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Information on EC 3.2.1.18 - exo-alpha-sialidase and Organism(s) Influenza B virus and UniProt Accession P27907
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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: Influenza B virus
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 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
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + N-acetylneuraminic acid
-
-
-
-
?
additional information
?
-
plaque formation on MDCK and Vero cells at different temperatures, investigation of influence of different hemagglutinin and neuraminidase combinations on enzyme activity
-
-
?
additional information
?
-
plaque formation on MDCK and Vero cells at different temperatures, investigation of influence of different hemagglutinin and neuraminidase combinations on enzyme activity
-
-
?
additional information
?
-
-
plaque formation on MDCK and Vero cells at different temperatures, investigation of influence of different hemagglutinin and neuraminidase combinations on enzyme activity
-
-
?
additional information
?
-
plaque formation on MDCK and Vero cells, investigation of influence of different hemagglutinin and neuraminidase combinations on enzyme activity
-
-
?
additional information
?
-
plaque formation on MDCK and Vero cells, investigation of influence of different hemagglutinin and neuraminidase combinations on enzyme activity
-
-
?
additional information
?
-
-
plaque formation on MDCK and Vero cells, investigation of influence of different hemagglutinin and neuraminidase combinations on enzyme activity
-
-
?
additional information
?
-
-
egg or Madin Darby canine kidney cell isolated virus strains tend to exhibit highest activity against 3'-sialyl-bound sialic acid whereas Vero isolated strain favour 6'-sialyl-(N-acetyllactosamine)-bound 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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,4S,5R)-5-[(1R,2R)-1-(acetylamino)-2-ethoxybut-3-en-1-yl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
(2R,4S,5R)-5-[(1R,2R)-1-(acetylamino)-2-methoxybut-3-en-1-yl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
(2R,4S,5R)-5-[(1R,2R)-1-(acetylamino)-2-methoxypent-4-en-1-yl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
(2R,4S,5R)-5-[(1R,2S)-1-(acetylamino)-2-hydroxy-2-methylpentyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
(2R,4S,5R)-5-[(1R,2S)-1-(acetylamino)-2-methoxy-2-methylpentyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
i.e. A-315675
(2R,4S,5R)-5-[(1S,2S)-1-(acetylamino)-2-hydroxybut-3-en-1-yl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
(2R,4S,5R)-5-[(1S,2S)-1-(acetylamino)-2-hydroxybutyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
(2R,4S,5R)-5-[(2S)-1-(acetylamino)-2-hydroxypent-4-en-1-yl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
(2R,4S,5R)-5-[(2S)-1-(acetylamino)-2-hydroxypentyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
2-((E)-4'-hydroxyphenylidene)-4,6-dihydroxy-2,3-dihydrobenzofuran-3-one
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000048
(2R,4S,5R)-5-[(1R,2R)-1-(acetylamino)-2-ethoxybut-3-en-1-yl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
0.0000006
(2R,4S,5R)-5-[(1R,2R)-1-(acetylamino)-2-methoxybut-3-en-1-yl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
0.00000067
(2R,4S,5R)-5-[(1R,2R)-1-(acetylamino)-2-methoxypent-4-en-1-yl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
0.0000012
(2R,4S,5R)-5-[(1R,2S)-1-(acetylamino)-2-hydroxy-2-methylpentyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
0.00000014
(2R,4S,5R)-5-[(1R,2S)-1-(acetylamino)-2-methoxy-2-methylpentyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
0.000002
(2R,4S,5R)-5-[(1S,2S)-1-(acetylamino)-2-hydroxybut-3-en-1-yl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
0.0000028
(2R,4S,5R)-5-[(1S,2S)-1-(acetylamino)-2-hydroxybutyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
0.0000016
(2R,4S,5R)-5-[(2S)-1-(acetylamino)-2-hydroxypent-4-en-1-yl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
0.0000013
(2R,4S,5R)-5-[(2S)-1-(acetylamino)-2-hydroxypentyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000254
2-((E)-4'-hydroxyphenylidene)-4,6-dihydroxy-2,3-dihydrobenzofuran-3-one
influenza B virus
-
pH 6.5, 37°C
0.0000229
2-((E)-4'-hydroxyphenylidene)-6-hydroxy-2,3-dihydrobenzofuran-3-one
influenza B virus
-
pH 6.5, 37°C
0.00000311
laninamivir
influenza B virus
-
wild type enzyme, strain B/Kochi/60/2011, pH and temperature not specified in the publication
0.00000419
laninamivir
influenza B virus
-
wild type enzyme, strain B/Kochi/41/2011, pH and temperature not specified in the publication
0.00000468
laninamivir
influenza B virus
-
wild type enzyme, strain B/Kochi/59/2011, pH and temperature not specified in the publication
0.00001161
laninamivir
influenza B virus
-
mutant enzyme P139S, strain B/Kochi/41/2011, pH and temperature not specified in the publication
0.00001343
laninamivir
influenza B virus
-
mutant enzyme Q138R, strain B/Kochi/60/2011, pH and temperature not specified in the publication
0.00001747
laninamivir
influenza B virus
-
mutant enzyme G140R, strain B/Kochi/59/2011, pH and temperature not specified in the publication
0.00000228
oseltamivir carboxylate
influenza B virus
-
mutant enzyme Q138R, strain B/Kochi/60/2011, pH and temperature not specified in the publication
0.0000026
oseltamivir carboxylate
influenza B virus
-
wild type enzyme, strain B/Kochi/60/2011, pH and temperature not specified in the publication
0.0000039
oseltamivir carboxylate
influenza B virus
-
wild type enzyme, strain B/Kochi/59/2011, pH and temperature not specified in the publication
0.00000498
oseltamivir carboxylate
influenza B virus
-
wild type enzyme, strain B/Kochi/41/2011, pH and temperature not specified in the publication
0.00002305
oseltamivir carboxylate
influenza B virus
-
mutant enzyme G140R, strain B/Kochi/59/2011, pH and temperature not specified in the publication
0.00002525
oseltamivir carboxylate
influenza B virus
-
mutant enzyme P139S, strain B/Kochi/41/2011, pH and temperature not specified in the publication
0.00000076
peramivir
influenza B virus
-
wild type enzyme, strain B/Kochi/41/2011, pH and temperature not specified in the publication
0.00000079
peramivir
influenza B virus
-
wild type enzyme, strain B/Kochi/60/2011, pH and temperature not specified in the publication
0.00000097
peramivir
influenza B virus
-
wild type enzyme, strain B/Kochi/59/2011, pH and temperature not specified in the publication
0.00001614
peramivir
influenza B virus
-
mutant enzyme Q138R, strain B/Kochi/60/2011, pH and temperature not specified in the publication
0.000127
peramivir
influenza B virus
-
mutant enzyme P139S, strain B/Kochi/41/2011, pH and temperature not specified in the publication
0.0001273
peramivir
influenza B virus
-
mutant enzyme G140R, strain B/Kochi/59/2011, pH and temperature not specified in the publication
0.0000013
zanamivir
influenza B virus
-
wild type enzyme, strain B/Kochi/60/2011, pH and temperature not specified in the publication
0.00000156
zanamivir
influenza B virus
-
wild type enzyme, strain B/Kochi/41/2011, pH and temperature not specified in the publication
0.00000175
zanamivir
influenza B virus
-
wild type enzyme, strain B/Kochi/59/2011, pH and temperature not specified in the publication
0.0000122
zanamivir
influenza B virus
-
mutant enzyme Q138R, strain B/Kochi/60/2011, pH and temperature not specified in the publication
0.00001998
zanamivir
influenza B virus
-
mutant enzyme P139S, strain B/Kochi/41/2011, pH and temperature not specified in the publication
0.00002371
zanamivir
influenza B virus
-
mutant enzyme G140R, strain B/Kochi/59/2011, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains B/Memphis/20/96, B/Memphis/20-152K/96, B/Hong Kong/45/2005, and B/Hong Kong/36/2005
Uniprot
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of the enzyme alone or in complex with sialic acid, modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R152K
the mutation leads to resistance against nfluenza virus neuraminidase inhibitors
G140R
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
P139S
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
Q138R
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
deoxycholate
-
incubation with 1% (w/v) deoxycholate results in no significant loss of enzyme activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, comparison to other strains
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Katinger, D.; Romanova, J.; Ferko, B.; Fekete, H.; Egorov, A.
Effect of a single mutation in neuraminidase on the properties of Influenza B virus isolates
Arch. Virol.
149
173-181
2004
influenza B virus (Q80A54), influenza B virus (Q80A58), influenza B virus
Katinger, D.; Mochalova, L.; Chinarev, A.; Bovin, N.; Romanova, J.
Specificity of neuraminidase activity from influenza viruses isolated in different hosts tested with novel substrates
Arch. Virol.
149
2131-2140
2004
influenza A virus, influenza B virus
Krueger, A.C.; Xu, Y.; Kati, W.M.; Kempf, D.J.; Maring, C.J.; McDaniel, K.F.; Molla, A.; Montgomery, D.; Kohlbrenner, W.E.
Synthesis of potent pyrrolidine influenza neuraminidase inhibitors
Bioorg. Med. Chem. Lett.
18
1692-1695
2008
influenza A virus, influenza B virus, influenza B virus B/Memphis/3/89, influenza A virus A/N1/PR/8/34
Liu, A.L.; Wang, H.D.; Lee, S.M.; Wang, Y.T.; Du, G.H.
Structure-activity relationship of flavonoids as influenza virus neuraminidase inhibitors and their in vitro anti-viral activities
Bioorg. Med. Chem.
16
7141-7147
2008
influenza A virus, influenza B virus, influenza A virus A/Jinan/15/90, influenza A virus A/PR/8/34, influenza B virus B/Jiangsu/10/2003
Mochalova, L.; Bright, R.; Xu, X.; Korchagina, E.; Chinarev, A.; Bovin, N.; Klimov, A.
Shift in oligosaccharide specificities of hemagglutinin and neuraminidase of influenza B viruses resistant to neuraminidase inhibitors
Glycoconj. J.
27
321-327
2010
influenza B virus (P27907)
Fujisaki, S.; Imai, M.; Takashita, E.; Taniwaki, T.; Xu, H.; Kishida, N.; Yokoyama, M.; Sato, H.; Tashiro, M.; Odagiri, T.
Mutations at the monomer-monomer interface away from the active site of influenza B virus neuraminidase reduces susceptibility to neuraminidase inhibitor drugs
J. Infect. Chemother.
19
891-895
2013
influenza B virus, influenza B virus B/Kochi/41/2011, influenza B virus B/Kochi/59/2011, influenza B virus B/Kochi/60/2011
EXTERNAL LINKS (specific for EC-Number 3.2.1.18)
Transporter Classification Database (TCDB): 1.A.32.1.3
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