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Information on EC 3.2.1.18 - exo-alpha-sialidase and Organism(s) Influenza A virus and UniProt Accession P06820

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EC Tree
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 A virus
UNIPROT: P06820
Word Map
The taxonomic range for the selected organisms is: Influenza A 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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alpha-sialidase
276462
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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-acylneuraminate glycohydrolase
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NANase
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neuraminidase
neuraminidase 1
302477, 302478
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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
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
reaction and kinetic mechanisms
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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
2'-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + N-acetylneuraminic acid
show the reaction diagram
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?
2-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferol + alpha-D-N-acetylneuraminic acid
show the reaction diagram
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?
2-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + alpha-D-N-acetylneuraminic acid
show the reaction diagram
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?
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
?
show the reaction diagram
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?
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferol + alpha-D-N-acetylneuraminic acid
show the reaction diagram
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?
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferone + N-acetylneuraminic acid
show the reaction diagram
alpha(2-3)-sialyllactose + H2O
sialic acid + lactose
show the reaction diagram
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preference for alpha(2-3)-linkages
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?
alpha(2-6)-sialyllactose + H2O
sialic acid + lactose
show the reaction diagram
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?
bovine brain gangliosides + H2O
sialic acid + ?
show the reaction diagram
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?
bovine submaxillary gland mucin + H2O
sialic acid + ?
show the reaction diagram
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?
Candida albicans cells + H2O
desialylated Candida albicans cells + sialic acid
show the reaction diagram
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?
colominic acid + H2O
sialic acid + ?
show the reaction diagram
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?
fetuin + H2O
?
show the reaction diagram
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?
fetuin + H2O
sialic acid + ?
show the reaction diagram
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?
Neu5Ac-alpha-(2->3)-Gal-beta-4-nitrophenol + H2O
Neu5Ac + 4-nitrophenyl beta-D-galactopyranoside
show the reaction diagram
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?
Neu5Ac-alpha-(2->6)-Gal-beta-4-nitrophenol + H2O
Neu5Ac + 4-nitrophenyl beta-D-galactopyranoside
show the reaction diagram
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?
Neu5Acalpha(2->3)LacNAcbeta-4-aminophenyl + H2O
?
show the reaction diagram
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best substrate
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?
Neu5Acalpha(2->6)LacNAcbeta-4-aminophenyl + H2O
?
show the reaction diagram
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?
Neu5AcF-alpha-(2->3)-Gal-beta-4-nitrophenol + H2O
Neu5AcF + 4-nitrophenyl beta-D-galactopyranoside
show the reaction diagram
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?
Neu5glycolyl-alpha-(2->3)-Gal-beta-4-nitrophenol + H2O
N-glycolylneuraminic acid + 4-nitrophenyl beta-D-galactopyranoside
show the reaction diagram
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?
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]-3,4-dimethylpyridinium + H2O
sialic acid + 3,4-dimethylpyridine
show the reaction diagram
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?
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]-3-methylpyridinium + H2O
sialic acid + 3-methylpyridine
show the reaction diagram
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?
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]-4-methylpyridinium + H2O
sialic acid + 4-methylpyridine
show the reaction diagram
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?
N[(5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosyl)onate]pyridinium + H2O
sialic acid + pyridine
show the reaction diagram
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?
orosomucoid + 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
bovine brain gangliosides + H2O
sialic acid + ?
show the reaction diagram
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?
bovine submaxillary gland mucin + H2O
sialic acid + ?
show the reaction diagram
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?
colominic acid + H2O
sialic acid + ?
show the reaction diagram
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?
fetuin + H2O
?
show the reaction diagram
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?
fetuin + H2O
sialic acid + ?
show the reaction diagram
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?
orosomucoid + H2O
sialic acid + ?
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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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+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
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(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
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(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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(3R,4R,5R)-4-acetamido-3-(1-(diaminomethylamino)-3-hydroxypropan-2-yloxy)-5-((1S)-1,2,3-trihydroxypropyl)cyclohex-1-enecarboxylic acid
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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
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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
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(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
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(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
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(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-(4-phenethyl-[1,2,3]triazol-1-yl)cyclohex-1-ene-1-carboxylic acid
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(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-guanidinocyclohex-1-ene-1-carboxylic acid
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(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
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(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-[4-(1-hydroxycyclohexyl)[1,2,3]triazol-1-yl]cyclohex-1-ene-1-carboxylic acid
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(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-[4-(1-hydroxycyclopentyl)[1,2,3]triazol-1-yl]cyclohex-1-ene-1-carboxylic acid
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(3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-[4-(3-hydroxypropyl)[1,2,3]triazol-1-yl]cyclohex-1-ene-1-carboxylic acid
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(4R)-2-(2-carboxyphenyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-(2-carboxyphenyl)-3-(chloroacetyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-(2-carboxyphenyl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-(2-carboxyphenyl)-3-glycyl-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-(2-hydroxy-3-methoxyphenyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-(2-hydroxy-3-methoxyphenyl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-(2-hydroxyphenyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-(2-hydroxyphenyl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-(2-nitrophenyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-(2-nitrophenyl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-(4-cyanophenyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-(4-cyanophenyl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-(4-cyanophenyl)-3-glycyl-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-(furan-2-yl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-(furan-2-yl)-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-(furan-2-yl)-3-glycyl-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-phenyl-1,3-thiazolidine-4-carboxylic acid
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(4R)-2-phenyl-3-(phenylacetyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-3-(chloroacetyl)-2-(2-hydroxy-3-methoxyphenyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-3-(chloroacetyl)-2-(2-hydroxyphenyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-3-(chloroacetyl)-2-(2-nitrophenyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-3-(chloroacetyl)-2-(4-cyanophenyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-3-(chloroacetyl)-2-(furan-2-yl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-3-(chloroacetyl)-2-phenyl-1,3-thiazolidine-4-carboxylic acid
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(4R)-3-glycyl-2-(2-hydroxy-3-methoxyphenyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-3-glycyl-2-(2-hydroxyphenyl)-1,3-thiazolidine-4-carboxylic acid
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(4R)-3-glycyl-2-(2-nitrophenyl)-1,3-thiazolidine-4-carboxylic acid
-
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(4R)-3-glycyl-2-phenyl-1,3-thiazolidine-4-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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2-(E-4'-hydroxyphenylidene)-4,6-dihydroxy-2,3-dihydrobenzo-furan-3-one
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2-(E-4'-hydroxyphenylidene)-6-hydroxy-2,3-dihydrobenzofuran-3-one
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2-(E-benzylidene)-6-hydroxy-2,3-dihydrobenzofuran-3-one
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2-deoxy-2,3-dehydro-N-acetylneuraminic acid
4-(acetylamino)-3,5-bis(guanidino)-2-ethoxybenzoic acid
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4-(acetylamino)-5-(guanidino)-2-(cyclopentyloxy)benzoic acid
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4-(acetylamino)-5-(guanidino)-2-butoxybenzoic acid
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4-(acetylamino)-5-(guanidino)-2-isopropoxybenzoic acid
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5,7,4'-trihydroxy-8-methoxyflavone
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7,4'-di-O-galloyltricetinflavan
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7-O-galloyltricetinflavan
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CID2601775
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the IUPAC name is 2-[(4-amino-5-cyclopropyl-1,2,4-triazol-3-yl)sulfanyl]-N-(cyclopentylcarbamoyl)acetamide
CID9796290
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the IUPAC name is 6-[2-[[2-[(2S)-2-cyanopyrrolidin-1-yl]-2-oxoethyl]amino]ethylamino]pyridine-3-carbonitrile
daidzein
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genistein
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ginkgetin
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hinokiflavone
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hinokiflavone-sialic acid
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hispidulin
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kaempferol
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kaempferol 3-O-beta-xylopyranosyl-(1->2)-beta-D-glucopyranoside
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L-Cysteine hydrochloride
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lung surfactant protein A
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lung surfactant protein D has greater neuraminidase inhibitory activity than mannose-binding lectin, which in turn has greater activity than lung surfactant protein A
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lung surfactant protein D
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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
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luteolin 7-O-beta-D-glucopyranoside
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mannose-binding lectin
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lung surfactant protein D has greater neuraminidase inhibitory activity than mannose-binding lectin, which in turn has greater activity than lung surfactant protein A
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methyl 4-(acetylamino)-3,5-bis(guanidino)-2-ethoxybenzoate
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methyl 4-(acetylamino)-3-amino-5-hydroxycyclopent-1-ene-1-carboxylate
-
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methyl 4-(acetylamino)-5-amino-2-(3-methylbutoxy)benzoate
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-
myricetin
-
-
oseltamivir
oseltamivir carboxylate
oseltamivir phosphate
i.e. Tamiflu
peramivir
quercetin
-
-
rhamnocitrin
-
i.e. 3,4',5-trihydroxy-7-methoxyflavone
scutellarein
-
-
sulfuretin
zanamivir
Zn2+
-
slight inhibition
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16
2-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid
-
pH 5.2
0.18
alpha-(2-3)-sialyllactose
-
pH 5.2
0.52
alpha-(2-6)-sialyllactose
-
pH 5.2
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
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
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
0.0000001
oseltamivir carboxylate
-
-
0.00000006
zanamivir
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
0.000022 - 0.0000221
2-((E)-4'-hydroxyphenylidene)-6-hydroxy-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
0.00004
4-(acetylamino)-5-(guanidino)-2-butoxybenzoic 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
0.0000289 - 0.0000316
apigenin
0.000026 - 0.0000463
dinatin
0.0000326 - 0.0000337
luteolin
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
0.0000000032 - 0.000021
oseltamivir
0.0000003 - 0.003367
oseltamivir carboxylate
0.0000003 - 0.004374
peramivir
0.0000277 - 0.0000296
sulfuretin
0.0000009 - 0.00502
zanamivir
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.15
-
purified enzyme, substrate alpha-(2-6)-sialyllactose
2.13
-
purified enzyme, substrate alpha-(2-3)-sialyllactose
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 hide
LITERATURE
4.4
-
with substrate alpha-(2-6)-sialyllactose
5
-
assay at
5.9
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
H1N1
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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; 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
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
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
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; plus dimer and tetramer, only the tetramer is enzymatically active. Monomer and dimer cannot be oligomerized to the tetramer. 1 * 55000, SDS-PAGE; plus monomer and tetramer, only the tetramer is enzymatically active. Monomer and dimer cannot be oligomerized to the tetramer. 2 * 55000, SDS-PAGE
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
200000 - 240000
-
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
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
homotetramer
-
-
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 hide
LITERATURE
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D198N
D198N/H274Y
A9YLL2, C3W5S3
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
D198N/R152K
A9YLL2, C3W5S3
inactive
D198N/R292K
A9YLL2, C3W5S3
inactive
E119A
A9YLL2, C3W5S3
the mutation confers reduced inhibition to zanamivir
E119A/D198N
A9YLL2, C3W5S3
inactive
E119A/H274Y
A9YLL2, C3W5S3
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
E119A/R152K
A9YLL2, C3W5S3
inactive
E119A/R292K
A9YLL2, C3W5S3
inactive
E119D
E119D/D198N
A9YLL2, C3W5S3
inactive
E119D/H274Y
A9YLL2, C3W5S3
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
E119D/R152K
A9YLL2, C3W5S3
inactive
E119D/R292K
A9YLL2, C3W5S3
inactive
E119G
A9YLL2, C3W5S3
the mutation confers reduced inhibition to zanamivir
E119G/D198N
A9YLL2, C3W5S3
inactive
E119G/H274Y
A9YLL2, C3W5S3
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
E119G/R152K
A9YLL2, C3W5S3
inactive
E119G/R292K
A9YLL2, C3W5S3
inactive
E227G
-
mutation results in an impairment of growth of the concerned virus
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
E277G
-
mutation results in an impairment of growth of the concerned virus
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
A9YLL2, C3W5S3
the mutation confers reduced inhibition to oseltamivir (63.6fold increase in IC50 compared to the wild type)
N294S/H274Y
A9YLL2, C3W5S3
inactive
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
R152K
A9YLL2, C3W5S3
the mutant exhibits reduced inhibition to oseltamivir (17.9fold in IC50 values) but shows wild type inhibition to zanamivir and peramivir
R152K/H274Y
A9YLL2, C3W5S3
inactive
R156K
-
neuraminidase activity is 71% of wild-type value
R292K
A9YLL2, C3W5S3
the mutant exhibits reduced inhibition to oseltamivir (33fold in IC50 values) but shows wild type inhibition to zanamivir and peramivir
R292K/H274Y
A9YLL2, C3W5S3
inactive
S179A
-
mutation results in an impairment of growth of the concerned virus
S219T/A272V/Del245-248
-
revertant constructed from mutant N146K/S219T/A272V/Del245-248 for analysis of resistance to oseltamivir
W178L
-
mutation results in an impairment of growth of the concerned virus
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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; 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
56
-
inactivation
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 hide
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
-
from several strains
-
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
recombinant protein
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in SF21 cells
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 hide
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
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
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
Manually annotated by BRENDA team
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, influenza A virus, Salmonella enterica subsp. enterica serovar Typhimurium, Vibrio cholerae
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
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
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
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
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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/California/05/2009/H1N1, influenza A virus A/Hong Kong/156/97/H5N1
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
influenza A virus, Paenarthrobacter ureafaciens, Streptococcus pneumoniae, Streptococcus pneumoniae IID553, Vibrio cholerae
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
Onsirisakul, N.; Nakakita, S.; Boonarkart, C.; Kongchanagul, A.; Suptawiwat, O.; Puthavathana, P.; Chaichuen, K.; Kittiniyom, K.; Suzuki, Y.; Auewarakul, P.
Substrate specificity of avian influenza H5N1 neuraminidase
World J. Virol.
3
30-36
2014
influenza A virus
Manually annotated by BRENDA team
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