3.2.1.18: exo-alpha-sialidase

This is an abbreviated version!
For detailed information about exo-alpha-sialidase, go to the full flat file.

Word Map on EC 3.2.1.18

Reaction

colominic acid
+
H2O
=
sialic acid
+
lactose

Synonyms

More, neuraminidase, sialidase, alpha-neuraminidase, acetylneuraminidase, acylneuraminyl glycohydrolase, mucopolysaccharide N-acetylneuraminylhydrolase, Acetylneuraminyl hydrolase, Cytosolic sialidase, G9 sialidase, Ganglioside sialidase, Lysosomal sialidase, Major 85 kDa surface antigen, Major surface antigen, Membrane sialidase, Mouse skeletal muscle sialidase, MSS, MTS, Murine thymic sialidase, N-acylneuraminate glycohydrolase, NANase, SA85-1.1 protein, SA85-1.2 protein, SA85-1.3 protein, STNA, endosialidase, N-acetylneuraminosyl glycohydrolase, hemagglutinin-neuraminidase glycoprotein, HN, acid sialidase, NA, haemagglutinin-neuraminidase protein, trans-sialidase, TcTS, MmNEU3, Neu, alpha-sialidase, NA1, ganglioside-specific sialidase, Neu3, VCNA, NA2, NAN1, HsNEU2, sialidase Neu2, NEU4, endoNF, TSia, sialidase-3, N-acetyl-alpha-neuraminidase 3, IID sialidase, Neu4L sialidase, NanB, N-acetyl-alpha-neuraminidase 4, sialidase-4, sialidase-2, N-acetyl-alpha-neuraminidase 2, NEU1, N-acetyl-alpha-neuraminidase 1, alpha2,6-sialyltransferase, NanA, endo-N, NanI, sialidase II, endo-sialidase, exo-alpha-sialidase, alpha-N-acylneuraminate glycohydrolase, neuramindase, hemagglutinin-neuraminidase, alpha2,6-trans-sialidase, alpha2,6-sialidase, DELTA15Pd2,6ST, NEU4 long, NEU4 short, N-acetyl-alpha-neuraminidase, NanJ, NanH, neuraminidase 1, neuraminidase-1, PA2794, sialidase/neuraminidase mutant F129A, endo-N-acylneuraminidase, NEU2, NanPs, neuraminidase 2, neuraminidase 3, exo-sialidase, trans-sialidase 1, Tr6, sialidase 4, Neu3e, Neu3a, Neu3d, glycosyl hydrolase, NEU4L, N-acylneuraminosyl glycohydrolase, TDE0471, KDNase, SiaBb1, Am0705, Am0707, Am1757, Am2085, GH33C, NanICD, NanC, sialyl hydrolase

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.18 exo-alpha-sialidase

Engineering

Engineering on EC 3.2.1.18 - exo-alpha-sialidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D84A
the mutation significantly lowers the activity of the enzyme, but this mutant remains a retaining glycosidase
R171L
the mutant has higher activity on a N-acetylneuraminic acid-based substrate than wild type enzyme
Y358H
the mutation significantly lowers the activity of the enzyme, but this mutant remains a retaining glycosidase
D84A
-
the mutation significantly lowers the activity of the enzyme, but this mutant remains a retaining glycosidase
-
R171L
-
the mutant has higher activity on a N-acetylneuraminic acid-based substrate than wild type enzyme
-
Y358H
-
the mutation significantly lowers the activity of the enzyme, but this mutant remains a retaining glycosidase
-
Y317A
site-directed mutagenesis, mutation of a catalytic residue, loss of nearly all sialidase activity, highly reduced HA activity, mutant shows reduced fusion promotion activity
Y317F
site-directed mutagenesis, mutation of a catalytic residue, reduced sialidase activity, altered HA activity, mutant shows reduced fusion promotion activity
R498K
site-directed mutagenesis, mutation of a catalytic residue, reduced sialidase activity, slightly reduced HA activity, mutant shows reduced fusion promotion activity
R498Q
site-directed mutagenesis, mutation of a catalytic residue, highly reduced sialidase activity, slightly reduced HA activity, mutant shows reduced fusion promotion activity
S418A
site-directed mutagenesis, mutation of a catalytic residue, unaltered sialidase activity, altered HA activity, mutant shows reduced fusion promotion activity
Y262F
site-directed mutagenesis, mutation of a catalytic residue, retaining of nearly all sialidase activity, altered HA activity, mutant shows reduced fusion promotion activity
Y262S
site-directed mutagenesis, mutation of a catalytic residue, loss of nearly all sialidase activity, highly reduced HA activity, mutant shows reduced fusion promotion activity
E258D
site-directed mutagenesis, mutation of a catalytic residue, highly reduced sialidase activity, slightly reduced HA activity, mutant shows reduced fusion promotion activity
Y317S
site-directed mutagenesis, mutation of a catalytic residue, highly reduced sialidase activity, highly reduced HA activity, mutant shows reduced fusion promotion activity
E347K
the mutation affects the reactivity of polyclonal serum to the variant strain
I192M
E347K
Avian orthoavulavirus 1 Herts/33
-
the mutation affects the reactivity of polyclonal serum to the variant strain
-
Y317A
Avian orthoavulavirus 1 Kansas
-
site-directed mutagenesis, mutation of a catalytic residue, loss of nearly all sialidase activity, highly reduced HA activity, mutant shows reduced fusion promotion activity
-
Y317F
Avian orthoavulavirus 1 Kansas
-
site-directed mutagenesis, mutation of a catalytic residue, reduced sialidase activity, altered HA activity, mutant shows reduced fusion promotion activity
-
R498K
Avian orthoavulavirus 1 Kansas
-
site-directed mutagenesis, mutation of a catalytic residue, reduced sialidase activity, slightly reduced HA activity, mutant shows reduced fusion promotion activity
-
R498Q
Avian orthoavulavirus 1 Kansas
-
site-directed mutagenesis, mutation of a catalytic residue, highly reduced sialidase activity, slightly reduced HA activity, mutant shows reduced fusion promotion activity
-
S418A
Avian orthoavulavirus 1 Kansas
-
site-directed mutagenesis, mutation of a catalytic residue, unaltered sialidase activity, altered HA activity, mutant shows reduced fusion promotion activity
-
E347K
Avian orthoavulavirus 1 ZJ-01/00
-
the mutation affects the reactivity of polyclonal serum to the variant strain
-
E581A
-
the mutation results in complete loss of sialidase activity
R294K
Y370F
R340A
site-directed mutagenesis, almost inactive mutant
R114A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N88D
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E51D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y181F
site-directed mutagenesis, inactive mutant
E113A
site-directed mutagenesis, inactive mutant
Y412A
-
site-directed mutagenesis, 55-70% reduced activity compared to the wild-type enzyme, no internalization due to impaired endocytosis, location in the plasma membrane and the cytosol
L415A
-
site-directed mutagenesis, 30-50% reduced activity compared to the wild-type enzyme, no internalization due to impaired endocytosis, location in the plasma membrane and the cytosol
G413A
-
site-directed mutagenesis, activity and localization in the cell similar to the wild-type enzyme
Y179F
site-directed mutagenesis, inactive mutant
D46A
inactive
D50S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y370C
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D234N
the mutation results in significantly lower levels of sialidase activity (25%) compared to the wild type and is associated with sialosis
E218A
inactive
H277F
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Q112A
the mutant shows nearly 4fold increased activity towards 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid compared to the wild type
G162A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K45A
the mutant shows about 3fold increased activity towards 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid compared to the wild type
R245A
site-directed mutagenesis, inactive mutant
V217M/G243R
-
the mutation is associated with sialidosis type I phenotype
A160G
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
M87G
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
I105G
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
M87G/I105G
site-directed mutagenesis, inactive mutant
A160G/M87G/I105G
site-directed mutagenesis, inactive mutant
R45V
site-directed mutagenesis, inactive mutant
G419STOP
site-directed mutagenesis, the C-terminal 10-residue truncation leads to an increase in activity compared to the wild-type enzyme
L408STOP
site-directed mutagenesis, the large deletion leads to inactivation of the mutant
E225S
site-directed mutagenesis, almost inactive mutant
R25H
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
I407STOP
site-directed mutagenesis, almost inactive mutant
T403STOP
site-directed mutagenesis, inactive mutant
E51S
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
R114Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V107M
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E218Q
inactive
V217A
the mutation results in significantly lower levels of sialidase activity (44%) compared to the wild type and is associated with sialosis
Q270A
the mutant shows about 4fold increased activity towards 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid compared to the wild type
Q270E
the mutant shows about wild type activity
N173S
-
mutant sensitive to 4-azido-5-isobutyrylamino-2,3-didehydro-2,3,4,5-tetradeoxy-d-glycero-d-galacto-2-nonulopyranosic acid in neuraminidase inhibition assays but more than 10000fold less sensitive to the compound in hemagglutination inhibition tests than a recombinant Sendai virus whose hemagglutinin-neuraminidase is replaced with that of human parainfluenza virus-1. Its susceptibility to 4-azido-5-isobutyrylamino-2,3-didehydro-2,3,4,5-tetradeoxy-d-glycero-d-galacto-2-nonulopyranosic acid in plaque reduction assays is reduced fivefold and does not differ from that of recombinant Sendai virus whose hemagglutinin-neuraminidase was replaced with that of human parainfluenza virus-1 in mice. The N173S mutant fails to be efficiently eluted from erythrocytes and released from cells. It demonstrates reduced growth in cell culture and superior growth in mice. Rresults are consistent with the loss of the N-linked glycan at residue 173 in the mutant. Study suggests that the N-linked glycan at residue 173 masks a second receptor-binding site
R156K
-
neuraminidase activity is 71% of wild-type value
E277G
-
mutation results in an impairment of growth of the concerned virus
R292K
the mutant exhibits reduced inhibition to oseltamivir (33fold in IC50 values) but shows wild type inhibition to zanamivir and peramivir
D198N
E119D
R152K
the mutant exhibits reduced inhibition to oseltamivir (17.9fold in IC50 values) but shows wild type inhibition to zanamivir and peramivir
E227G
-
mutation results in an impairment of growth of the concerned virus
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
H274Y
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
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
W178L
-
mutation results in an impairment of growth of the concerned virus
S179A
-
mutation results in an impairment of growth of the concerned virus
E119A
the mutation confers reduced inhibition to zanamivir
N294S
the mutation confers reduced inhibition to oseltamivir (63.6fold increase in IC50 compared to the wild type)
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
S219T/A272V/Del245-248
-
revertant constructed from mutant N146K/S219T/A272V/Del245-248 for analysis of resistance to oseltamivir
N146K/A272V/Del245-248
-
revertant constructed from mutant N146K/S219T/A272V/Del245-248 for analysis of resistance to oseltamivir
N146K/S219T/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
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
E119G
the mutation confers reduced inhibition to zanamivir
E119A/R152K
inactive
E119D/R152K
inactive
E119G/R152K
inactive
D198N/R152K
inactive
E119A/D198N
inactive
E119D/D198N
inactive
R152K/H274Y
inactive
E119G/D198N
inactive
E119A/H274Y
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
E119D/H274Y
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
E119G/H274Y
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
R292K/H274Y
inactive
N294S/H274Y
inactive
E119A/R292K
inactive
E119D/R292K
inactive
E119G/R292K
inactive
D198N/R292K
inactive
D198N/H274Y
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
H274Y
-
the mutation confers resistance to oseltamivir, the viral fitness of the A/Brisbane/59/2007-like H274Y variant is not impaired
H275Y
the major oseltamivir resistance mutation H275Y causes a significant decrease in the enzyme's ability to bind oseltamivir
N248D
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
E119D
-
the mutation confers reduced inhibition by oseltamivir (a 95-fold increase in the 50% inhibitory concentration) and highly reduced inhibition by zanamivir, peramivir. and laninamivir (2660fold, 460fold, and 651fold increases in the 50% inhibitory concentration, respectively)
R152K
-
the mutant remains susceptible to peramivir, but confers reduced inhibition by zanamivir, oseltamivir, and laninamivir
N386K
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
N200S
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
Q136K
-
the mutation confers mainly reduced to highly reduced inhibition by zanamivir, peramivir, and laninamivir, but remains susceptible to oseltamivir
E119G
-
the mutation confers mainly reduced to highly reduced inhibition by zanamivir, peramivir, and laninamivir, but remains susceptible to oseltamivir
K432E
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
D199E
-
the mutant shows increased enzyme activity compared to the wild type enzyme
P458T
-
the mutant with decreased activity exhibits highly reduced inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
V264I
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
N270K
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
I321V
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
N369K
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
I223V
the substitution alone confers only a moderate reduction in oseltamivir affinity
S247N
the substitution alone confers only a moderate reduction in oseltamivir affinity
H275Y/I223V
the mutations result in extreme impairment of oseltamivir's inhibition potency
H275Y/S247N
the mutations result in extreme impairment of oseltamivir's inhibition potency
N248D
influenza A virus H1N1 pdm09
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
-
E119D
influenza A virus H1N1 pdm09
-
the mutation confers reduced inhibition by oseltamivir (a 95-fold increase in the 50% inhibitory concentration) and highly reduced inhibition by zanamivir, peramivir. and laninamivir (2660fold, 460fold, and 651fold increases in the 50% inhibitory concentration, respectively)
-
R152K
influenza A virus H1N1 pdm09
-
the mutant remains susceptible to peramivir, but confers reduced inhibition by zanamivir, oseltamivir, and laninamivir
-
N386K
influenza A virus H1N1 pdm09
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
-
N200S
influenza A virus H1N1 pdm09
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
-
H155Y
the mutation decreases enzymatic activity
V99I
the mutation increases enzymatic activity
N369H
the mutation increases enzymatic activity
S434D
the mutation decreases enzymatic activity
S372N
the mutation decreases enzymatic activity
S372H
the mutation decreases enzymatic activity
I400M
the mutation decreases enzymatic activity
W403R
the mutation decreases enzymatic activity
K432E
the mutation decreases enzymatic activity
M257I
the mutation decreases enzymatic activity
A284T
the mutation decreases enzymatic activity
S389R
the mutation decreases enzymatic activity for transferrin and increases enzymatic activity for fetuin
Y347N
the mutation increases enzymatic activity
R152K
the mutation leads to resistance against nfluenza virus neuraminidase inhibitors
G140R
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
Q138R
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
P139S
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
G140R
influenza B virus B/Kochi/41/2011
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
-
Q138R
influenza B virus B/Kochi/41/2011
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
-
P139S
influenza B virus B/Kochi/41/2011
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
-
G140R
influenza B virus B/Kochi/59/2011
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
-
Q138R
influenza B virus B/Kochi/59/2011
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
-
P139S
influenza B virus B/Kochi/59/2011
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
-
G140R
influenza B virus B/Kochi/60/2011
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
-
Q138R
influenza B virus B/Kochi/60/2011
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
-
P139S
influenza B virus B/Kochi/60/2011
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
-
Y370A
catalyzes the hydrolysis of phenyl beta-sialoside with an inversion of the anomeric configuration, 4% of the activity with Y370G
Y370G
Y370N
catalyzes the hydrolysis of phenyl beta-sialoside with an inversion of the anomeric configuration, 9% of the activity with Y370N
Y370T
catalyzes the hydrolysis of phenyl beta-sialoside with an inversion of the anomeric configuration, 9% of the activity with Y370T
E335K
D79A
-
inactive
R198K
-
inactive
R260A
-
inactive
R152K
-
the mutation mediates reduced inhibition by oseltamivir, zanamivir, peramivir and laninamivir (10-100fold increase of IC50 value compared to the wild type enzyme)
H274Y
-
mutant isolated from patient infected with H5N1. Ratio Ki mutant/Ki wild-type for inhibition by oseltamivir is 265, for inhibition by zanamivir is 1.9, respectively
E83G
-
mutation isolated in influenza virus subtype H3N2
D79V/S366N
-
mutation isolated in influenza virus subtype H3N1
L206I
-
mutation isolated in influenza virus subtype H4N1
N294S
-
mutant isolated from patient infected with H5N1. Ratio Ki mutant/Ki wild-type for inhibition by oseltamivir is 81, for inhibition by zanamivir is 7.2, respectively
Y252H
-
mutant isolated from patient infected with H5N1. Ratio Ki mutant/Ki wild-type for inhibition by oseltamivir is 0.1, for inhibition by zanamivir is 1.2, respectively
R368K
-
the mutation mediates reduced inhibition by oseltamivir, zanamivir and laninamivir (96-57fold increase of IC50 value compared to the wild type enzyme) as well as peramivir (172fold increase of IC50 value compared to the wild type enzyme)
R152K/V94I
-
the mutations mediate reduced inhibition by oseltamivir, zanamivir, peramivir and laninamivir (10-100fold increase of IC50 value compared to the wild type enzyme)
V94IK
-
the mutant shows normal inhibition by oseltamivir, zanamivir, peramivir and laninamivir
R152K
unidentified influenza virus A/Quebec/144147/09
-
the mutation mediates reduced inhibition by oseltamivir, zanamivir, peramivir and laninamivir (10-100fold increase of IC50 value compared to the wild type enzyme)
-
R368K
unidentified influenza virus A/Quebec/144147/09
-
the mutation mediates reduced inhibition by oseltamivir, zanamivir and laninamivir (96-57fold increase of IC50 value compared to the wild type enzyme) as well as peramivir (172fold increase of IC50 value compared to the wild type enzyme)
-
R152K/V94I
unidentified influenza virus A/Quebec/144147/09
-
the mutations mediate reduced inhibition by oseltamivir, zanamivir, peramivir and laninamivir (10-100fold increase of IC50 value compared to the wild type enzyme)
-
V94IK
unidentified influenza virus A/Quebec/144147/09
-
the mutant shows normal inhibition by oseltamivir, zanamivir, peramivir and laninamivir
-
H274Y
-
mutant isolated from patient infected with H5N1. Ratio Ki mutant/Ki wild-type for inhibition by oseltamivir is 265, for inhibition by zanamivir is 1.9, respectively
-
N294S
-
mutant isolated from patient infected with H5N1. Ratio Ki mutant/Ki wild-type for inhibition by oseltamivir is 81, for inhibition by zanamivir is 7.2, respectively
-
Y252H
-
mutant isolated from patient infected with H5N1. Ratio Ki mutant/Ki wild-type for inhibition by oseltamivir is 0.1, for inhibition by zanamivir is 1.2, respectively
-
additional information