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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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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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Select one or more organisms in this record:
This record set is specific for:
Influenza B virus
UNIPROT: P27907
Word Map
The taxonomic range for the selected organisms is: Influenza B virus
The enzyme appears in selected viruses and cellular organisms
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylneuraminidase
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Acetylneuraminyl hydrolase
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acylneuraminyl glycohydrolase
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alpha-neuraminidase
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Cytosolic sialidase
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G9 sialidase
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Ganglioside sialidase
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Lysosomal sialidase
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Major 85 kDa surface antigen
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Major surface antigen
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Membrane sialidase
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Mouse skeletal muscle sialidase
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MSS
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MTS
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mucopolysaccharide N-acetylneuraminylhydrolase
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Murine thymic sialidase
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N-acetyl-alpha-neuraminidase
278728
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N-acylneuraminate glycohydrolase
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NANase
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neuraminidase
SA85-1.1 protein
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SA85-1.2 protein
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SA85-1.3 protein
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sialidase
STNA
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + N-acetylneuraminic acid
show the reaction diagram
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-
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-
?
fetuin + H2O
?
show the reaction diagram
-
-
-
-
?
fetuin + H2O
sialic acid + ?
show the reaction diagram
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-
-
?
additional information
?
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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
fetuin + H2O
?
show the reaction diagram
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-
-
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?
fetuin + H2O
sialic acid + ?
show the reaction diagram
Q80A54, Q80A58
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
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(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
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(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
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(2R,4S,5R)-5-[(1R,2S)-1-(acetylamino)-2-hydroxy-2-methylpentyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
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(2R,4S,5R)-5-[(1R,2S)-1-(acetylamino)-2-methoxy-2-methylpentyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
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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
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(2R,4S,5R)-5-[(1S,2S)-1-(acetylamino)-2-hydroxybutyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
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(2R,4S,5R)-5-[(2S)-1-(acetylamino)-2-hydroxypent-4-en-1-yl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
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(2R,4S,5R)-5-[(2S)-1-(acetylamino)-2-hydroxypentyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
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2-((E)-4'-hydroxyphenylidene)-4,6-dihydroxy-2,3-dihydrobenzofuran-3-one
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2-((E)-4'-hydroxyphenylidene)-6-hydroxy-2,3-dihydrobenzofuran-3-one
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apigenin
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laninamivir
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luteolin
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oseltamivir
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oseltamivir carboxylate
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peramivir
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sulfuretin
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
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-
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
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-
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
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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
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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
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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
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-
0.0000028
(2R,4S,5R)-5-[(1S,2S)-1-(acetylamino)-2-hydroxybutyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
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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
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0.0000013
(2R,4S,5R)-5-[(2S)-1-(acetylamino)-2-hydroxypentyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
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0.0000011
oseltamivir carboxylate
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0.0000001
zanamivir
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000254
2-((E)-4'-hydroxyphenylidene)-4,6-dihydroxy-2,3-dihydrobenzofuran-3-one
influenza B virus
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pH 6.5, 37°C
0.0000229
2-((E)-4'-hydroxyphenylidene)-6-hydroxy-2,3-dihydrobenzofuran-3-one
influenza B virus
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pH 6.5, 37°C
0.0000457
apigenin
influenza B virus
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pH 6.5, 37°C
0.0000332
dinatin
influenza B virus
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pH 6.5, 37°C
0.00000311 - 0.00001747
laninamivir
0.0000533
luteolin
influenza B virus
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pH 6.5, 37°C
0.000000217
oseltamivir
influenza B virus
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pH 6.5, 37°C
0.00000228 - 0.00002525
oseltamivir carboxylate
0.00000076 - 0.0001273
peramivir
0.0000512
sulfuretin
influenza B virus
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pH 6.5, 37°C
0.0000013 - 0.00002371
zanamivir
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
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
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
G140R
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the mutation is associated with reduced susceptibility to neuraminidase inhibitors
P139S
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the mutation is associated with reduced susceptibility to neuraminidase inhibitors
Q138R
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the mutation is associated with reduced susceptibility to neuraminidase inhibitors
R152K
the mutation leads to resistance against nfluenza virus neuraminidase inhibitors
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme activity is not influenced by 0.1% (w/v) RapiGest
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deoxycholate
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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, influenza B virus (Q80A54), influenza B virus (Q80A58)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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 A virus A/N1/PR/8/34, influenza B virus, influenza B virus B/Memphis/3/89
Manually annotated by BRENDA team
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 A virus A/Jinan/15/90, influenza A virus A/PR/8/34, influenza B virus, influenza B virus B/Jiangsu/10/2003
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Sultana, I.; Yang, K.; Getie-Kebtie, M.; Couzens, L.; Markoff, L.; Alterman, M.; Eichelberger, M.C.
Stability of neuraminidase in inactivated influenza vaccines
Vaccine
32
2225-2230
2014
influenza A virus, influenza A virus H3N2, influenza B virus
Manually annotated by BRENDA team
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