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2-deoxy-2,3-didehydro-N-acetyl-9-O-acetylneuraminate + H2O
?
3'-O-acetylthymidine + H2O
thymidine + acetate
-
8% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
4-methylumbelliferyl butyrate + H2O
4-methylumbelliferone + butyrate
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
4-nitrophenylacetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-O-acetyl sialic acid + H2O
sialic acid + acetate
-
-
-
-
?
5-N-acetyl-4,9-di-O-acetylneuraminic acid alpha-methylglycoside + H2O
4,9-di-O-acetylneuraminic acid alpha-methylglycoside + acetate
sialate-9-O-acetylesterase activity
analysis by gas chromatography/mass spectrometry
-
?
5-N-acetyl-7(8),9-di-O-acetylneuraminic acid + H2O
?
-
-
-
?
5-N-acetyl-9-O-acetylneuraminic acid + H2O
5-N-acetylneuraminic acid + acetate
5-N-glycolyl-9-O-acetylneuraminic acid + H2O
5-N-glycolylneuraminic acid + acetate
-
-
-
?
9-O-acetyl sialic acid + H2O
sialic acid + acetate
9-O-acetyl-N-acetylneuraminic acid + H2O
N-acetylneuraminic acid + acetate
-
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
alacepril + H2O
deacetylalacepril + acetate
-
-
-
?
alpha-naphthyl acetate + H2O
1-naphthol + acetate
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
-
-
-
?
bovine submandibular gland mucin + H2O
?
bovine submaxillary mucin + H2O
?
-
-
-
-
?
CMP-O9-acetyl-N-acetylneuraminate + H2O
CMP-N-acetylneuraminate + acetate
-
SsNeuA is a bifunctional CMP-Neu5Ac synthetase/O-acetylesterase, which strictly de-O-acetylates CMP-O-acetyl-Neu5Ac
-
-
?
cytidine 5'-monophospho-N-acetylneuraminic acid + H2O
?
methyl 6-O-(N-acetyl-9-O-acetyl-alpha-D-neuramin-2-yl)-alpha-D-glucoside + H2O
methyl 6-O-(N-acetyl-alpha-D-neuramin-2-yl)-alpha-D-glucoside + acetate
-
methyl N-acetylneuraminide, 25°C, 60 min, pH 7
NMR-based enzyme assay
-
?
methyl 6-S-(N-acetyl-9-O-acetyl-alpha-D-neuramin-2-yl)-6-thio-alpha-D-glucoside + H2O
methyl 6-S-(N-acetyl-alpha-D-neuramin-2-yl)-alpha-D-glucoside + acetate
N-acetyl-4-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
N-acetyl-4-O-acetylneuraminic acid + H2O
N-acetylneuraminate + acetate
-
pH 8, 30 min, 37°C, catalysed only by esterase with pI 5.7
analyses by HPLC
-
?
N-acetyl-9-O-acetyl-neuraminic acid + H2O
N-acetylneuraminic acid + acetate
N-acetyl-9-O-acetyl-neuraminic acid alpha-methylglycoside + H2O
N-acetylneuraminic acid alpha-methylglycoside + acetate
methyl N-acetylneuraminide, 25°C, 60 min, pH 7
NMR-based enzyme assay
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
N-acetyl-9-O-acetylneuraminate beta-methylglycoside + H2O
N-acetylneuraminate beta-methylglycoside + acetate
-
70% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
N-acetyl-9-O-acetylneuraminate lactose + H2O
N-acetylneuraminate lactose + acetate
N-acetyl-9-O-acetylneuraminic acid + H2O
?
-
-
-
-
?
N-acetyl-9-O-acetylneuraminic acid + H2O
N-acetylneuraminate + acetate
-
pH 8, 30 min, 37°C, catalysed by esterase with pI 4.8 and esterase with pI 5.7
analyses by HPLC
-
?
N-acetyl-9-O-lactoylneuraminic acid + H2O
9-O-lactoylneuraminic acid + acetate
N-acetyl-O-5,9-diacetylneuraminate + H2O
N-acetylneuraminate + acetate
N-acetyl-O-9-acetylneuraminate + H2O
N-acetylneuraminate + acetate
N-acetyl-O-acetylneuraminate + H2O
?
-
-
-
-
?
N-acetyl-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
destroys receptors on the surface of the target cells
-
-
?
O-9-acetyl-GD3-S-phenyl + H2O
?
-
i.e. 9-O-acetyl-NeuAcalpha-2,8-NeuAcalpha-2,3-Galbeta-1,4-Glcbeta-S-phenyl
-
-
?
O-acetylserine + H2O
serine + acetate
-
less than 5% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
rat serum glycoprotein + H2O
?
-
90% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
spironolactone + H2O
?
-
-
-
?
thiophenyl acetate + H2O
thiophenol + acetate
triacetin + H2O
?
-
26% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
additional information
?
-
2-deoxy-2,3-didehydro-N-acetyl-9-O-acetylneuraminate + H2O
?
-
55% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
2-deoxy-2,3-didehydro-N-acetyl-9-O-acetylneuraminate + H2O
?
-
37% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
130% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
220% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
-
-
-
?
4-methylumbelliferyl butyrate + H2O
4-methylumbelliferone + butyrate
-
14% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
4-methylumbelliferyl butyrate + H2O
4-methylumbelliferone + butyrate
-
less than 5% of the activity compared to 4-methylumbelliferyl acetate at pH 5.5
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
680% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
3500% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
3500% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
72% of the activity compared to 4-methylumbelliferyl acetate at pH 5.5
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
5-N-acetyl-9-O-acetylneuraminic acid + H2O
5-N-acetylneuraminic acid + acetate
-
-
-
?
5-N-acetyl-9-O-acetylneuraminic acid + H2O
5-N-acetylneuraminic acid + acetate
-
-
-
-
?
5-N-acetyl-9-O-acetylneuraminic acid + H2O
5-N-acetylneuraminic acid + acetate
-
-
-
?
5-N-acetyl-9-O-acetylneuraminic acid + H2O
5-N-acetylneuraminic acid + acetate
-
-
-
?
5-N-acetyl-9-O-acetylneuraminic acid + H2O
5-N-acetylneuraminic acid + acetate
-
-
-
-
?
5-N-acetyl-9-O-acetylneuraminic acid + H2O
5-N-acetylneuraminic acid + acetate
-
-
-
-
?
5-N-acetyl-9-O-acetylneuraminic acid + H2O
5-N-acetylneuraminic acid + acetate
-
-
-
-
?
5-N-acetyl-9-O-acetylneuraminic acid + H2O
5-N-acetylneuraminic acid + acetate
-
-
-
-
?
5-N-acetyl-9-O-acetylneuraminic acid + H2O
5-N-acetylneuraminic acid + acetate
-
-
-
-
?
5-N-acetyl-9-O-acetylneuraminic acid + H2O
5-N-acetylneuraminic acid + acetate
-
-
-
?
5-N-acetyl-9-O-acetylneuraminic acid + H2O
5-N-acetylneuraminic acid + acetate
-
-
-
?
9-O-acetyl sialic acid + H2O
sialic acid + acetate
-
-
-
-
?
9-O-acetyl sialic acid + H2O
sialic acid + acetate
-
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
-
2% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
acetyl-CoA + H2O
CoA + acetate
-
-
-
?
alpha-naphthyl acetate + H2O
1-naphthol + acetate
-
643% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
alpha-naphthyl acetate + H2O
1-naphthol + acetate
-
2200% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
alpha-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
alpha-naphthyl acetate + H2O
1-naphthol + acetate
-
65% of the activity compared to 4-methylumbelliferyl acetate at pH 5.5
-
-
?
bovine submandibular gland mucin + H2O
?
-
no hydrolysis
-
-
?
bovine submandibular gland mucin + H2O
?
-
30% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
cytidine 5'-monophospho-N-acetylneuraminic acid + H2O
?
-
-
-
-
?
cytidine 5'-monophospho-N-acetylneuraminic acid + H2O
?
-
-
-
-
?
methyl 6-S-(N-acetyl-9-O-acetyl-alpha-D-neuramin-2-yl)-6-thio-alpha-D-glucoside + H2O
methyl 6-S-(N-acetyl-alpha-D-neuramin-2-yl)-alpha-D-glucoside + acetate
-
thio-linked N-acetylneuraminosylglucoside, 25°C, 60 min, pH 7
NMR-based enzyme assay
-
?
methyl 6-S-(N-acetyl-9-O-acetyl-alpha-D-neuramin-2-yl)-6-thio-alpha-D-glucoside + H2O
methyl 6-S-(N-acetyl-alpha-D-neuramin-2-yl)-alpha-D-glucoside + acetate
-
thio-linked N-acetylneuraminosylglucoside, 25°C, 60 min, pH 7
NMR-based enzyme assay
-
?
methyl 6-S-(N-acetyl-9-O-acetyl-alpha-D-neuramin-2-yl)-6-thio-alpha-D-glucoside + H2O
methyl 6-S-(N-acetyl-alpha-D-neuramin-2-yl)-alpha-D-glucoside + acetate
thio-linked N-acetylneuraminosylglucoside, 25°C, 60 min, pH 7
NMR-based enzyme assay
-
?
N-acetyl-4-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
60% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
N-acetyl-4-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
no hydrolysis at pI 4.8, same rate of hydrolysis at pI 5.7 compared to N-acetyl-9-O-acetylneuraminate
-
-
?
N-acetyl-4-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
3% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
N-acetyl-4-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
3% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
N-acetyl-9-O-acetyl-neuraminic acid + H2O
N-acetylneuraminic acid + acetate
-
25°C, 60 min, pH 7, slow activity due to alpha: beta anomeric ratio of about 5: 95
NMR-based enzyme assay
-
?
N-acetyl-9-O-acetyl-neuraminic acid + H2O
N-acetylneuraminic acid + acetate
25°C, 60 min, pH 7, slow activity due to alpha: beta anomeric ratio of about 5:95
NMR-based enzyme assay
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
at pI 4.8 and pI 5.7
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
-
?
N-acetyl-9-O-acetylneuraminate lactose + H2O
N-acetylneuraminate lactose + acetate
-
same rate of hydrolysis compared to N-acetyl-9-O-acetylneuraminate
-
-
?
N-acetyl-9-O-acetylneuraminate lactose + H2O
N-acetylneuraminate lactose + acetate
-
96% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
N-acetyl-9-O-acetylneuraminate lactose + H2O
N-acetylneuraminate lactose + acetate
-
96% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
N-acetyl-9-O-lactoylneuraminic acid + H2O
9-O-lactoylneuraminic acid + acetate
-
-
-
-
?
N-acetyl-9-O-lactoylneuraminic acid + H2O
9-O-lactoylneuraminic acid + acetate
-
-
-
-
?
N-acetyl-O-5,9-diacetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
?
N-acetyl-O-5,9-diacetylneuraminate + H2O
N-acetylneuraminate + acetate
-
-
-
?
N-acetyl-O-9-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
best substrate
-
-
?
N-acetyl-O-9-acetylneuraminate + H2O
N-acetylneuraminate + acetate
-
contribution of Ser19 and His301 to catalysis, active site structure, overview
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
Isavirus salaris
-
pH 8
-
-
?
sialic acid + H2O
?
-
-
-
?
sialic acid + H2O
?
-
-
-
?
thiophenyl acetate + H2O
thiophenol + acetate
-
305% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
thiophenyl acetate + H2O
thiophenol + acetate
-
12% of the activity compared to N-acetyl-9-O-acetylneuraminate
-
-
?
additional information
?
-
-
O-acetylated sialic acids
-
-
?
additional information
?
-
-
O-acetylated sialic acids
-
-
?
additional information
?
-
-
O-acetylated sialic acids
-
-
?
additional information
?
-
-
O-acetylated sialic acids
-
-
?
additional information
?
-
-
no hydrolysis with N-acetyl-4-O-lactoylneuraminate, N-acetyl-9-O-acetylneuraminate methyl ester
-
-
?
additional information
?
-
-
no hydrolysis with N-glycoloyl-9-O-lactoylneuraminate, bovine submandibular gland mucin, rat serum glycoprotein, rat erythrocytes
-
-
?
additional information
?
-
-
no hydrolysis with N-acetyl-7-O-acetylneuraminate, horse alpha1-acid glycoprotein, N-acetylneuraminate methyl ester
-
-
?
additional information
?
-
-
O-acetylated sialic acids
-
-
?
additional information
?
-
-
alpha-anomer specificity
-
-
?
additional information
?
-
purified enzyme destroys BCoV receptors on rat erythrocytes and Madin-Darby bovine kidney (MDBK) cells
-
-
?
additional information
?
-
-
specific for alpha-anomer of N-acetyl-9-O-acetyl-neuraminic acid, N-acetyl-9-O-acetyl-neuraminic acid beta-methylglycoside is no substrate (60 min, 25°C, pH 7)
-
-
?
additional information
?
-
-
substrate specificity towards aglycon moiety
-
-
?
additional information
?
-
-
the enzyme of Bovine coronavirus exhibits sialate-9-O-acetylesterase specificity
-
-
?
additional information
?
-
-
alpha-anomer specificity
-
-
?
additional information
?
-
-
specific for alpha-anomer of N-acetyl-9-O-acetyl-neuraminic acid, N-acetyl-9-O-acetyl-neuraminic acid beta-methylglycoside is no substrate (60 min, 25°C, pH 7)
-
-
?
additional information
?
-
-
substrate specificity towards aglycon moiety
-
-
?
additional information
?
-
-
O-acetylated sialic acids
-
-
?
additional information
?
-
-
no hydrolysis with N-acetyl-7-O-acetylneuraminate, horse alpha1-acid glycoprotein, N-acetylneuraminate methyl ester
-
-
?
additional information
?
-
-
O-acetylated sialic acids
-
-
?
additional information
?
-
-
alpha-naphthylacetate, 9-O-acetyl sialyllactose, serum alpha1 acid glycoprotein, and erythrocyte membranes containing N-acetyl-4-O-acetylneuraminic acid or N-acetyl-9-O-acetylneuraminic acid are susceptible to SOAE catalysed hydrolysis
-
-
?
additional information
?
-
-
glycosidically linked sialic acids are also substrate, hydrolysis of 20% under standard conditions
-
-
?
additional information
?
-
-
liberation of sialic acid from gland mucin (mainly containing N-acetyl-4-O-acetylneuraminic acid)
-
-
?
additional information
?
-
-
N-acetyl-4-O-acetylneuraminic acid is slightly preferred over N-acetyl-9-O-acetylneuraminic acid as substrate for esterase with pI 5.7
-
-
?
additional information
?
-
-
N-acetyl-7-O-acetylneuraminic acid is no substrate
-
-
?
additional information
?
-
-
O-acetylated sialic acids
-
-
?
additional information
?
-
-
NanS is also active on phenylacetate, butylacetate, triacetin, and slightly on rosmarinic acid and propylacetate, substrate specificity, overview. NanS shows negligible aryl esterase activity with alpha-naphthyl acetate and alpha-naphthyl propionate as substrates and no measurable lipolytic activity or thioesterase activity
-
-
?
additional information
?
-
-
specifically hydrolyses 9-O-acetylgroups on sialic acid
-
?
additional information
?
-
-
O-acetyl esters
-
-
?
additional information
?
-
sialic acid acetyl esterase removes acetyl moieties from the 9-OH position of sialic acid
-
-
?
additional information
?
-
-
sialic acid acetyl esterase removes acetyl moieties from the 9-OH position of sialic acid
-
-
?
additional information
?
-
-
no hydrolysis with N-acetyl-4-O-lactoylneuraminate, N-acetyl-9-O-acetylneuraminate methyl ester
-
-
?
additional information
?
-
-
no hydrolysis with acetyl-coenzyme A, acetylthiocholine iodide
-
-
?
additional information
?
-
-
no hydrolysis with N-acetyl-7-O-acetylneuraminate, horse alpha1-acid glycoprotein, N-acetylneuraminate methyl ester
-
-
?
additional information
?
-
-
O-acetylated sialic acids
-
-
?
additional information
?
-
-
incubation of the enzyme with chicken erythrocytes abolishes the agglutinability the erythrocytes
-
-
?
additional information
?
-
alpha-anomer specificity
-
-
?
additional information
?
-
-
alpha-anomer specificity
-
-
?
additional information
?
-
Ser57 is essential for substrate binding and orientation and catalytic activity, NMR-analyses and molecular modelling
-
-
?
additional information
?
-
-
Ser57 is essential for substrate binding and orientation and catalytic activity, NMR-analyses and molecular modelling
-
-
?
additional information
?
-
enzyme activity independent of chemical nature of aglycon moiety
-
-
?
additional information
?
-
-
enzyme activity independent of chemical nature of aglycon moiety
-
-
?
additional information
?
-
specific for alpha-anomer of N-acetyl-9-O-acetyl-neuraminic acid, N-acetyl-9-O-acetyl-neuraminic acid beta-methylglycoside is no substrate (60 min, 25°C, pH 7)
-
-
?
additional information
?
-
-
specific for alpha-anomer of N-acetyl-9-O-acetyl-neuraminic acid, N-acetyl-9-O-acetyl-neuraminic acid beta-methylglycoside is no substrate (60 min, 25°C, pH 7)
-
-
?
additional information
?
-
-
the enzyme of Influenza C virus exhibits sialate-9-O-acetylesterase specificity
-
-
?
additional information
?
-
alpha-anomer specificity
-
-
?
additional information
?
-
Ser57 is essential for substrate binding and orientation and catalytic activity, NMR-analyses and molecular modelling
-
-
?
additional information
?
-
enzyme activity independent of chemical nature of aglycon moiety
-
-
?
additional information
?
-
specific for alpha-anomer of N-acetyl-9-O-acetyl-neuraminic acid, N-acetyl-9-O-acetyl-neuraminic acid beta-methylglycoside is no substrate (60 min, 25°C, pH 7)
-
-
?
additional information
?
-
-
MHV Sia receptor-binding specificity corresponds to the sialate-O-acetylesterase substrate preference of hemagglutinin-esterase , and hemagglutinin-esterase is sufficient to mediate virion binding to natural sialoglycoconjugates
-
-
?
additional information
?
-
-
MHV Sia receptor-binding specificity corresponds to the sialate-O-acetylesterase substrate preference of hemagglutinin-esterase , and hemagglutinin-esterase is sufficient to mediate virion binding to natural sialoglycoconjugates
-
-
?
additional information
?
-
-
MHV Sia receptor-binding specificity corresponds to the sialate-O-acetylesterase substrate preference of hemagglutinin-esterase , and hemagglutinin-esterase is sufficient to mediate virion binding to natural sialoglycoconjugates
-
-
?
additional information
?
-
-
the enzyme of Influenzy C virus exhibits sialate-4-O-acetylesterase specificity
-
-
?
additional information
?
-
-
MHV Sia receptor-binding specificity corresponds to the sialate-O-acetylesterase substrate preference of hemagglutinin-esterase, and hemagglutinin-esterase is sufficient to mediate virion binding to natural sialoglycoconjugates
-
-
?
additional information
?
-
-
enhanced B-cell receptor signalling through hyper-9-O-acetylation of alpha2-6-linked sialic acid on N-glycans and defective CD22 inhibitory signalling in absence of the enzyme
-
-
?
additional information
?
-
-
sialic acid acetyl esterase removes acetyl moieties from the 9-OH position of sialic acid
-
-
?
additional information
?
-
-
the enzyme of Rat sialoadacryoadenitis coronavirus exhibits sialate-4-O-acetylesterase specificity
-
-
?
additional information
?
-
-
strict substrate specificity for O-acetylated acids and a broad specificity for small synthetic esters, little or no activity against natural acetylated compounds other than sialic acids
-
-
?
additional information
?
-
-
LSE can act only on O-acetyl-esters at the 9-position of sialic acids
-
-
?
additional information
?
-
-
O-acetyl esters
-
-
?
additional information
?
-
-
specific for sialic acids and selectively cleaves acetyl groups at the 9-position. it deacetylates di-O-acetyl- and tri-O-acetyl-N-acetylneuraminic acids by first cleaving the O-acetyl ester at the 9-position. The 7- and 8-acetylesters then undergo spontaneous migration to the 9-position, where they can be cleaved
-
-
?
additional information
?
-
NanS can act upon complex N-glycans released from erythropoietin, bovine submaxillary mucin and oral epithelial cell-bound glycans. When incubated with its cognate sialidase, NanS increases sialic acid release from mucin and oral epithelial cell surfaces. Enzyme does not remove acetyl groups at the 4-O position
-
-
?
additional information
?
-
-
NanS can act upon complex N-glycans released from erythropoietin, bovine submaxillary mucin and oral epithelial cell-bound glycans. When incubated with its cognate sialidase, NanS increases sialic acid release from mucin and oral epithelial cell surfaces. Enzyme does not remove acetyl groups at the 4-O position
-
-
?
additional information
?
-
the enzyme show no activity with N-acetyl-O-5,4-diacetylneuraminate
-
-
?
additional information
?
-
-
the enzyme show no activity with N-acetyl-O-5,4-diacetylneuraminate
-
-
?
additional information
?
-
the enzyme show no activity with N-acetyl-O-5,4-diacetylneuraminate
-
-
?
additional information
?
-
-
O-acetylated sialic acids
-
-
?
additional information
?
-
-
O-acetylated sialic acids
-
-
?
additional information
?
-
-
O-acetylated sialic acids
-
-
?
additional information
?
-
-
O-acetylated sialic acids
-
-
?
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2-alpha-thiomethylmercuryl 9-acetamido-9-deoxy sialoside
-
competitive inhibition, Ki: 4.2 mM; the inhibitor is used to prepare heavy atom derivatives of the crystals
9-acetamido-N-acetyl-O-acetylneuraminate
Alpha-naphthyl acetate
-
competitive inhibitor
ammonium (allyl 5-acetamido-3,5-dideoxy-4-O-methyl-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
ammonium (allyl 5-acetamido-9-O-methyl-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
bis-p-nitrophenyl phosphate
-
little effect on the activity
CHAPS
-
lowers the activity by 40%
deoxycholate
-
75-80% loss of activity at 2% concentration
diammonium (allyl 5-acetamido-3,5-dideoxy-4-O-(P-methylphosphonyl)-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
diammonium (allyl 5-acetamido-3,5-dideoxy-9-O-(P-methylphosphonyl)-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
Diethyl-4-nitrophenylphosphate
diisopropyl fluorophosphate
diisopropyl fluorophosphates
-
complete inhibition at 1 mM
diisopropylfluorophosphate
-
1 mM, 25°C, 15 min, total loss of activity
F-
-
little effect on the activity
N-acetyl-9-O-acetylneuraminate
-
substrate inhibition above 2 mM
p-chloromercuribenzoate
-
little effect on the activity
paraoxon
-
diethyl-4-nitrohenylphosphate (E600), 1 mM at 25°C within 15 min leads to total loss of activity
phenylmethylsulfonyl fluoride
-
complete inhibition at 10 mM
PMSF
-
45% inhibition at 1 mM
2,3-Butanedione
-
inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition
2,3-Butanedione
-
inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition
2,3-Butanedione
-
inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition
2,3-Butanedione
-
inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition
2,3-Butanedione
-
irreversibly inactivated
2,3-Butanedione
-
inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition
3,4-dichloroisocoumarin
-
-
3,4-dichloroisocoumarin
-
-
3,4-dichloroisocoumarin
-
-
3,4-dichloroisocoumarin
-
-
9-acetamido-N-acetyl-O-acetylneuraminate
-
no effect up to 5 mM
9-acetamido-N-acetyl-O-acetylneuraminate
-
little effect at 5 mM
ammonium (allyl 5-acetamido-3,5-dideoxy-4-O-methyl-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
-
-
ammonium (allyl 5-acetamido-3,5-dideoxy-4-O-methyl-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
-
-
ammonium (allyl 5-acetamido-9-O-methyl-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
-
-
ammonium (allyl 5-acetamido-9-O-methyl-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
-
-
Cu2+
5 mM, 30% residual activity
Cu2+
-
complete inhibition at 1 mM
diammonium (allyl 5-acetamido-3,5-dideoxy-4-O-(P-methylphosphonyl)-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
-
-
diammonium (allyl 5-acetamido-3,5-dideoxy-4-O-(P-methylphosphonyl)-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
-
-
diammonium (allyl 5-acetamido-3,5-dideoxy-9-O-(P-methylphosphonyl)-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
-
-
diammonium (allyl 5-acetamido-3,5-dideoxy-9-O-(P-methylphosphonyl)-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
-
-
Diethyl-4-nitrophenylphosphate
-
50% inhibition at 0.0024 mM
Diethyl-4-nitrophenylphosphate
-
-
Diethyl-4-nitrophenylphosphate
-
50% inhibition at 0.24 mM
Diethyl-4-nitrophenylphosphate
-
Diethyl-4-nitrophenylphosphate
-
-
Diethyl-4-nitrophenylphosphate
-
irreversibly inactivated
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
50% inhibition at 0.35 mM
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
DFP strong inhibition
diisopropyl fluorophosphate
-
50% inhibition at 0.01 mM
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
irreversibly inactivated
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
irreversibly inactivated
Hg2+
-
50% inhibition at 0.0035 mM
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
little effect on the activity
Phenylglyoxal
-
inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition
Phenylglyoxal
-
inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition
Phenylglyoxal
-
inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition
Phenylglyoxal
-
inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition
Phenylglyoxal
-
irreversibly inactivated
Phenylglyoxal
-
inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition
physostigmine
-
25% inhibition at 10 mM
physostigmine
-
25% inhibition at 10 mM
additional information
not inhibitory: Ca2+, Zn2+, Co2+, Mn2+ and Mg2+ or EDTA
-
additional information
-
not inhibitory: Ca2+, Zn2+, Co2+, Mn2+ and Mg2+ or EDTA
-
additional information
-
synthesis and evaluation of a series of sialosides modified at the 4- and 9-hydroxy group for inhibition of the viral haemagglutinin-esterase activity from various Orthomyxoviruses and Coronaviruses, overview. While no inhibition of the sialate-4-O-acetylesterases from Mouse hepatitis virus strain S or Sialodacryoadenitis virus is found, a 9-O-methyl derivative displays inhibitory activity against recombinant sialate-9-O-acetylesterase from Influenza C virus. No inhibition of Bovine coronavirus by ammonium (allyl 5-acetamido-3,5-dideoxy-4-O-methyl-D-glycero-alpha-D-galacto-2-nonulopyranosidonate) and diammonium (allyl 5-acetamido-3,5-dideoxy-4-O-(P-methylphosphonyl)-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
-
additional information
-
bis-(4-nitrophenyl)phosphate, 1 mM Ca2+, 1 mM ethylene diaminotetraacetate (EDTA) without influence on activity
-
additional information
-
no inhibition by PMSF
-
additional information
-
synthesis and evaluation of a series of sialosides modified at the 4- and 9-hydroxy group for inhibition of the viral haemagglutinin-esterase activity from various Orthomyxoviruses and Coronaviruses, overview. While no inhibition of the sialate-4-O-acetylesterases from Mouse hepatitis virus strain S or Sialodacryoadenitis virus is found, a 9-O-methyl derivative displays inhibitory activity against recombinant sialate-9-Oacetylesterase from Influenza C virus. No inhibition of Influenza C virus by ammonium (allyl 5-acetamido-3,5-dideoxy-4-O-methyl-D-glycero-a-D-galacto-2-nonulopyranosidonate) and diammonium (allyl 5-acetamido-3,5-dideoxy-4-O-(P-methylphosphonyl)-D-glycero-a-d-galacto-2-nonulopyranosidonate)
-
additional information
-
synthesis and evaluation of a series of sialosides modified at the 4- and 9-hydroxy group for inhibition of the viral haemagglutinin-esterase activity from various Orthomyxoviruses and Coronaviruses, overview. While no inhibition of the sialate-4-O-acetylesterases from Mouse hepatitis virus strain S or Sialodacryoadenitis virus is found, a 9-O-methyl derivative displays inhibitory activity against recombinant sialate-9-O-acetylesterase from Influenza C virus. No inhibition of Mouse hepatitis virus strain S by ammonium (allyl 5-acetamido-9-O-methyl-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosidonate) and diammonium (allyl 5-acetamido-3,5-dideoxy-9-O-(P-methylphosphonyl)-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
-
additional information
-
synthesis and evaluation of a series of sialosides modified at the 4- and 9-hydroxy group for inhibition of the viral haemagglutinin-esterase activity from various Orthomyxoviruses and Coronaviruses, overview. While no inhibition of the sialate-4-O-acetylesterases from Mouse hepatitis virus strain S or Sialodacryoadenitis virus is found, a 9-O-methyl derivative displays inhibitory activity against recombinant sialate-9-O-acetylesterase from Influenza C virus. No inhibition of Rat sialoadacryoadenitis coronavirus by ammonium (allyl 5-acetamido-9-O-methyl-3,5-dideoxy-dglycero-alpha-D-galacto-2-nonulopyranosidonate) and diammonium (allyl 5-acetamido-3,5-dideoxy-9-O-(P-methylphosphonyl)-D-glycero-alpha-D-galacto-2-nonulopyranosidonate)
-
additional information
-
not affected by detergents, i.e. Triton X-100, Triton CF-54, saponin; not affected by EDTA
-
additional information
-
not affected by detergents, i.e. Triton X-100, Triton CF-54, saponin
-
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evolution
-
although the backbone of the structure is similar to previously characterized family members, sequence comparisons indicate that this family can be further subdivided into two subfamilies with somewhat different fingerprints. NanS is the founding member of group II. Sequence motifs and two subfamilies of SGNH hydrolases, overview
evolution
-
in apparent contrast to human and ungulate host range variants of Betacoronavirus-1, murine coronaviruses actually bind to O-Ac-sialic acids via hemagglutinin-esterase exclusively. Apparently, expansion of group A betacoronaviruses into new hosts and niches is accompanied by changes in hemagglutinin-esterase ligand and substrate preference and in the roles of hemagglutinin-esterase and sialidase in Sia receptor usage
evolution
-
in apparent contrast to human and ungulate host range variants of Betacoronavirus-1, murine coronaviruses actually bind to O-Ac-sialic acids via hemagglutinin-esterase exclusively. Apparently, expansion of group A betacoronaviruses into new hosts and niches is accompanied by changes in hemagglutinin-esterase ligand and substrate preference and in the roles of hemagglutinin-esterase and sialidase in Sia receptor usage
evolution
-
in apparent contrast to human and ungulate host range variants of Betacoronavirus-1, murine coronaviruses actually bind to O-Ac-sialic acids via hemagglutinin-esterase exclusively. Apparently, expansion of group A betacoronaviruses into new hosts and niches is accompanied by changes in hemagglutinin-esterase ligand and substrate preference and in the roles of hemagglutinin-esterase and sialidase in Sia receptor usage
evolution
-
in apparent contrast to human and ungulate host range variants of Betacoronavirus-1, murine coronaviruses actually bind to O-Ac-sialic acids via hemagglutinin-esterase exclusively. Apparently, expansion of group A betacoronaviruses into new hosts and niches is accompanied by changes in hemagglutinin-esterase ligand and substrate preference and in the roles of hemagglutinin-esterase and sialidase in Sia receptor usage
evolution
-
in apparent contrast to human and ungulate host range variants of Betacoronavirus-1, murine coronaviruses actually bind to O-Ac-sialic acids via hemagglutinin-esterase exclusively. Apparently, expansion of group A betacoronaviruses into new hosts and niches is accompanied by changes in hemagglutinin-esterase ligand and substrate preference and in the roles of hemagglutinin-esterase and sialidase in Sia receptor usage
-
malfunction
-
mice with a mutation in sialate: O-acetyl esterase (inframe deletion of exon 2, resulting in a protein lacking esterase activity) exhibit enhanced B cell receptor activation, defects in peripheral B cell development, and spontaneously develop antichromatin autoantibodies and glomerular immune complex deposits. The 9-O-acetylation state of sialic acid regulates the function of CD22, a Siglec that functions in vivo as an inhibitor of BCR signaling
malfunction
-
decreased sialate-O-acetylesterase activity occurs both in lysosomal and cytosolic fractions of childhood acute lymphoblastic leukemia, ALL, cell lines and primary cells from bone marrow of patients compared to peripheral blood mononuclear cells from healthy donors, which preferentially hydrolyse O-acetyl groups at C-9 of Sia
malfunction
defective variants of the enzyme are associated with an increased risk of various autoimmune diseases such as type 1 diabetes. Enzyme mutation A467V is involved in anti-PIT-1 antibody syndrome, phenotypes, overview
physiological function
-
besides sialidases, the haemagglutinin-esterases of Influenza C virus, Isavirus, Betacoronaviruses and Toroviruses represent another class of receptor-destroying enzymes, RDEs. They are sialate-O-acetylesterases, SOAE, hydrolysing O-acetyl esters of O-acetylated sialic acid derivatives as sialate-4-O-acetylesterases, 4-SOAE, and sialate-9-O-acetylesterases, 9-SOAE. The enzyme of Bovine coronavirus exhibits sialate-9-O-acetylesterase specificity
physiological function
-
besides sialidases, the haemagglutinin-esterases of Influenza C virus, Isavirus, Betacoronaviruses and Toroviruses represent another class of receptor-destroying enzymes, RDEs. They are sialate-O-acetylesterases, SOAE, hydrolysing O-acetyl esters of O-acetylated sialic acid derivatives as sialate-4-O-acetylesterases, 4-SOAE, and sialate-9-O-acetylesterases, 9-SOAE. The enzyme of Influenza C virus exhibits sialate-9-O-acetylesterase specificity
physiological function
-
besides sialidases, the haemagglutinin-esterases of Influenza C virus, Isavirus, Betacoronaviruses and Toroviruses represent another class of receptor-destroying enzymes, RDEs. They are sialate-O-acetylesterases, SOAE, hydrolysing O-acetyl esters of O-acetylated sialic acid derivatives as sialate-4-O-acetylesterases, 4-SOAE, and sialate-9-O-acetylesterases, 9-SOAE. The enzyme of Mouse hepatitis virus strain S exhibits sialate-4-O-acetylesterase specificity
physiological function
-
besides sialidases, the haemagglutinin-esterases of Influenza C virus, Isavirus, Betacoronaviruses and Toroviruses represent another class of receptor-destroying enzymes, RDEs. They are sialate-O-acetylesterases, SOAE, hydrolysing O-acetyl esters of O-acetylated sialic acid derivatives as sialate-4-O-acetylesterases, 4-SOAE, and sialate-9-O-acetylesterases, 9-SOAE. The enzyme of Rat sialoadacryoadenitis coronavirus exhibits sialate-4-O-acetylesterase specificity
physiological function
-
sialate-O-acetylesterases, SIAE, are important enzymes in sialic acid metabolism. They hydrolyse 4- or 9-O-acetyl groups of either glycosidically linked or free sialic acids released from glycoconjugates by sialidases. Both sialate-O-acetylesterase, SIAE, and sialate-O-acetyltranferase, SOAT, activities seem to be responsible for the enhanced level of Neu5,9Ac2 in lymphoblasts, which is a hall mark in acute lymphoblastic leukemia
physiological function
-
the O-acetylesterase is probably essential for the synthesis of capsular Neu5Ac in Streptococcus suis
physiological function
-
sialic acid acetyl esterase removes acetyl moieties from the 9-OH position of sialic acid, and thus permits alpha2,6 linked sialic acid on N-glycans on B cell glycoproteins to interact with CD22/Siglec-2, a sialic acid binding lectin that can inhibit B cell antigen receptor signaling
physiological function
sialic acid acetyl esterase removes acetyl moieties from the 9-OH position of sialic acid, and thus permits alpha2,6 linked sialic acid on N-glycans on B cell glycoproteins to interact with CD22/Siglec-2, a sialic acid binding lectin that can inhibit B cell antigen receptor signaling
physiological function
sialic acid acetylesterase plays a crucial role in regulating the threshold of autoantibody production of B-cells
physiological function
a SiaBb1 construct that lacks the SGNH hydrolase and Lam G domains cannot catalyze 4-nitrophenyl acetate hydrolysis, but retains sialidase activity
physiological function
expression of gene complements an Escherichia coli K-12 NanS deletion strain. Recombinant Escherichia coli degrades 5-N-acetyl-9-O-acetylneuraminic acid and is able to grow on 5-N-acetyl-9-O-acetylneuraminic acid as sole carbon source
physiological function
when incubated with its cognate sialidase, NanS increases sialic acid release from mucin and oral epithelial cell surfaces. The esterase improves sialic acid harvesting for Tannerella forsythia and potentially other members of the oral microbiome
additional information
-
SsNeuAc contains a asignature consensus sequence for serine esterase, Gly-Xaa-Ser-Xaa-Gly, is found within the C-terminal half
additional information
-
the NanS catalytic center contains Ser19 and His301 but no Asp/Glu is present to form the classical catalytic triad
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F211A
abrogated ligand recognition and binding
L266A
abrogated ligand recognition and binding
L267A
abrogated ligand recognition and binding
S40A
catalytically inactive, active site residue, retained lectin activity
Y184A
decreased ligand binding affinity
E26A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type NanS
H301N
-
site-directed mutagenesis, inactive mutant
S19A
-
site-directed mutagenesis, inactive mutant
S300A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type NanS
T294A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type NanS
T294S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type NanS
A385T
naturally occuring mutation
A394T
naturally occuring mutation
C443R
naturally occuring mutation
F404S
naturally occuring mutation
G419E
naturally occuring mutation
G514A
naturally occuring mutation
G64S
naturally occuring mutation, the enzyme shows unaltered catalytic activity compared to the wild-type enzyme. The mutant enzyme is poorly secreted when overexpressed
H447R
naturally occuring mutation
H472Q
naturally occuring mutation
K434T
naturally occuring mutation
M456I
naturally occuring mutation
M456T
naturally occuring mutation
M89V
naturally occuring mutation, the enzyme shows unaltered catalytic activity compared to the wild-type enzyme. The mutant enzyme is poorly secreted when overexpressed
Q309P
naturally occuring mutation, the mutant shows highly reduced catalytic activity compared with the wild-type enzyme
Q428L
naturally occuring mutation
Q462R
naturally occuring mutation
R387W
naturally occuring mutation
R393C
naturally occuring mutation
R393H
naturally occuring mutation
R479C
naturally occuring mutation
S127A
naturally occuring mutation, the enzyme shows below 10% catalytic activity compared to the wild-type enzyme
V459I
naturally occuring mutation
S57T
-
loss of esterase activity
C196F
-
naturally occuring mutation, the mutant shows highly reduced catalytic activity compared with the wild-type enzyme
Q335P
-
naturally occuring mutation, the mutant shows highly reduced catalytic activity compared with the wild-type enzyme
S258A
-
site-directed mutagenesis
A467V
naturally occuring mutation from patients with anti-PIT-1 antibody syndrome. The mutation occurs in a heterozygous state in all the patients with anti-PIT-1 antibody syndrome, and in 6% of control subjects, the prevalence is significantly increased in the patients
A467V
naturally occuring mutation, the enzyme shows over 110% catalytic activity compared to the wild-type enzyme. The mutant is secreted upon overexpression
H377A
complete loss of activity
H377A
the mutation abolishes the enzymatic activity
K71R
naturally occuring mutation from patients with anti-PIT-1 antibody syndrome. The mutation occurs in a heterozygous state in 2 of 3 patients with anti-PIT-1 antibody syndrome, and in 11% of control subjects, the prevalence is significantly increased in the patients
K71R
naturally occuring mutation, the enzyme shows over 50% catalytic activity compared to the wild-type enzyme. The mutant is secreted upon overexpression
S332A
no significant influence on activity
S332A
the mutation does not influence the activity of the enzyme significantly
T132A
complete loss of activity
T132A
the mutation abolishes the enzymatic activity
additional information
-
construction of recombinant MHV-A59 derivatives in which the autologous genes for hemagglutinin-esterase and sialidase are replaced by those of MHV-S or MHV-DVIM by targeted RNA recombination. The mutants do not express functional hemagglutinin-esterase, in MHV-A59, the hemagglutinin-esterase gene is interrupted by a nonsense mutation at codon 15 and that consequently MHV-A59 and derivates rMHV-A59-SDVIM and rMHV-A59-SS do not express the hemagglutinin-esterase protein
additional information
-
the mutant SsNeuAs truncated from 166 to 233 amino acids at the N-terminal a re active for pNP-Ac and their esterase activities are almost the same as the wild-type, only with one exception of the SsNeuA167-410, while the mutant SsNeuAs terminated at amino acid position of 227, 232, 233, 241, 247, 267, 283, 293, 312, 322, 338, 355 and 377 are inactive in CMP-Neu5Ac synthetase activity, even removal of 33 amino acid residues at C-terminal of the SsNeuA leads to a complete loss of CMP-Neu5Ac synthetase activity
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