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Information on EC 3.2.1.18 - exo-alpha-sialidase and Organism(s) Mus musculus and UniProt Accession O35657

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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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This record set is specific for:
Mus musculus
UNIPROT: O35657
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The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
neuraminidase, sialidase, glycosyl hydrolase, trans-sialidase, hemagglutinin-neuraminidase, major surface antigen, alpha2,6-sialyltransferase, cytosolic sialidase, endosialidase, neuraminidase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
neuraminidase 1
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acetylneuraminidase
-
-
-
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Acetylneuraminyl hydrolase
-
-
-
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acylneuraminyl glycohydrolase
-
-
-
-
alpha-neuraminidase
-
-
-
-
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
-
-
-
-
Major surface antigen
-
-
-
-
Membrane sialidase
-
-
-
-
MmNEU3
-
-
Mouse skeletal muscle sialidase
-
-
-
-
MSS
-
-
-
-
MTS
-
-
-
-
mucopolysaccharide N-acetylneuraminylhydrolase
-
-
-
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Murine thymic sialidase
-
-
-
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N-acylneuraminate glycohydrolase
-
-
-
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NANase
-
-
-
-
neuraminidase
SA85-1.1 protein
-
-
-
-
SA85-1.2 protein
-
-
-
-
SA85-1.3 protein
-
-
-
-
sialidase
STNA
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
9001-67-6
-
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
-
-
-
?
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferol + alpha-D-N-acetylneuraminic acid
show the reaction diagram
ganglioside GD1a + H2O
ganglioside GM1 + sialic acid
show the reaction diagram
ganglioside GD1a + H2O
sialic acid + ?
show the reaction diagram
-
-
-
-
?
ganglioside GM3 + H2O
sialic acid + ?
show the reaction diagram
additional information
?
-
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
ganglioside GD1a + H2O
ganglioside GM1 + sialic acid
show the reaction diagram
ganglioside GM3 + H2O
sialic acid + ?
show the reaction diagram
-
in transfected cells, mainly via cell-cell-interaction
-
-
?
additional information
?
-
-
the enzyme modifies the ganglioside pattern of adjacent cells, involved in cell-cell-interaction
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cathepsin A
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
quantification by RT-PCR
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
isoform Neu3 plays a key role in skeletal muscle differentiation by strictly modulating the ganglioside content of adjacent cells, with special regard to GM3
Manually annotated by BRENDA team
-
low expression of Neu-2
Manually annotated by BRENDA team
-
low expression of Neu-2
Manually annotated by BRENDA team
-
low amount of Neu-1
Manually annotated by BRENDA team
-
low expression of Neu-2
Manually annotated by BRENDA team
-
low expression of Neu-2
Manually annotated by BRENDA team
additional information
-
tissue distribution of the 3 isozymes, Neu-1 is ubiquitously expressed at higher level, except for skeletal muscle
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the absence of Neu1 results in the increased sialylation of the cell surface proteins, probably affecting multiple receptors for phagocytosis. Macrophages from the Neu1-deficient mice show increased sialylation and impaired phosphorylation of FcgammaRas well as markedly reduced phosphorylation of Syk kinase in response to treatment with immunoglobulin G-opsonized beads
physiological function
treatment of the cells with purified mouse Neu1 reduces surface sialylation and restores phagocytosis. Cell surface Neu1 activates the phagocytosis in macrophages and dendritic cells through desialylation of surface receptors, thus, contributing to their functional integrity
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NEUR1_MOUSE
409
0
44591
Swiss-Prot
Secretory Pathway (Reliability: 5)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminally HA-tagged enzyme, transient functional overexpression in COS-7 cells, location at the cell surface in the plasma membrane
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
in macrophages from isoform Neu1 deficient mice, a model for sialidosis, oversialylated lysosomal membrane protein Lamp-1 enhances lysosomal exocytosis. Silencing of Lamp-1 reverts this phenotype by interfering with the docking of lysosomes at the plasma membrane. In Neu1-/- mice the excessive exocytosis of serine proteases in the bone niche leads to inactivation of extracellular serpins, premature degradation of VCAM-1, and loss of bone marrow retention
medicine
-
isoform Neu3 plays a key role in skeletal muscle differentiation by strictly modulating the ganglioside content of adjacent cells, with special regard to GM3. Induced down-regulation of NEU3, even when partial, totally inhibits cell's capability to differentiate by increasing the GM3 level above a critical point, which causes epidermal growth factor receptor inhibition and ultimately its down-regulation and an higher responsiveness of myoblasts to the apoptotic stimuli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, P.; Zhang, J.; Bian, H.; Wu, P.; Kuvelkar, R.; Kung, T.T.; Crawley, Y.; Egan, R.W.; Billah, M.M.
Induction of lysosomal and plasma membrane-bound sialidases in human T-cells via T-cell receptor
Biochem. J.
380
425-433
2004
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Papini, N.; Anastasia, L.; Tringali, C.; Croci, G.; Bresciani, R.; Yamaguchi, K.; Miyagi, T.; Preti, A.; Prinetti, A.; Prioni, S.; Sonnino, S.; Tettamanti, G.; Venerando, B.; Monti, E.
The plasma membrane-associated sialidase MmNEU3 modifies the ganglioside pattern of adjacent cells supporting its involvement in cell-to-cell interactions
J. Biol. Chem.
279
16989-16995
2004
Mus musculus
Manually annotated by BRENDA team
Starcher, B.; dAzzo, A.; Keller, P.W.; Rao, G.K.; Nadarajah, D.; Hinek, A.
Neuraminidase-1 is required for the normal assembly of elastic fibers
Am. J. Physiol. Lung Cell Mol. Physiol.
295
L637-L647
2008
Mus musculus
Manually annotated by BRENDA team
Yogalingam, G.; Bonten, E.J.; van de Vlekkert, D.; Hu, H.; Moshiach, S.; Connell, S.A.; dAzzo, A.
Neuraminidase 1 is a negative regulator of lysosomal exocytosis
Dev. Cell
15
74-86
2008
Mus musculus (O35657), Homo sapiens (Q99519), Homo sapiens
Manually annotated by BRENDA team
Anastasia, L.; Papini, N.; Colazzo, F.; Palazzolo, G.; Tringali, C.; Dileo, L.; Piccoli, M.; Conforti, E.; Sitzia, C.; Monti, E.; Sampaolesi, M.; Tettamanti, G.; Venerando, B.
NEU3 sialidase strictly modulates GM3 levels in skeletal myoblasts C2C12 thus favoring their differentiation and protecting them from apoptosis
J. Biol. Chem.
283
36265-36271
2008
Mus musculus
Manually annotated by BRENDA team
Seyrantepe, V.; Iannello, A.; Liang, F.; Kanshin, E.; Jayanth, P.; Samarani, S.; Szewczuk, M.R.; Ahmad, A.; Pshezhetsky, A.V.
Regulation of phagocytosis in macrophages by neuraminidase 1
J. Biol. Chem.
285
206-215
2010
Mus musculus (O35657), Mus musculus
Manually annotated by BRENDA team