3.2.1.18: exo-alpha-sialidase
This is an abbreviated version!
For detailed information about exo-alpha-sialidase, go to the full flat file.
Word Map on EC 3.2.1.18
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3.2.1.18
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influenza
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sialic
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viruses
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vaccine
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pandemic
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oseltamivir
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lectin
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sialylated
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oligosaccharide
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subtype
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epitope
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erythrocyte
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gangliosides
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lymphocyte
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reassortant
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hemagglutination
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anti-influenza
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chicken
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glycans
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surveillance
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galactose
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cholera
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desialylation
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hn
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glycoconjugates
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outbreak
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cruzi
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poultry
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virion
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bird
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pronase
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parainfluenza
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epidemic
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n-acetylneuraminic
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trypanosoma
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peanut
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mucin
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n-linked
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newcastle
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agglutination
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perfringens
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nucleoprotein
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prophylaxis
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concanavalin
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medicine
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drift
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sendai
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analysis
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n-acetylgalactosamine
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ferret
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nutrition
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endoglycosidase
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molecular biology
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diagnostics
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gm3
- 3.2.1.18
- influenza
-
sialic
- viruses
- vaccine
- pandemic
- oseltamivir
- lectin
-
sialylated
- oligosaccharide
- subtype
- epitope
- erythrocyte
- gangliosides
- lymphocyte
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reassortant
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hemagglutination
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anti-influenza
- chicken
- glycans
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surveillance
- galactose
- cholera
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desialylation
- hn
- glycoconjugates
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outbreak
- cruzi
-
poultry
- virion
- bird
- pronase
- parainfluenza
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epidemic
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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
Reaction
Synonyms
acetylneuraminidase, Acetylneuraminyl hydrolase, acid sialidase, acylneuraminyl glycohydrolase, alpha-N-acylneuraminate glycohydrolase, alpha-neuraminidase, alpha-sialidase, alpha2,6-sialidase, alpha2,6-sialyltransferase, alpha2,6-trans-sialidase, Am0705, Am0707, Am1757, Am2085, Cytosolic sialidase, DELTA15Pd2,6ST, endo-N, endo-N-acylneuraminidase, endo-sialidase, endoNF, endosialidase, exo-alpha-sialidase, exo-sialidase, G9 sialidase, Ganglioside sialidase, ganglioside-specific sialidase, GH33C, glycosyl hydrolase, haemagglutinin-neuraminidase protein, hemagglutinin-neuraminidase, hemagglutinin-neuraminidase glycoprotein, HN, HsNEU2, IID sialidase, KDNase, Lysosomal sialidase, Major 85 kDa surface antigen, Major surface antigen, Membrane sialidase, MmNEU3, More, Mouse skeletal muscle sialidase, MSS, MTS, mucopolysaccharide N-acetylneuraminylhydrolase, Murine thymic sialidase, N-acetyl-alpha-neuraminidase, N-acetyl-alpha-neuraminidase 1, N-acetyl-alpha-neuraminidase 2, N-acetyl-alpha-neuraminidase 3, N-acetyl-alpha-neuraminidase 4, N-acetylneuraminosyl glycohydrolase, N-acylneuraminate glycohydrolase, N-acylneuraminosyl glycohydrolase, NA, NA1, NA2, NAN1, NanA, NANase, NanB, NanC, NanH, NanI, NanICD, NanJ, NanPs, Neu, NEU1, NEU2, Neu3, Neu3a, Neu3d, Neu3e, NEU4, NEU4 long, NEU4 short, NEU4L, Neu4L sialidase, neuramindase, neuraminidase, neuraminidase 1, neuraminidase 2, neuraminidase 3, neuraminidase-1, PA2794, SA85-1.1 protein, SA85-1.2 protein, SA85-1.3 protein, SiaBb1, sialidase, sialidase 4, sialidase II, sialidase Neu2, sialidase-2, sialidase-3, sialidase-4, sialidase/neuraminidase mutant F129A, sialyl hydrolase, STNA, TcTS, TDE0471, Tr6, trans-sialidase, trans-sialidase 1, TSia, VCNA
ECTree
3.2.1.18 exo-alpha-sialidaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.2.1.18 - exo-alpha-sialidase
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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
2'-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid + H2O
?
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?
alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-R
?
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the enzyme is selective for alpha(2-3)-linked sialic acid
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?
ganglioside GM3 + H2O
sialic acid + ?
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in transfected cells, mainly via cell-cell-interaction
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?
ganglioside GD1a + H2O
ganglioside GM1 + sialic acid
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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
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-
?
ganglioside GD1a + H2O
ganglioside GM1 + sialic acid
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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
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?
ganglioside GD1a + H2O
ganglioside GM1 + sialic acid
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in transfected cells, mainly via cell-cell-interaction
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?
additional information
?
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essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification
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?
additional information
?
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essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification
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?
additional information
?
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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
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?
additional information
?
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essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification
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?
additional information
?
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essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification
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?
additional information
?
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enzyme is involved in the metabolism of gangliosides
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?
additional information
?
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essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification
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?
additional information
?
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endoNF is therefore an inverting glycosidase
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?
additional information
?
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essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification
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?
additional information
?
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enzyme is required for cellular signaling and for the production of cytokine interleukin-4 by activated T-lymphocytes, inherited enzyme defiency results in sialidosis or galactosialidosis, both severe metaboic disorders associated with lysosomal storage of oligosaccharides and glycopeptides
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?
additional information
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sialidase-3 is a key enzyme for ganglioside hydrolysis. Neu3 is an important regulator of insulin sensitivity and glucose tolerance
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?
additional information
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the Neu3 gene represents a physiological modulator of vascular smooth muscle cells responses that may contribute to plaque instability in atherosclerosis
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?
additional information
?
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increased CD15 and decreased CD15s expression during myeloid differentiation is sialidase dependent. Both CD15s synthesis and sialidase activity are induced by CD44 ligation, but the increase in sialidase activity dominates, such that the overall expression pattern upon CD44 ligation is a decrease in CD15s expression with an accompanying increase in CD15. The observed increase in CD15 results predominantly from conversion of CD15s to CD15 on glycoproteins
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?
additional information
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neuraminidase causes the desialylation of both PDGF and IGF-1 receptors and diminishes the intracellular signals induced by the mitogenic ligands PDGF-BB and IGF-2
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?
additional information
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the induction of hST3Gal V, which synthesizes ganglioside GM3 and reduction of Neu3 by phorbol 12-myristate 13-acetate, are linked for the expression of differentiation marker protein, CD41b surface antigen. Neu3 overexpression inhibits the PMA-induced ERK1/2 and p38 MAPK phosphorylation in the K-562 cells. Down-regulation of expression of CD41b surface antigen is dependent on expression of Neu3 gene. Neu3 inhibitor 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, while specific glucosylceramide synthase inhibitor 1-phenyl-2-decanoylamino-3-morpholino-1-propanol inhibits megakaryocytic differentiation of K-562 cells
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?
additional information
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sialidase NEU3 shows high enzymatic specificity toward gangliosides
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?
additional information
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essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification
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?
additional information
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the enzyme modifies the ganglioside pattern of adjacent cells, involved in cell-cell-interaction
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?
additional information
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essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification
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?
additional information
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essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification, enzyme is responsible for decomposition of organic material in various biotopes
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?
additional information
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essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification, enzyme is responsible for decomposition of organic material in various biotopes
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?
additional information
?
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essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification
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?
additional information
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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
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?
additional information
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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
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?
additional information
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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
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?
additional information
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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
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?
additional information
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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
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?
additional information
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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
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additional information
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NanB may contribute to Strreptococcus pneumoniae colonization and pathogenesis
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additional information
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NanB may contribute to Strreptococcus pneumoniae colonization and pathogenesis
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additional information
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Streptococcus pneumoniae is able to utilize complex N-linked human glycoconjugates as a sole source of carbon to sustain growth and efficient growth is dependent upon the sequential deglycosylation of the glycoconjugate substrate by pneumococcal exoglycosidases NanA, BgaA, and StrH. The second pneumococcal neuraminidase, NanB, is involved in the deglycosylation of host glycoconjugates and NanB activity can partially compensate for the loss or dysfunction of NanA
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additional information
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Streptococcus pneumoniae is able to utilize complex N-linked human glycoconjugates as a sole source of carbon to sustain growth and efficient growth is dependent upon the sequential deglycosylation of the glycoconjugate substrate by pneumococcal exoglycosidases NanA, BgaA, and StrH. The second pneumococcal neuraminidase, NanB, is involved in the deglycosylation of host glycoconjugates and NanB activity can partially compensate for the loss or dysfunction of NanA
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?
additional information
?
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essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification
-
-
?
additional information
?
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essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification
-
-
?
additional information
?
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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
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?
