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Information on EC 3.2.1.18 - exo-alpha-sialidase and Organism(s) Influenza A virus and UniProt Accession Q07599
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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 A 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
-
-
-
-
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
reaction and kinetic mechanisms
-
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-methylumbelliferone + N-acetylneuraminic acid
-
-
-
?
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 + 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-methylumbelliferol + alpha-D-N-acetylneuraminic acid
-
-
-
-
?
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + N-acetylneuraminic acid
alpha(2-3)-sialyllactose + H2O
sialic acid + lactose
-
preference for alpha(2-3)-linkages
-
-
?
Candida albicans cells + H2O
desialylated Candida albicans cells + sialic acid
-
-
-
-
?
Neu5Ac-alpha-(2->3)-Gal-beta-4-nitrophenol + H2O
Neu5Ac + 4-nitrophenyl beta-D-galactopyranoside
-
-
-
-
?
Neu5Ac-alpha-(2->6)-Gal-beta-4-nitrophenol + H2O
Neu5Ac + 4-nitrophenyl beta-D-galactopyranoside
-
-
-
-
?
Neu5AcF-alpha-(2->3)-Gal-beta-4-nitrophenol + H2O
Neu5AcF + 4-nitrophenyl beta-D-galactopyranoside
-
-
-
-
?
Neu5glycolyl-alpha-(2->3)-Gal-beta-4-nitrophenol + H2O
N-glycolylneuraminic acid + 4-nitrophenyl beta-D-galactopyranoside
-
-
-
-
?
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]-3,4-dimethylpyridinium + H2O
sialic acid + 3,4-dimethylpyridine
-
-
-
-
?
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]-3-methylpyridinium + H2O
sialic acid + 3-methylpyridine
-
-
-
-
?
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]-4-methylpyridinium + H2O
sialic acid + 4-methylpyridine
-
-
-
-
?
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]pyridinium + H2O
sialic acid + pyridine
-
-
-
-
?
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + N-acetylneuraminic acid
-
-
-
-
?
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + N-acetylneuraminic acid
-
-
-
?
additional information
?
-
-
enzyme agglutinates erythrocytes from human blood
-
-
?
additional information
?
-
-
spontaneous hydrolysis of pyridinium salts of alpha-D-N-acetylneuraminic acid occurs via 2 different ways, effects on the enzymic reaction mechanism are investigated
-
-
?
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
-
-
?
additional information
?
-
-
neuraminidase substrate specificity study of human and avian influenza A viruses, using a library of twenty alpha23- or alpha26-linked para-nitrophenol-tagged sialylgalactosides and thirty-seven strains of human and avian influenza A viruses, overview. Neuraminidases of all viruses tested cleave both alpha2-3- and alpha2-6-linked sialosides but prefer alpha23-linked ones and the activity is dependent on the terminal sialic acid structure
-
-
?
additional information
?
-
-
substrate specificity of the viral enzyme with sialic acid, methyl 3'-sialyllactoside, methyl 6'-sialyllactoside, ligand conformations, enzyme-ligand interactions, and loop flexibility, analyzed by molecular docking and molecular dynamics simulations, and molecular modeling, overview. Methyl 3'-sialyllactoside has only weak interactions with the 150-loop, whereas the enzyme N1-methyl 6'-sialyllactoside complex shows strong interactions. The avian neuraminidase N1 preferentially cleaves sialic acid from alpha-(2-3)-Gal glycoconjugates over alpha-(2-6)-Gal, also due to the altered flexibility of loops in and around the active site
-
-
?
additional information
?
-
-
the enzyme shows higher activity on alpha2,3-linked sialic acid than alpha2,6-linked
-
-
?
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
Ca2+
Mg2+
-
activates about 2fold, increase in initial reaction velocity, required
additional information
-
decrease in activity through removal of divalent cations results in decreased immunogenicity, antibody response decreases by about 68-76%, 80% of the original activity is restored by addition of Ca2+ and Mg2+
Ca2+
-
activates about 2fold, increase in initial reaction velocity, required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R/S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-(4-phenethyl-[1,2,3]triazol-1-yl)cyclohex-2-ene-1-carboxylic acid
-
-
(1R/S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-[4-(1-hydroxy-1-methylethyl)[1,2,3]triazol-1-yl]cyclohex-2-ene-1-carboxylic acid
-
-
(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
-
-
(3R,4R,5R)-4-acetamido-3-(1-(diaminomethylamino)-3-hydroxypropan-2-yloxy)-5-((1S)-1,2,3-trihydroxypropyl)cyclohex-1-enecarboxylic acid
-
obtained by structure-based design using crystal structure PDB ID 2hty and in order to exploit experimentally identified potential benefits offered by the 150-cavity adjacent to the H5N1 neuramindase active site. Inhibitor shows low binding free energy
(3R,4R,5R)-4-acetamido-5-((1S)-2-carboxy-1,2-dihydroxyethyl)-3-(1-(diaminomethylamino)-3-hydroxypropan-2-yloxy)cyclohex-1-enecarboxylic acid
-
obtained by structure-based design using crystal structure PDB ID 2hty and in order to exploit experimentally identified potential benefits offered by the 150-cavity adjacent to the H5N1 neuramindase active site. Inhibitor shows low binding free energy
(3S,4R,5R)-4-acetamido-3-amino-5-(1-ethylpropoxy)cyclohex-1-ene-1-carboxylic acid
-
-
(3S,4R,5R)-4-acetamido-3-[4-((17alpha)-estra-1,3,5(10)-triene-3,17-dihydroxy-17-yl)[1,2,3]triazol-1-yl]-5-(1-ethylpropoxy)cyclohex-1-ene-1-carboxylic acid
-
-
(3S,4R,5R)-4-acetamido-5-(1-ethyl-propoxy)-3-[4-(1-hydroxypropyl)[1,2,3]triazol-1-yl]cyclohex-1-ene-1-carboxylic acid
-
-
(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-(4-phenethyl-[1,2,3]triazol-1-yl)cyclohex-1-ene-1-carboxylic acid
-
-
(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-guanidinocyclohex-1-ene-1-carboxylic acid
-
-
(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-[4-(1-hydroxy-1-methylethyl)[1,2,3]triazol-1-yl]cyclohex-1-ene-1-carboxylic acid
-
-
(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-[4-(1-hydroxycyclohexyl)[1,2,3]triazol-1-yl]cyclohex-1-ene-1-carboxylic acid
-
-
(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-[4-(1-hydroxycyclopentyl)[1,2,3]triazol-1-yl]cyclohex-1-ene-1-carboxylic acid
-
-
(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-[4-(3-hydroxypropyl)[1,2,3]triazol-1-yl]cyclohex-1-ene-1-carboxylic acid
-
-
(4R)-2-(2-carboxyphenyl)-3-(chloroacetyl)-1,3-thiazolidine-4-carboxylic acid
-
-
(4R)-2-(2-carboxyphenyl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
-
-
(4R)-2-(2-hydroxy-3-methoxyphenyl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
-
-
(4R)-2-(2-hydroxyphenyl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
-
-
(4R)-2-(2-nitrophenyl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
-
-
(4R)-2-(4-cyanophenyl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
-
-
(4R)-2-(furan-2-yl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
-
-
(4R)-3-(chloroacetyl)-2-(2-hydroxy-3-methoxyphenyl)-1,3-thiazolidine-4-carboxylic acid
-
-
(4R)-3-(chloroacetyl)-2-(2-hydroxyphenyl)-1,3-thiazolidine-4-carboxylic acid
-
-
(4R)-3-(chloroacetyl)-2-(2-nitrophenyl)-1,3-thiazolidine-4-carboxylic acid
-
-
(4R)-3-(chloroacetyl)-2-(4-cyanophenyl)-1,3-thiazolidine-4-carboxylic acid
-
-
(4R)-3-(chloroacetyl)-2-(furan-2-yl)-1,3-thiazolidine-4-carboxylic acid
-
-
(4R)-3-glycyl-2-(2-hydroxy-3-methoxyphenyl)-1,3-thiazolidine-4-carboxylic acid
-
-
2-((E)-4'-hydroxyphenylidene)-4,6-dihydroxy-2,3-dihydrobenzofuran-3-one
-
-
CID2601775
-
the IUPAC name is 2-[(4-amino-5-cyclopropyl-1,2,4-triazol-3-yl)sulfanyl]-N-(cyclopentylcarbamoyl)acetamide
CID9796290
-
the IUPAC name is 6-[2-[[2-[(2S)-2-cyanopyrrolidin-1-yl]-2-oxoethyl]amino]ethylamino]pyridine-3-carbonitrile
lung surfactant protein A
-
lung surfactant protein D has greater neuraminidase inhibitory activity than mannose-binding lectin, which in turn has greater activity than lung surfactant protein A
-
lung surfactant protein D
-
neuraminidase inhibition by lung surfactant protein D correlates with binding of its carbohydrate recognition domain to oligomannose oligosaccharides on the viral hemagglutinin. The effects of lung surfactant protein D are additive with oseltamivir. Neuraminidase inhibition is observed using fetuin or MDCK cells as a substrate, but not in assays using a soluble sialic acid analogue. Lung surfactant protein D has greater neuraminidase inhibitory activity than mannose-binding lectin, which in turn has greater activity than lung surfactant protein A
-
mannose-binding lectin
-
lung surfactant protein D has greater neuraminidase inhibitory activity than mannose-binding lectin, which in turn has greater activity than lung surfactant protein A
-
2-deoxy-2,3-dehydro-N-acetylneuraminic acid
-
inhibition occurs in the micromolar range
oseltamivir
-
-
oseltamivir
-
the robust neuraminidase activity of the 2009H1N1 virus is responsible for the high sensitivity of the virus to oseltamivir
sulfuretin
-
i.e. 2-(Z-3',4'-dihydroxyphenylidene)-6-hydroxy-2,3-dihydrobenzofuran-3-one
additional information
-
construction of homologous and heterologous dimers and trimers and trimers of inhibitors such as oseltamivir(R)-CH2-(R)oseltamivir, oseltamivir(R)-O-zanamivir, oseltamivir(R)-CH2-2-deoxy-2,3-dehydro-N-acetylneuraminic acid and calculation of molecular properties and ligand efficiency values
-
additional information
-
design Influenza NA inhibitors that exhibit increased activity based on thiazolidine ring, evaluation of thiazolidine-4-carboxylic acid derivatives as Influenza neuraminidase inhibitors
-
additional information
-
inhibitory activity of triazole-containing carbocycles related to oseltamivir against virus-like particles containing the influenza virus neuraminidase-1 activity, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.261 - 0.385
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]-3,4-dimethylpyridinium
0.138 - 0.14
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]-3-methylpyridinium
0.45
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]-4-methylpyridinium
-
pH 9.5, 37°C
0.021 - 0.216
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]pyridinium
0.261
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]-3,4-dimethylpyridinium
-
pH 9.5, 37°C
0.385
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]-3,4-dimethylpyridinium
-
pH 6.0, 37°C
0.138
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]-3-methylpyridinium
-
pH 9.5, 37°C
0.14
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]-3-methylpyridinium
-
pH 6.0, 37°C
0.021
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]pyridinium
-
pH 6.0, 37°C
0.216
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]pyridinium
-
pH 9.5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kcat at pH 9.5, 37°C, relative to the reported kcat at pH 6.0, 37°C, with substrate 4-nitrophenyl alpha-D-N-acetylneurminide
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06
(1R/S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-(4-phenethyl-[1,2,3]triazol-1-yl)cyclohex-2-ene-1-carboxylic acid
-
pH 7.4, 37°C
0.019
(1R/S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-[4-(1-hydroxy-1-methylethyl)[1,2,3]triazol-1-yl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.4, 37°C
0.000021
(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
-
-
0.0000198
(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
-
-
0.0000173
(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
-
-
0.0000013
(2R,4S,5R)-5-[(1R,2S)-1-(acetylamino)-2-hydroxy-2-methylpentyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
0.00000021
(2R,4S,5R)-5-[(1R,2S)-1-(acetylamino)-2-methoxy-2-methylpentyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
0.000025
(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
-
-
0.0000115
(2R,4S,5R)-5-[(1S,2S)-1-(acetylamino)-2-hydroxybutyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
0.00001
(2R,4S,5R)-5-[(2S)-1-(acetylamino)-2-hydroxypent-4-en-1-yl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
0.0000053
(2R,4S,5R)-5-[(2S)-1-(acetylamino)-2-hydroxypentyl]-4-[(1Z)-prop-1-en-1-yl]pyrrolidine-2-carboxylic acid
-
-
0.0000015
(3S,4R,5R)-4-acetamido-3-amino-5-(1-ethylpropoxy)cyclohex-1-ene-1-carboxylic acid
-
pH 7.4, 37°C
0.0058
(3S,4R,5R)-4-acetamido-3-[4-((17alpha)-estra-1,3,5(10)-triene-3,17-dihydroxy-17-yl)[1,2,3]triazol-1-yl]-5-(1-ethylpropoxy)cyclohex-1-ene-1-carboxylic acid
-
pH 7.4, 37°C
0.000072
(3S,4R,5R)-4-acetamido-5-(1-ethyl-propoxy)-3-[4-(1-hydroxypropyl)[1,2,3]triazol-1-yl]cyclohex-1-ene-1-carboxylic acid
-
pH 7.4, 37°C
0.0012
(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-(4-phenethyl-[1,2,3]triazol-1-yl)cyclohex-1-ene-1-carboxylic acid
-
pH 7.4, 37°C
0.00000046
(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-guanidinocyclohex-1-ene-1-carboxylic acid
-
pH 7.4, 37°C
0.00013
(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-[4-(1-hydroxy-1-methylethyl)[1,2,3]triazol-1-yl]cyclohex-1-ene-1-carboxylic acid
-
pH 7.4, 37°C
0.0048
(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-[4-(1-hydroxycyclohexyl)[1,2,3]triazol-1-yl]cyclohex-1-ene-1-carboxylic acid
-
pH 7.4, 37°C
0.011
(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-[4-(1-hydroxycyclopentyl)[1,2,3]triazol-1-yl]cyclohex-1-ene-1-carboxylic acid
-
pH 7.4, 37°C
0.00046
(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-[4-(3-hydroxypropyl)[1,2,3]triazol-1-yl]cyclohex-1-ene-1-carboxylic acid
-
pH 7.4, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0181
(4R)-2-(2-carboxyphenyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.0107
(4R)-2-(2-carboxyphenyl)-3-(chloroacetyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00192
(4R)-2-(2-carboxyphenyl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00028
(4R)-2-(2-carboxyphenyl)-3-glycyl-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.0123
(4R)-2-(2-hydroxy-3-methoxyphenyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00162
(4R)-2-(2-hydroxy-3-methoxyphenyl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.0202
(4R)-2-(2-hydroxyphenyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00065
(4R)-2-(2-hydroxyphenyl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.0225
(4R)-2-(2-nitrophenyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00187
(4R)-2-(2-nitrophenyl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.0234
(4R)-2-(4-cyanophenyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00247
(4R)-2-(4-cyanophenyl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00081
(4R)-2-(4-cyanophenyl)-3-glycyl-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.0431
(4R)-2-(furan-2-yl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00289
(4R)-2-(furan-2-yl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00098
(4R)-2-(furan-2-yl)-3-glycyl-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.0213
(4R)-2-phenyl-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00121
(4R)-2-phenyl-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00792
(4R)-3-(chloroacetyl)-2-(2-hydroxy-3-methoxyphenyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00584
(4R)-3-(chloroacetyl)-2-(2-hydroxyphenyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00765
(4R)-3-(chloroacetyl)-2-(2-nitrophenyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00864
(4R)-3-(chloroacetyl)-2-(4-cyanophenyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.0129
(4R)-3-(chloroacetyl)-2-(furan-2-yl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00753
(4R)-3-(chloroacetyl)-2-phenyl-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00014
(4R)-3-glycyl-2-(2-hydroxy-3-methoxyphenyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00021
(4R)-3-glycyl-2-(2-hydroxyphenyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00102
(4R)-3-glycyl-2-(2-nitrophenyl)-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.00053
(4R)-3-glycyl-2-phenyl-1,3-thiazolidine-4-carboxylic acid
influenza A virus
-
pH and temperature not specified in the publication
0.0000223 - 0.0000256
2-((E)-4'-hydroxyphenylidene)-4,6-dihydroxy-2,3-dihydrobenzofuran-3-one
0.000032
4-(acetylamino)-3,5-bis(guanidino)-2-ethoxybenzoic acid
influenza A virus
-
pH 3.5, 37°C
0.000041
4-(acetylamino)-5-(guanidino)-2-(cyclopentyloxy)benzoic acid
influenza A virus
-
pH 3.5, 37°C
0.000049
4-(acetylamino)-5-(guanidino)-2-isopropoxybenzoic acid
influenza A virus
-
pH 3.5, 37°C
0.000036
methyl 4-(acetylamino)-3,5-bis(guanidino)-2-ethoxybenzoate
influenza A virus
-
pH 3.5, 37°C
0.000038
methyl 4-(acetylamino)-5-amino-2-(3-methylbutoxy)benzoate
influenza A virus
-
pH 3.5, 37°C
0.0000223
2-((E)-4'-hydroxyphenylidene)-4,6-dihydroxy-2,3-dihydrobenzofuran-3-one
influenza A virus
-
pH 6.5, 37°C
0.0000256
2-((E)-4'-hydroxyphenylidene)-4,6-dihydroxy-2,3-dihydrobenzofuran-3-one
influenza A virus
-
pH 6.5, 37°C
0.000022
2-((E)-4'-hydroxyphenylidene)-6-hydroxy-2,3-dihydrobenzofuran-3-one
influenza A virus
-
pH 6.5, 37°C
0.0000221
2-((E)-4'-hydroxyphenylidene)-6-hydroxy-2,3-dihydrobenzofuran-3-one
influenza A virus
-
pH 6.5, 37°C
0.0000003
oseltamivir carboxylate
influenza A virus
mutant enzyme R292K, pH and temperature not specified in the publication
0.0000007
oseltamivir carboxylate
influenza A virus
wild type enzyme, pH and temperature not specified in the publication
0.0000007
oseltamivir carboxylate
influenza A virus
mutant enzyme E119G, pH and temperature not specified in the publication
0.0000022
oseltamivir carboxylate
influenza A virus
wild type enzyme, pH and temperature not specified in the publication
0.0000029
oseltamivir carboxylate
influenza A virus
mutant enzyme D198N, pH and temperature not specified in the publication
0.0000054
oseltamivir carboxylate
influenza A virus
mutant enzyme E119A, pH and temperature not specified in the publication
0.0000125
oseltamivir carboxylate
influenza A virus
mutant enzyme ER152K, pH and temperature not specified in the publication
0.0000136
oseltamivir carboxylate
influenza A virus
mutant enzyme E119G, pH and temperature not specified in the publication
0.000016
oseltamivir carboxylate
influenza A virus
mutant enzyme E119D, pH and temperature not specified in the publication
0.00002
oseltamivir carboxylate
influenza A virus
-
pH and temperature not specified in the publication
0.0000218
oseltamivir carboxylate
influenza A virus
mutant enzyme E119A, pH and temperature not specified in the publication
0.0000231
oseltamivir carboxylate
influenza A virus
mutant enzyme R292K, pH and temperature not specified in the publication
0.0000244
oseltamivir carboxylate
influenza A virus
mutant enzyme N294S, pH and temperature not specified in the publication
0.0000445
oseltamivir carboxylate
influenza A virus
mutant enzyme N294S, pH and temperature not specified in the publication
0.0000975
oseltamivir carboxylate
influenza A virus
mutant enzyme H274Y, pH and temperature not specified in the publication
0.0001572
oseltamivir carboxylate
influenza A virus
mutant enzyme E119G/H274Y, pH and temperature not specified in the publication
0.0001916
oseltamivir carboxylate
influenza A virus
mutant enzyme E119D, pH and temperature not specified in the publication
0.0003514
oseltamivir carboxylate
influenza A virus
mutant enzyme E119D/H274Y, pH and temperature not specified in the publication
0.00059
oseltamivir carboxylate
influenza A virus
mutant enzyme D198N/H274Y, pH and temperature not specified in the publication
0.000792
oseltamivir carboxylate
influenza A virus
mutant enzyme H274Y, pH and temperature not specified in the publication
0.00082
oseltamivir carboxylate
influenza A virus
mutant enzyme E119A/H274Y, pH and temperature not specified in the publication
0.001762
oseltamivir carboxylate
influenza A virus
mutant enzyme E119G/H274Y, pH and temperature not specified in the publication
0.002682
oseltamivir carboxylate
influenza A virus
mutant enzyme E119D/H274Y, pH and temperature not specified in the publication
0.003367
oseltamivir carboxylate
influenza A virus
mutant enzyme E119A/H274Y, pH and temperature not specified in the publication
0.0000003
peramivir
influenza A virus
wild type enzyme, pH and temperature not specified in the publication
0.0000006
peramivir
influenza A virus
mutant enzyme R292K, pH and temperature not specified in the publication
0.0000007
peramivir
influenza A virus
mutant enzyme N294S, pH and temperature not specified in the publication
0.0000009
peramivir
influenza A virus
mutant enzyme D198N, pH and temperature not specified in the publication
0.0000011
peramivir
influenza A virus
mutant enzyme R152K, pH and temperature not specified in the publication
0.0000013
peramivir
influenza A virus
wild type enzyme, pH and temperature not specified in the publication
0.0000014
peramivir
influenza A virus
mutant enzyme N294S, pH and temperature not specified in the publication
0.0000021
peramivir
influenza A virus
mutant enzyme E119A, pH and temperature not specified in the publication
0.0000022
peramivir
influenza A virus
mutant enzyme R292K, pH and temperature not specified in the publication
0.0000095
peramivir
influenza A virus
mutant enzyme E119A, pH and temperature not specified in the publication
0.0000152
peramivir
influenza A virus
mutant enzyme H274Y, pH and temperature not specified in the publication
0.0000245
peramivir
influenza A virus
mutant enzyme E119G, pH and temperature not specified in the publication
0.0000304
peramivir
influenza A virus
mutant enzyme H274Y, pH and temperature not specified in the publication
0.000031
peramivir
influenza A virus
mutant enzyme E119D, pH and temperature not specified in the publication
0.0000508
peramivir
influenza A virus
mutant enzyme D198N/H274Y, pH and temperature not specified in the publication
0.0001421
peramivir
influenza A virus
mutant enzyme E119G, pH and temperature not specified in the publication
0.001867
peramivir
influenza A virus
mutant enzyme E119D, pH and temperature not specified in the publication
0.002117
peramivir
influenza A virus
mutant enzyme E119D/H274Y, pH and temperature not specified in the publication
0.003492
peramivir
influenza A virus
mutant enzyme E119A/H274Y, pH and temperature not specified in the publication
0.004374
peramivir
influenza A virus
mutant enzyme E119A/H274Y, pH and temperature not specified in the publication
0.0000009
zanamivir
influenza A virus
wild type enzyme, pH and temperature not specified in the publication
0.0000011
zanamivir
influenza A virus
mutant enzyme R292K, pH and temperature not specified in the publication
0.0000014
zanamivir
influenza A virus
mutant enzyme H274Y, pH and temperature not specified in the publication
0.0000014
zanamivir
influenza A virus
mutant enzyme N294S, pH and temperature not specified in the publication
0.0000016
zanamivir
influenza A virus
mutant enzyme N294S, pH and temperature not specified in the publication
0.0000019
zanamivir
influenza A virus
wild type enzyme, pH and temperature not specified in the publication
0.0000029
zanamivir
influenza A virus
mutant enzyme D198N/H274Y, pH and temperature not specified in the publication
0.0000031
zanamivir
influenza A virus
mutant enzyme R292K, pH and temperature not specified in the publication
0.0000037
zanamivir
influenza A virus
mutant enzyme D198N, pH and temperature not specified in the publication
0.000004
zanamivir
influenza A virus
mutant enzyme R152K, pH and temperature not specified in the publication
0.0000068
zanamivir
influenza A virus
mutant enzyme H274Y, pH and temperature not specified in the publication
0.00001019
zanamivir
influenza A virus
mutant enzyme E119G, pH and temperature not specified in the publication
0.0000499
zanamivir
influenza A virus
mutant enzyme E119A/H274Y, pH and temperature not specified in the publication
0.0000521
zanamivir
influenza A virus
mutant enzyme E119A, pH and temperature not specified in the publication
0.0000957
zanamivir
influenza A virus
mutant enzyme E119A/H274Y, pH and temperature not specified in the publication
0.0000959
zanamivir
influenza A virus
mutant enzyme E119A, pH and temperature not specified in the publication
0.0001221
zanamivir
influenza A virus
mutant enzyme E119D/H274Y, pH and temperature not specified in the publication
0.0001233
zanamivir
influenza A virus
mutant enzyme E119D/H274Y, pH and temperature not specified in the publication
0.0001447
zanamivir
influenza A virus
mutant enzyme E119G/H274Y, pH and temperature not specified in the publication
0.0002019
zanamivir
influenza A virus
mutant enzyme E119G/H274Y, pH and temperature not specified in the publication
0.0002511
zanamivir
influenza A virus
mutant enzyme E119D, pH and temperature not specified in the publication
0.000525
zanamivir
influenza A virus
mutant enzyme E119D, pH and temperature not specified in the publication
0.0008329
zanamivir
influenza A virus
mutant enzyme E119G, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11.58
-
purified enzyme, substrate 2-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid
additional information
-
activity of different strains in presence or absence of divalent cations, overview
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
additional information
low-glycosylation in och1-defective Pichia pastoris enhances the immunogenicity of recombinant neuraminidase and elicits similar antibody titers with less antigen when compared with hyper- and non-glycosylated neuraminidases after vaccination of mice
malfunction
-
neuraminidase insertion mutant virus shows increased particles formation, in pseudotyped particles system, activity compared to the wild-type virus. Compared with the wild-type AH N1, from A/California/05/2009/H1N1, the wild-type 09N1 exhibits higher neuraminidase activity and releases more pseudoparticles. Deletion/insertion of the 09s60 segment does not alter this relationship. The infectivity of pseudoparticles harboring neuraminidase in combination with the hemagglutinin from HPAI H5N1 (AH H5) is decreased by insertion of 09s60 into AH N1 and is increased by deletion of 09s60 from 09N1, the mutation also alters the oligomeric structure, overview
malfunction
-
neuraminidase insertion mutant virus shows increased particles formation, in pseudotyped particles system, activity compared to the wild-type virus. Compared with the wild-type AH N1, the wild-type 09N1 exhibits higher neuraminidase activity and releases more pseudoparticles. Deletion/insertion of the 09s60 segment does not alter this relationship. The infectivity of pseudoparticles harboring neuraminidase in combination with the hemagglutinin from HPAI H5N1 (AH H5, from A/Hong Kong/156/97/H5N1) is decreased by insertion of 09s60 into AH N1 and is increased by deletion of 09s60 from 09N1, the mutation also alters the oligomeric structure, overview
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
x * 59000-97000, hyperglycosylated recombinant enzyme, SDS-PAGE, x * 66000, low-glycosylated recombinant enzyme, SDS-PAGE, x * 45000, non-glycosylated recombinant enzyme, SDS-PAGE
55000
66000
x * 59000-97000, hyperglycosylated recombinant enzyme, SDS-PAGE, x * 66000, low-glycosylated recombinant enzyme, SDS-PAGE, x * 45000, non-glycosylated recombinant enzyme, SDS-PAGE
55000
plus dimer and monomer, only the tetramer is enzymatically active. 4 * 55000, SDS-PAGE. Molecular mass is slightly higher than that of monomer and dimer, and only tetramer is resistant to trypsin digestion
55000
plus dimer and tetramer, only the tetramer is enzymatically active. Monomer and dimer cannot be oligomerized to the tetramer. 1 * 55000, SDS-PAGE
55000
plus monomer and tetramer, only the tetramer is enzymatically active. Monomer and dimer cannot be oligomerized to the tetramer. 2 * 55000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 59000-97000, hyperglycosylated recombinant enzyme, SDS-PAGE, x * 66000, low-glycosylated recombinant enzyme, SDS-PAGE, x * 45000, non-glycosylated recombinant enzyme, SDS-PAGE
dimer
plus monomer and tetramer, only the tetramer is enzymatically active. Monomer and dimer cannot be oligomerized to the tetramer. 2 * 55000, SDS-PAGE
monomer
plus dimer and tetramer, only the tetramer is enzymatically active. Monomer and dimer cannot be oligomerized to the tetramer. 1 * 55000, SDS-PAGE
oligomer
-
the wild-type neuraminidase from this virus occurs primarily as a 120 kDa dimer but also as a tetramer and, in lesser amounts, as a 60 kDa monomer. The molecular masses of AH N1 and AH N1+09s60 expressed in pseudoparticle-infected 293T cells are 50 kDa and 60 kDa, respectively
tetramer
plus dimer and monomer, only the tetramer is enzymatically active. 4 * 55000, SDS-PAGE. Molecular mass is slightly higher than that of monomer and dimer, and only tetramer is resistant to trypsin digestion
additional information
-
enzyme possesses 2 distinct regions, a globular one, exposed to the exterior, and a stem portion, part of which is inserted into the virion envelope
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
deglycosylation of monomer, dimer or tetramer with PNGase F results in molecular masses of 48000 Da. Glycosylation of tetramer is different from monomer and dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q136K
the neuraminidase mutation has no effect on oseltamivir susceptibility but causes approximately a 300fold and a 70fold reduction in zanamivir and peramivir susceptibility, respectively. The mutant strain displays greater viral fitness than the wild-type virus in MDCK cells but equivalent infectivity and transmissibility in a ferret model
D198N
D198N/H274Y
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
E119A/H274Y
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
E119D
E119D/H274Y
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
E119G/H274Y
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
E245G
-
neuraminidase activity is 73% of wild-type value. IC50 for zanamivir is 2.9fold higher than wild-type value. IC50 for oseltamivir is 2.3fold higher than wild-type value
H274Y
I222L
-
neuraminidase activity is 82% of wild-type value. IC50 for zanamivir is 5.1fold higher than wild-type value. IC50 for oseltamivir is 18fold higher than wild-type value
N146K/A272V/Del245-248
-
revertant constructed from mutant N146K/S219T/A272V/Del245-248 for analysis of resistance to oseltamivir
N146K/S219T/A272V
-
revertant constructed from mutant N146K/S219T/A272V/Del245-248 for analysis of resistance to oseltamivir
N146K/S219T/A272V/Del245-248
-
mutant isolated from an oseltamivir-resistant virus from an immunocompromised child. The deletion is the sole change responsible for resistance
N146K/S219T/Del245-248
-
revertant constructed from mutant N146K/S219T/A272V/Del245-248 for analysis of resistance to oseltamivir
N294D
-
neuraminidase activity is 74% of wild-type value. IC50 for zanamivir is 2.4fold higher than wild-type value. IC50 for oseltamivir is 2.3fold higher than wild-type value
N294S
the mutation confers reduced inhibition to oseltamivir (63.6fold increase in IC50 compared to the wild type)
R152K
the mutant exhibits reduced inhibition to oseltamivir (17.9fold in IC50 values) but shows wild type inhibition to zanamivir and peramivir
R292K
the mutant exhibits reduced inhibition to oseltamivir (33fold in IC50 values) but shows wild type inhibition to zanamivir and peramivir
S219T/A272V/Del245-248
-
revertant constructed from mutant N146K/S219T/A272V/Del245-248 for analysis of resistance to oseltamivir
additional information
D198N
-
neuraminidase activity is 10% of wild-type value. IC50 for zanamivir is 5fold higher than wild-type value. IC50 for oseltamivir is 5.5fold higher than wild-type value
D198N
the mutation moderately affects the susceptibility to neuraminidase inhibitors
E119D
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
H274Y
-
neuraminidase activity is 104% of wild-type value. IC50 for zanamivir is 3.2fold higher than wild-type value. IC50 for oseltamivir is 9.4fold higher than wild-type value
H274Y
-
mutant resistant to oseltamivir, used for design of multi-binding-site inhibitors
H274Y
the mutation confers highly reduced inhibition to oseltamivir (1131.4fold increase in IC50 values compared to the wild type) and reduced inhibition to peramivir by 50.6fold
additional information
-
study on the effects of single-point amino acid substitutions on the structure and function of neuraminidase proteins. The rate of tolerant random one amino acid substitutions is 47%. Rates of tolerant substitutions for the stalk and for the surface and inner portion are 79%, 54%, and 19%, respectively. The ratio of mutations with which the enzyme loses neuraminidase activity, but is transported to the cell surface, decreases in proportion to the distance from the structural center of enzyme active site
additional information
-
construction of insertion mutant enzyme by deleting the 20-aa segment, residues 49-68, from the stalk region of 2009H1N1 neuraminidase, and inserting this segment, designated 09s60, into the stalk region of H5N1 neuraminidase
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 25
0 - 25
-
the enzyme is stable at 4 and 25°C for 24 h. At 37°C, the activity is retained for at least 7 h in the monovalent bulks, but by 24 h it has about 50% of its original activity. Three freeze-thaw cycles lead to a loss of about 70% of enzyme activity
0 - 25
-
the enzyme is stable at 4 and 25°C for 24 h. At 37°C, the activity is retained for at least 7 h in the monovalent bulks, but by 24 h it has about 75% of its original activity. Three freeze-thaw cycles lead to a loss of about 20% of enzyme activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
incubation with 0.1% (w/v) RapiGest results in almost complete loss of enzyme activity
-
incubation with 0.1% (w/v) RapiGest results in approximately 80% loss of enzyme activity
-
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
from inoculated chicken egg allantoic fluid, by ultracentrifugation, gel filtration and proteolytic treatment with pronase, soluble 'head' part of the enzyme complex
-
recombinant enzyme from insect cells by density gradient centrifugation and gel filtration
-
recombinant His-tagged viral neuraminidase by nickel affinity chromatography, desalting gel filtration, and cation exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged viral neuraminidase in wild-type Pichia pastoris strain GS115, an alpha-1,6-mannosyltransferase (och1)-defective Pichia pastoris mutant strain, and in Escherichia coli, resulting in a hyper-glycosylated, a low-glycosylated, and a non-glycosylated enzyme, respectively
expression of recombinant enzyme in Trichoplusia ni insect cells via baculoirus infection, subcloning in Escherichia coli DH5alpha
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
virtual screening method for inhibitors based on consensus scoring and ligand efficiency indices, which allows the combination of pharmacodynamic and pharmacokinetic properties into unique measures
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
de Barros, J.F., Jr.; Sales Alviano, D.; da Silva, M.H.; Dutra Wigg, M.; Sales Alviano, C.; Schauer, R.; dos Santos Silva Couceiro, J.N.
Characterization of sialidase from an influenza A (H3N2) virus strain: kinetic parameters and substrate specificity
Intervirology
46
199-206
2003
influenza A virus
Chou, D.T.H.; Watson, J.N.; Scholte, A.A.; Borgford, T.J.; Bennet, A.J.
Effect of neutral pyridine leaving groups on the mechanisms of influenza type A viral sialidase-catalyzed and spontaneous hydrolysis reactions of alpha-D-N-acetylneuraminides
J. Am. Chem. Soc.
122
8357-8364
2000
influenza A virus
-
Johansson, B.E.; Brett, I.C.
Variation in the divalent cation requirements of influenza A virus N2 neuraminidases
J. Biochem.
134
345-352
2003
influenza A 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
Tecle, T.; White, M.R.; Crouch, E.C.; Hartshorn, K.L.
Inhibition of influenza viral neuraminidase activity by collectins
Arch. Virol.
152
1731-1742
2007
influenza A virus
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
Richard, M.; Deleage, C.; Barthelemy, M.; Lin, Y.P.; Hay, A.; Lina, B.; Ferraris, O.
Impact of influenza A virus neuraminidase mutations on the stability, activity, and sensibility of the neuraminidase to neuraminidase inhibitors
J. Clin. Virol.
41
20-24
2008
influenza A virus
Wu, Z.L.; Ethen, C.; Hickey, G.E.; Jiang, W.
Active 1918 pandemic flu viral neuraminidase has distinct N-glycan profile and is resistant to trypsin digestion
Biochem. Biophys. Res. Commun.
379
749-753
2009
influenza A virus (Q9IGQ6), influenza A virus A/South Carolina/1/1918 H1N1 (Q9IGQ6)
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
Zhang, J.; Wang, Q.; Fang, H.; Xu, W.; Liu, A.; Du, G.
Design, synthesis, inhibitory activity, and SAR studies of hydrophobic p-aminosalicylic acid derivatives as neuraminidase inhibitors
Bioorg. Med. Chem.
16
3839-3847
2008
influenza A virus
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
Mitrasinovic, P.M.
On the structure-based design of novel inhibitors of H5N1 influenza A virus neuraminidase (NA)
Biophys. Chem.
140
35-38
2009
influenza A virus
Garcia-Sosa, A.T.; Sild, S.; Maran, U.
Design of multi-binding-site inhibitors, ligand efficiency, and consensus screening of avian influenza H5N1 wild-type neuraminidase and of the oseltamivir-resistant H274Y variant
J. Chem. Inf. Model.
48
2074-2080
2008
influenza A virus
Abed, Y.; Baz, M.; Boivin, G.
A novel neuraminidase deletion mutation conferring resistance to oseltamivir in clinical influenza A/H3N2 virus
J. Infect. Dis.
199
180-183
2009
influenza A virus
Yano, T.; Nobusawa, E.; Nagy, A.; Nakajima, S.; Nakajima, K.
Effects of single-point amino acid substitutions on the structure and function neuraminidase proteins in influenza A virus
Microbiol. Immunol.
52
216-223
2008
influenza A virus, influenza A virus A/tokyo/3/67
DUrsi, P.; Chiappori, F.; Merelli, I.; Cozzi, P.; Rovida, E.; Milanesi, L.
Virtual screening pipeline and ligand modelling for H5N1 neuraminidase
Biochem. Biophys. Res. Commun.
383
445-449
2009
influenza A virus, influenza A virus N1
Mercader, A.G.; Pomilio, A.B.
QSAR study of flavonoids and biflavonoids as influenza H1N1 virus neuraminidase inhibitors
Eur. J. Med. Chem.
45
1724-1730
2010
influenza A virus
Sung, J.C.; Van Wynsberghe, A.W.; Amaro, R.E.; Li, W.W.; McCammon, J.A.
Role of secondary sialic acid binding sites in influenza N1 neuraminidase
J. Am. Chem. Soc.
132
2883-2885
2010
influenza A virus (P06820)
Hurt, A.C.; Holien, J.K.; Parker, M.; Kelso, A.; Barr, I.G.
Zanamivir-resistant influenza viruses with a novel neuraminidase mutation
J. Virol.
83
10366-10373
2009
influenza A virus (Q07599)
Cui, Y.; Jiao, Z.; Gong, J.; Yu, Q.; Zheng, X.; Quan, J.; Luo, M.; Yang, Z.
Development of new stereodiverse diaminocyclitols as inhibitors of influenza virus neuraminidase
Org. Lett.
12
4-7
2010
influenza A virus
Liu, Y.; Jing, F.; Xu, Y.; Xie, Y.; Shi, F.; Fang, H.; Li, M.; Xu, W.
Design, synthesis and biological activity of thiazolidine-4-carboxylic acid derivatives as novel influenza neuraminidase inhibitors
Bioorg. Med. Chem.
19
2342-2348
2011
influenza A virus
Mohan, S.; McAtamney, S.; Haselhorst, T.; von Itzstein, M.; Pinto, B.M.
Carbocycles related to oseltamivir as influenza virus group-1-specific neuraminidase inhibitors. Binding to N1 enzymes in the context of virus-like particles
J. Med. Chem.
53
7377-7391
2010
influenza A virus
Raab, M.; Tvaroska, I.
The binding properties of the H5N1 influenza virus neuraminidase as inferred from molecular modeling
J. Mol. Model.
17
1445-1456
2011
influenza A virus
Yang, Y.; Chang, S.; Gong, X.; Wu, J.; Liu, B.
Expression, purification and characterization of low-glycosylation influenza neuraminidase in alpha-1,6-mannosyltransferase defective Pichia pastoris
Mol. Biol. Rep.
39
857-864
2011
influenza A virus (Q7TG96), influenza A virus newCaledonia/20/99(H1N1) (Q7TG96)
Wu, J.; Zhang, F.; Wang, M.; Xu, C.; Song, J.; Zhou, J.; Lin, X.; Zhang, Y.; Wu, X.; Tan, W.; Lu, J.; Zhao, H.; Gao, J.; Zhao, P.; Lu, J.; Wang, Y.
Characterization of neuraminidases from the highly pathogenic avian H5N1 and 2009 pandemic H1N1 influenza A viruses
PLoS ONE
5
e15825
2010
influenza A virus, influenza A virus A/Hong Kong/156/97/H5N1, influenza A virus A/California/05/2009/H1N1
Li, Y.; Cao, H.; Dao, N.; Luo, Z.; Yu, H.; Chen, Y.; Xing, Z.; Baumgarth, N.; Cardona, C.; Chen, X.
High-throughput neuraminidase substrate specificity study of human and avian influenza A viruses
Virology
415
12-19
2011
influenza A virus
Naumov, P.; Yasuda, N.; Rabeh, W.M.; Bernstein, J.
The elusive crystal structure of the neuraminidase inhibitor Tamiflu (oseltamivir phosphate): molecular details of action
Chem. Commun. (Camb. )
49
1948-1950
2013
influenza A virus (Q6DPL2)
von Grafenstein, S.; Wallnoefer, H.G.; Kirchmair, J.; Fuchs, J.E.; Huber, R.G.; Schmidtke, M.; Sauerbrei, A.; Rollinger, J.M.; Liedl, K.R.
Interface dynamics explain assembly dependency of influenza neuraminidase catalytic activity
J. Biomol. Struct. Dyn.
33
104-120
2015
influenza A virus
Halbherr, S.J.; Ludersdorfer, T.H.; Ricklin, M.; Locher, S.; Berger Rentsch, M.; Summerfield, A.; Zimmer, G.
Biological and protective properties of immune sera directed to influenza virus neuraminidase
J. Virol.
89
1550-1563
2015
influenza A virus, influenza A virus H7N7
Baek, Y.H.; Song, M.S.; Lee, E.Y.; Kim, Y.I.; Kim, E.H.; Park, S.J.; Park, K.J.; Kwon, H.I.; Pascua, P.N.; Lim, G.J.; Kim, S.; Yoon, S.W.; Kim, M.H.; Webby, R.J.; Choi, Y.K.
Profiling and characterization of potentially multidrug-resistant influenza neuraminidase 1 (N1) strains against neuraminidase inhibitors
J. Virol.
89
287-299
2015
influenza A virus (A9YLL2), influenza A virus (C3W5S3)
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
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 B virus, influenza A virus H3N2
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Transporter Classification Database (TCDB): 1.A.32.1.3
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