
?
bovine submaxillary gland mucin + H2O
sialic acid + ?
-
-
-
?
alpha(2-3')-sialyllactose + H2O
sialic acid + lactose
nanH encoded enzyme is highly specific for the (2-3')-sialyllactose
-
-
?
alpha(2-3')-sialyllactose + H2O
sialic acid + lactose
the nanB encoded enzyme hydrolyzes both 2-3'- and 2-6'-sialyllactose
-
-
?
additional information
?
-
most strains of Pasteurella multocida produce sialidase activity which may contribute to colonization of the respiratory tract by the mucosal pathogen, or for production of lesions in an actiev infection
-
-
?
additional information
?
-
most strains of Pasteurella multocida produce sialidase activity which may contribute to colonization of the respiratory tract by the mucosal pathogen, or for production of lesions in an actiev infection
-
-
?
additional information
?
-
-
most strains of Pasteurella multocida produce sialidase activity which may contribute to colonization of the respiratory tract by the mucosal pathogen, or for production of lesions in an actiev infection
-
-
?
additional information
?
-
most strains of Pasteurella multocida produce sialidase activity which may contribute to colonization of the respiratory tract by the mucosal pathogen, or for production of lesions in an active infection
-
-
?
additional information
?
-
most strains of Pasteurella multocida produce sialidase activity which may contribute to colonization of the respiratory tract by the mucosal pathogen, or for production of lesions in an active infection
-
-
?
additional information
?
-
-
most strains of Pasteurella multocida produce sialidase activity which may contribute to colonization of the respiratory tract by the mucosal pathogen, or for production of lesions in an active infection
-
-
?
additional information
?
-
-
essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification
-
-
?
additional information
?
-
substrate specificity, no or poor activity with ganglioside GM1, colominic acid, and alpha(2-6')-sialyllactose
-
-
?
additional information
?
-
substrate specificity, no or poor activity with ganglioside GM1, colominic acid, and alpha(2-6')-sialyllactose
-
-
?
additional information
?
-
-
substrate specificity, no or poor activity with ganglioside GM1, colominic acid, and alpha(2-6')-sialyllactose
-
-
?
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
?
-
most strains of Pasteurella multocida produce sialidase activity which may contribute to colonization of the respiratory tract by the mucosal pathogen, or for production of lesions in an actiev infection
-
-
?
additional information
?
-
most strains of Pasteurella multocida produce sialidase activity which may contribute to colonization of the respiratory tract by the mucosal pathogen, or for production of lesions in an actiev infection
-
-
?
additional information
?
-
-
most strains of Pasteurella multocida produce sialidase activity which may contribute to colonization of the respiratory tract by the mucosal pathogen, or for production of lesions in an actiev infection
-
-
?
additional information
?
-
most strains of Pasteurella multocida produce sialidase activity which may contribute to colonization of the respiratory tract by the mucosal pathogen, or for production of lesions in an active infection
-
-
?
additional information
?
-
most strains of Pasteurella multocida produce sialidase activity which may contribute to colonization of the respiratory tract by the mucosal pathogen, or for production of lesions in an active infection
-
-
?
additional information
?
-
-
most strains of Pasteurella multocida produce sialidase activity which may contribute to colonization of the respiratory tract by the mucosal pathogen, or for production of lesions in an active infection
-
-
?
additional information
?
-
-
essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.063
alpha(2-3')-sialyllactose
recombinant enzyme, pH 6.8, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene nanB, from fowl cholera isolates, quantitiative relation of the 2 sialidase ativities, encoded by genes nanB and nanH, in different isolates, overview
SwissProt
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
insertional inactivation of nanH results in a mutant, which is not deficient in sialidase production, but exhibits reduced activity
additional information
insertional inactivation of nanH results in a mutant, which is not deficient in sialidase production, but exhibits reduced activity
additional information
-
insertional inactivation of nanH results in a mutant, which is not deficient in sialidase production, but exhibits reduced activity
additional information
insertional inactivation of nanH, encoding the second sialidase of the organism, results in a mutant, which is not deficient in sialidase production, but exhibits reduced activity
additional information
insertional inactivation of nanH, encoding the second sialidase of the organism, results in a mutant, which is not deficient in sialidase production, but exhibits reduced activity
additional information
-
insertional inactivation of nanH, encoding the second sialidase of the organism, results in a mutant, which is not deficient in sialidase production, but exhibits reduced activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli, 950fold, by ammonium sulfate precipitation, and several chromatographic steps
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene nanB, DNA and amino acid sequence determination and analysis, expression in Escherichia coli of the gene rendering the recombinant cells capable of utilizing several sialoconjugates when grown on a minimal medium with these conjugates as sole carbon source
genes nanH, DNA and amino acid sequence determination and analysis, expression in Escherichia coli of the gene rendering the recombinant cells capable of utilizing several sialoconjugates when grown on a minimal medium with these conjugates as sole carbon source
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Mizan, S.; Henk, A.; Stallings, A.; Maier, M.; Lee, M.D.
Cloning and characterization of sialidases with 2-6' and 2-3' sialyl lactose specificity from Pasteurella multocida
J. Bacteriol.
182
6874-6883
2000
Pasteurella multocida (Q9EZV6), Pasteurella multocida (Q9EZV7), Pasteurella multocida
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
EXTERNAL LINKS (specific for EC-Number 3.2.1.18)
Transporter Classification Database (TCDB): 1.A.32.1.3
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