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Information on EC 3.2.1.18 - exo-alpha-sialidase and Organism(s) Streptococcus pneumoniae and UniProt Accession P62575
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3.2.1.18 exo-alpha-sialidaseIUBMB Comments
The enzyme does not act on 4-O-acetylated sialic acids. endo-alpha-Sialidase activity is listed as EC 3.2.1.129, endo-alpha-sialidase. See also EC 4.2.2.15 anhydrosialidase.
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Word Map
- 3.2.1.18
- influenza
-
sialic
- viruses
- vaccine
- pandemic
- oseltamivir
- lectin
-
sialylated
- oligosaccharide
- subtype
- epitope
- erythrocyte
- gangliosides
- lymphocyte
-
reassortant
-
hemagglutination
-
anti-influenza
- chicken
- glycans
-
surveillance
- galactose
- cholera
-
desialylation
- hn
- glycoconjugates
-
outbreak
- cruzi
-
poultry
- virion
- bird
- pronase
- parainfluenza
-
epidemic
-
n-acetylneuraminic
- trypanosoma
- peanut
- mucin
-
n-linked
- newcastle
-
agglutination
- perfringens
- nucleoprotein
-
prophylaxis
-
concanavalin
- medicine
-
drift
-
sendai
- analysis
- n-acetylgalactosamine
- ferret
- nutrition
-
endoglycosidase
- molecular biology
- diagnostics
- gm3
The taxonomic range for the selected organisms is: Streptococcus pneumoniae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
neuraminidase, sialidase, glycosyl hydrolase, trans-sialidase, hemagglutinin-neuraminidase, major surface antigen, alpha2,6-sialyltransferase, cytosolic sialidase, endosialidase, lysosomal sialidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylneuraminidase
-
-
-
-
Acetylneuraminyl hydrolase
-
-
-
-
acylneuraminyl glycohydrolase
-
-
-
-
alpha-neuraminidase
-
-
-
-
Cytosolic sialidase
-
-
-
-
G9 sialidase
-
-
-
-
Ganglioside sialidase
-
-
-
-
Lysosomal sialidase
-
-
-
-
Major 85 kDa surface antigen
-
-
-
-
Major surface antigen
-
-
-
-
Membrane sialidase
-
-
-
-
Mouse skeletal muscle sialidase
-
-
-
-
MSS
-
-
-
-
MTS
-
-
-
-
mucopolysaccharide N-acetylneuraminylhydrolase
-
-
-
-
Murine thymic sialidase
-
-
-
-
N-acylneuraminate glycohydrolase
-
-
-
-
NanA
NANase
-
-
-
-
neuraminidase
SA85-1.1 protein
-
-
-
-
SA85-1.2 protein
-
-
-
-
SA85-1.3 protein
-
-
-
-
sialidase
STNA
-
-
-
-
neuraminidase
-
-
-
-
sialidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
acetylneuraminyl hydrolase
The enzyme does not act on 4-O-acetylated sialic acids. endo-alpha-Sialidase activity is listed as EC 3.2.1.129, endo-alpha-sialidase. See also EC 4.2.2.15 anhydrosialidase.
CAS REGISTRY NUMBER
COMMENTARY
9001-67-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(N-glycolylneuraminic acid)(alpha2,3)Galbeta-p-nitrophenol + H2O
(N-glycolylneuraminic acid)(alpha2,3)Gal + p-nitrophenol
-
-
-
-
?
2'-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid + H2O
?
-
-
-
-
?
2-chloro-5-(4-methoxyspiro(1,2-dioxetane-3,29-(5-chloro)tricyclo[3.3.1.13,7]decan)-4-yl-phenyl-5-acetamido-3,5-dideoxy-alpha-D-glycero-D-galacto-2-nonulopyranoside)onate + H2O
?
-
-
-
-
?
4-nitrophenyl O-(3,5-dideoxy-5-fluoro-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-3)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-(3,5-dideoxy-5-fluoro-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-6)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-(3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-3)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-(3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-6)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-(3-deoxy-5-O-methyl-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-3)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-(3-deoxy-5-O-methyl-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-6)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-(5-azido-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-3)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-(5-azido-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid)-(2-6)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-[5-(2-azidoacetamido)-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid]-(2-3)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-[5-(2-azidoacetamido)-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid]-(2-6)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-[5-(2-fluoroacetamido)-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid]-(2-3)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-[5-(2-fluoroacetamido)-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid]-(2-6)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-[5-(2-methoxyacetamido)-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid]-(2-3)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl O-[5-(2-methoxyacetamido)-3,5-dideoxy-D-glycero-alpha-D-galacto-2-nonulopyranosylonic acid]-(2-6)-O-beta-D-galactopyranoside + H2O
?
-
-
-
-
?
N-acetylneuraminic acid-alpha-2,3-lactose + H2O
N-acetylneuraminic acid + lactose
-
-
-
-
?
N-acetylneuraminic acid-alpha-2,6-lactose + H2O
N-acetylneuraminic acid + lactose
-
-
-
-
?
N-acetylneuraminyllactose + H2O
N-acetylneuraminic acid + lactose
-
-
-
-
?
Neu5,9Ac2(alpha2,3)Galbeta-p-nitrophenol + H2O
Neu5,9Ac2(alpha2,3)Gal + p-nitrophenol
-
-
-
-
?
Neu5Ac(alpha2,3)Galbeta-p-nitrophenol + H2O
Neu5Ac(alpha2,3)Gal + p-nitrophenol
-
-
-
-
?
additional information
?
-
-
NanB may contribute to Strreptococcus pneumoniae colonization and pathogenesis
-
-
?
additional information
?
-
NanB may contribute to Strreptococcus pneumoniae colonization and pathogenesis
-
-
?
additional information
?
-
-
Streptococcus pneumoniae is able to utilize complex N-linked human glycoconjugates as a sole source of carbon to sustain growth and efficient growth is dependent upon the sequential deglycosylation of the glycoconjugate substrate by pneumococcal exoglycosidases NanA, BgaA, and StrH. The second pneumococcal neuraminidase, NanB, is involved in the deglycosylation of host glycoconjugates and NanB activity can partially compensate for the loss or dysfunction of NanA
-
-
?
additional information
?
-
Streptococcus pneumoniae is able to utilize complex N-linked human glycoconjugates as a sole source of carbon to sustain growth and efficient growth is dependent upon the sequential deglycosylation of the glycoconjugate substrate by pneumococcal exoglycosidases NanA, BgaA, and StrH. The second pneumococcal neuraminidase, NanB, is involved in the deglycosylation of host glycoconjugates and NanB activity can partially compensate for the loss or dysfunction of NanA
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid + H2O
?
-
-
-
-
?
additional information
?
-
-
NanB may contribute to Strreptococcus pneumoniae colonization and pathogenesis
-
-
?
additional information
?
-
NanB may contribute to Strreptococcus pneumoniae colonization and pathogenesis
-
-
?
additional information
?
-
-
Streptococcus pneumoniae is able to utilize complex N-linked human glycoconjugates as a sole source of carbon to sustain growth and efficient growth is dependent upon the sequential deglycosylation of the glycoconjugate substrate by pneumococcal exoglycosidases NanA, BgaA, and StrH. The second pneumococcal neuraminidase, NanB, is involved in the deglycosylation of host glycoconjugates and NanB activity can partially compensate for the loss or dysfunction of NanA
-
-
?
additional information
?
-
Streptococcus pneumoniae is able to utilize complex N-linked human glycoconjugates as a sole source of carbon to sustain growth and efficient growth is dependent upon the sequential deglycosylation of the glycoconjugate substrate by pneumococcal exoglycosidases NanA, BgaA, and StrH. The second pneumococcal neuraminidase, NanB, is involved in the deglycosylation of host glycoconjugates and NanB activity can partially compensate for the loss or dysfunction of NanA
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,6-anhydro-9-azido-3,5,9-trideoxy-5-(2-hydroxyacetamido)-D-glycero-D-galacto-non-2-enonic acid
-
-
2,6-anhydro-9-azido-5-(2-azidoacetamido)-3,5,9-trideoxy-D-glycero-D-galacto-non-2-enonic acid
-
-
5-acetamido-2,6-anhydro-3,5-dideoxy-9-O-methyl-D-glycero-D-galacto-non-2-enonic acid
-
-
5-acetamido-2,6-anhydro-9-azido-3,5,9-trideoxy-D-glycero-D-galacto-non-2-enonic acid
-
-
5-acetamido-9-aminopropyl-2,6-anhydro-3,5,9-trideoxy-D-glycero-D-galacto-non-2-enonic acid
-
-
2-deoxy-2,3-dehydro-N-acetylneuraminic acid
-
inhibition occurs in the micromolar range
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
2,6-anhydro-9-azido-3,5,9-trideoxy-5-(2-hydroxyacetamido)-D-glycero-D-galacto-non-2-enonic acid
Streptococcus pneumoniae
-
IC50 above 10 mM, with Neu5Acalpha(2->3)Galbeta-4-nitrophenyl as substrate, at pH 5.0 and 37°C
1
2,6-anhydro-9-azido-5-(2-azidoacetamido)-3,5,9-trideoxy-D-glycero-D-galacto-non-2-enonic acid
Streptococcus pneumoniae
-
IC50 above 1.0 mM, with Neu5Acalpha(2->3)Galbeta-4-nitrophenyl as substrate, at pH 5.0 and 37°C
3.7
2-deoxy-2,3-dehydro-N-acetylneuraminic acid
Streptococcus pneumoniae
-
with Neu5Acalpha(2->3)Galbeta-4-nitrophenyl as substrate, at pH 5.0 and 37°C
3
5-acetamido-2,6-anhydro-3,5-dideoxy-9-O-methyl-D-glycero-D-galacto-non-2-enonic acid
Streptococcus pneumoniae
-
with Neu5Acalpha(2->3)Galbeta-4-nitrophenyl as substrate, at pH 5.0 and 37°C
3.3
5-acetamido-2,6-anhydro-9-azido-3,5,9-trideoxy-D-glycero-D-galacto-non-2-enonic acid
Streptococcus pneumoniae
-
with Neu5Acalpha(2->3)Galbeta-4-nitrophenyl as substrate, at pH 5.0 and 37°C
5.4
5-acetamido-9-aminopropyl-2,6-anhydro-3,5,9-trideoxy-D-glycero-D-galacto-non-2-enonic acid
Streptococcus pneumoniae
-
with Neu5Acalpha(2->3)Galbeta-4-nitrophenyl as substrate, at pH 5.0 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the NanA neuraminidase of Streptococcus pneumoniae is involved in biofilm formation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
56500 Da domain that retains full enzymatic activity, in presence of inhibitor 2-deoxy-2,3-dehydro-N-acetyl neuraminic acid. 2.5 A resolution, space group P212121
free enzyme and in complex with N-acetylneuraminic acid or 2,3-dehydro-2-deoxy-N-acetylneuraminic acid, sitting drop vapor diffusion method, using 100 mM HEPES (pH 7.0) and 30% Jeffamine ED-2001 (pH 7.0), at 21°C
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
subcloning of a 56500 Da domain that retains full enzymatic activity
additional information
-
subcloning of a 56500 Da domain that retains full enzymatic activity
additional information
-
in neuraminidase NanA deletion mutant, NanB can partially support the growth of pneumococci on glycoconjugates
additional information
in neuraminidase NanA deletion mutant, NanB can partially support the growth of pneumococci on glycoconjugates
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
subcloning of a 56500 Da domain that retains full enzymatic activity, expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Stahl, W.L.; O'Tool, R.D.
Pneumococcal neuraminidase: purification and properties
Biochim. Biophys. Acta
268
480-487
1972
Streptococcus pneumoniae
Tanenbaum, S.W.; Gulbinsky, J.; Katz, M.; Sun, S.C.
Separation, purification and some properties of pneumococcal neuraminidase isoenzymes
Biochim. Biophys. Acta
198
242-254
1970
Streptococcus pneumoniae
Tanenbaum, S.W.; Sun, S.C.
Some molecular properties of pneumococcal neuraminidase isoenzymes
Biochim. Biophys. Acta
229
824-828
1971
Clostridium perfringens, Streptococcus pneumoniae
Chokhawala, H.A.; Yu, H.; Chen, X.
High-throughput substrate specificity studies of sialidases by using chemoenzymatically synthesized sialoside libraries
ChemBioChem
8
194-201
2007
Clostridium perfringens, Paenarthrobacter ureafaciens, Salmonella enterica subsp. enterica serovar Typhimurium, Streptococcus pneumoniae, Streptococcus sp.
Burnaugh, A.M.; Frantz, L.J.; King, S.J.
Growth of Streptococcus pneumoniae on human glycoconjugates is dependent upon the sequential activity of bacterial exoglycosidases
J. Bacteriol.
190
221-230
2008
Streptococcus pneumoniae, Streptococcus pneumoniae (Q54727)
Xu, G.; Li, X.; Andrew, P.W.; Taylor, G.L.
Structure of the catalytic domain of Streptococcus pneumoniae sialidase NanA
Acta Crystallogr. Sect. F
64
772-775
2008
Streptococcus pneumoniae (P62575), Streptococcus pneumoniae
Hsiao, Y.S.; Parker, D.; Ratner, A.J.; Prince, A.; Tong, L.
Crystal structures of respiratory pathogen neuraminidases
Biochem. Biophys. Res. Commun.
380
467-471
2009
Streptococcus pneumoniae, Pseudomonas aeruginosa
Parker, D.; Soong, G.; Planet, P.; Brower, J.; Ratner, A.J.; Prince, A.
The NanA neuraminidase of Streptococcus pneumoniae is involved in biofilm formation
Infect. Immun.
77
3722-3730
2009
Streptococcus pneumoniae
Cao, H.; Li, Y.; Lau, K.; Muthana, S.; Yu, H.; Cheng, J.; Chokhawala, H.A.; Sugiarto, G.; Zhang, L.; Chen, X.
Sialidase substrate specificity studies using chemoenzymatically synthesized sialosides containing C5-modified sialic acids
Org. Biomol. Chem.
7
5137-5145
2009
Clostridium perfringens, Streptococcus pneumoniae, Pasteurella multocida, Salmonella enterica subsp. enterica serovar Typhimurium, Vibrio cholerae serotype O1
Khedri, Z.; Li, Y.; Cao, H.; Qu, J.; Yu, H.; Muthana, M.M.; Chen, X.
Synthesis of selective inhibitors against V. cholerae sialidase and human cytosolic sialidase NEU2
Org. Biomol. Chem.
10
6112-6120
2012
Streptococcus pneumoniae, Vibrio cholerae (P0C6E9), Vibrio cholerae, Clostridium perfringens (P10481), Salmonella enterica subsp. enterica serovar Typhimurium (P29768), Homo sapiens (Q9Y3R4), Homo sapiens
Nishikawa, T.; Shimizu, K.; Tanaka, T.; Kuroda, K.; Takayama, T.; Yamamoto, T.; Hanada, N.; Hamada, Y.
Bacterial neuraminidase rescues influenza virus replication from inhibition by a neuraminidase inhibitor
PLoS ONE
7
e45371
2012
Paenarthrobacter ureafaciens, Streptococcus pneumoniae, influenza A virus, Vibrio cholerae serotype O1, Streptococcus pneumoniae IID553
EXTERNAL LINKS (specific for EC-Number 3.2.1.18)
Transporter Classification Database (TCDB): 1.A.32.1.3
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