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Information on EC 3.2.1.129 - endo-alpha-sialidase
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3.2.1.129 endo-alpha-sialidaseIUBMB Comments
Although the name endo-N-acetylneuraminidase has also been used for this enzyme, this is misleading since its activity is not restricted to acetylated substrates. An exo-alpha-sialidase activity is listed as EC 3.2.1.18 exo-alpha-sialidase. See also EC 4.2.2.15 anhydrosialidase.
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Word Map
- 3.2.1.129
-
polysialic
- ncam
-
polysialylated
-
psa-ncam
-
alpha-2,8-linked
-
polysias
-
bacteriophage-derived
-
psa-specific
- polysialyltransferase
-
colominic
-
neunac
- medicine
- biotechnology
- degradation
- molecular biology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
endoneuraminidase, endoneuraminidase-n, endo-n-acetylneuraminidase, endosialidase e, endosialidase nf, endont, endosialidasenf, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-2,8-sialosylhydrolase
-
-
-
-
endo-N
endo-N-acetylneuraminidase
endoE
endoneuraminidase
endoNF
endosialidase
endosialidase E
endosialidase NF
G102
-
-
-
-
neuraminidase, endo-
-
-
-
-
poly(alpha-2,8-sialoside) alpha-2,8-sialosylhydrolase
-
-
-
-
poly(alpha-2,8-sialosyl) endo-N-acetylneuraminidase
-
-
-
-
poly(sialoside) alpha-2,8-sialosylhydrolase
-
-
-
-
endo-N-acetylneuraminidase
-
-
-
-
endoneuraminidase
-
-
-
-
endoNF
-
proteolyitcally processed endosialidase lacking the N-terminal head-binding domain
endosialidase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sialyl-alpha(2-8)sialyl-alpha(2-8)sialyl-alpha(2-8)sialic acid + H2O = 2 sialyl-alpha(2-8)sialic acid
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
polysialoside (2->8)-alpha-sialosylhydrolase
Although the name endo-N-acetylneuraminidase has also been used for this enzyme, this is misleading since its activity is not restricted to acetylated substrates. An exo-alpha-sialidase activity is listed as EC 3.2.1.18 exo-alpha-sialidase. See also EC 4.2.2.15 anhydrosialidase.
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CAS REGISTRY NUMBER
COMMENTARY
91195-87-8
-
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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
alpha-2,8-linked polysialic acid + H2O
oligomers of polysialic acid
-
-
-
-
?
alpha-2,8-linked polysialic acid cross-linked by diepoxyoctane + H2O
oligomers of polysialic acid
-
polysialic acid hydrogel consisting of 20% (w/v) polysialic acid and a minimum of 0.6 equivalents diepoxyoctane, pH 7.4, 37°C
-
-
?
alpha-2,8-linked sialic acid residues cross-linked by diepoxyoctane + H2O
?
-
hydrogel with minimum chain length of 8
-
-
?
longchain alpha 2,8-linked polysialic acid + H2O
oligomers of alpha 2,8-linked polysialic acid
-
minimum substrate is tetrameric polysialic acid, processive enzyme activity on oligomers larger than that, confirmation by H NMR spectroscopy and anion-exchange chromatography
major product is an oligomer consisting of 3 monomers in wild-type and cleavage mutant S911A, in binding site mutant R837A/S848A more random oligomers are produced
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
polysialic acid capsules of bacteria + H2O
oligomers of alpha 2,8-linked polysialic acid
-
minimum substrate is tetrameric polysialic acid, processive enzyme activity on oligomers larger than that, confirmation by H NMR spectroscopy and anion-exchange chromatography
-
-
?
trifluoromethylumbelliferyl sialotetraoside + H2O
trifluoromethylumbelliferone + sialotetraoside
-
-
-
-
?
trifluoromethylumbelliferyl sialotrioside + H2O
trifluoromethylumbelliferone + sialotrioside
-
-
-
-
?
alpha-2,8-linked polysialic acid + H2O
?
-
specifically cleaves alpha 2,8-linked sialic acid residues with minimum chain length of 8, no effect on other sialic acid containing structures
-
-
?
poly(sialic) acid + H2O
?
-
all sialic acid residues (Sia1-5) are bound by endoNF
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
bacteriophage phi1.2
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
bacteriophage PK1A
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
bacteriophage PK1A
-
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
bacteriophage PK1A
-
brain glycoproteins
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
bacteriophage PK1A
-
enzyme requires the simultaneous presence adjacent to the site of cleavage a minimum of 3 sialic acid residues on the distal side and a minimum of 5 sialic acid residues on the proximal side
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
bacteriophage PK1E
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
bacteriophage PK1E
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
-
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
-
polysialic acid capsule isolated from Escherichia coli N67 or Escherichia coli K1
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
-
the minimum requirement for cleavage is alpha-2,8-(NeuAc)5
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
-
bacterial and neural membrane glycoconjugates
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
-
oligosialic acid from Escherichia coli K1
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
-
brain glycoproteins
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
-
catalyzes the hydrolysis of both alpha-2,8-linked poly(N-acetyl-D-neuraminic acid) and poly(N-glycoloyl-D-neuraminic acid)
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
-
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
-
no release of alpha-2,3-, alpha-2,6-, or alpha-2,9-linked sialic residues from a variety of other substrates
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
-
limited hydrolysis of the Escherichia coli K92 antigen, an N-acetylneuraminic acid homopolymer containing alternating alpha-2,8-, and alpha-2,9-linkages
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
-
rapid hydrolysis of both the O-acetylated and non-O-acetylted forms of the K1 antigen, an alpha-2,8-linked homopolymer of N-acetylneuraminic acid, and of Meningococcus B antigen
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
Vectrevirus K1E
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
Vectrevirus K1E
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
Vectrevirus K1E
-
-
-
?
polysialylated neural cell adhesion molecule + H2O
?
-
polysialic acid is an unbranched homopolymer of 100-300 alpha-2,8-linked silica acid residues
-
-
?
additional information
?
-
the endosialidase is a bifunctional enzyme with high activity against alpha-2,8- and low activity against alpha-2,9-linkages in a polySia chain
-
-
?
additional information
?
-
-
the endo-sialidase requires the occupation of a minimum of three subsites by sialic acid for efficient catalysis, so neither monomer (trifluoromethylumbelliferyl sialoside) nor dimer (trifluoromethylumbelliferyl sialobioside) are hydrolyzed by endoNF
-
-
?
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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
alpha-2,8-linked polysialic acid + H2O
oligomers of polysialic acid
-
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
polysialic acid capsules of bacteria + H2O
oligomers of alpha 2,8-linked polysialic acid
-
minimum substrate is tetrameric polysialic acid, processive enzyme activity on oligomers larger than that, confirmation by H NMR spectroscopy and anion-exchange chromatography
-
-
?
alpha-2,8-linked polysialic acid + H2O
?
-
specifically cleaves alpha 2,8-linked sialic acid residues with minimum chain length of 8, no effect on other sialic acid containing structures
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
bacteriophage phi1.2
-
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
bacteriophage PK1A
-
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
bacteriophage PK1E
-
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
-
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
-
-
-
-
?
poly(sialic) acids or oligo(sialic) acids containing alpha-2,8-linked N-acetylneuraminic acid + H2O
fragments of poly(sialic) acid or oligo(sialic) acids
Vectrevirus K1E
-
-
-
-
?
polysialylated neural cell adhesion molecule + H2O
?
-
polysialic acid is an unbranched homopolymer of 100-300 alpha-2,8-linked silica acid residues
-
-
?
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Unique alpha 2, 8-polysialylated glycoproteins in breast cancer and leukemia cells.
Dehydration
Cell surface expression of polysialic acid on NCAM is a prerequisite for activity-dependent morphological neuronal and glial plasticity.
Fasciculation
Analysis of high PSA N-CAM expression during mammalian spinal cord and peripheral nervous system development.
Fasciculation
Polysialic acid as a regulator of intramuscular nerve branching during embryonic development.
Infections
Administration of Capsule-Selective Endosialidase E Minimises Up-Regulation of Organ Gene Expression Induced by Experimental Systemic Infection with Escherichia coli K1.
Infections
Treatment of experimental Escherichia coli infection with recombinant bacteriophage-derived capsule depolymerase.
Leukemia
Unique alpha 2, 8-polysialylated glycoproteins in breast cancer and leukemia cells.
Neoplasm Metastasis
A nude mice model of human rhabdomyosarcoma lung metastases for evaluating the role of polysialic acids in the metastatic process.
Neoplasms
A nude mice model of human rhabdomyosarcoma lung metastases for evaluating the role of polysialic acids in the metastatic process.
Neoplasms
Polysialic acid of the neural cell adhesion molecule distinguishes small cell lung carcinoma from carcinoids.
Neoplasms
Polysialylated neural cell adhesion molecules expressed in human pituitary tumors and related to extrasellar invasion.
Seizures
PSA-NCAM-dependent GDNF signaling limits neurodegeneration and epileptogenesis in temporal lobe epilepsy.
Seizures
Targeting epileptogenesis-associated induction of neurogenesis by enzymatic depolysialylation of NCAM counteracts spatial learning dysfunction but fails to impact epilepsy development.
Sleep Deprivation
Role of polysialylated neural cell adhesion molecule in rapid eye movement sleep regulation in rats.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.85
tetrameric silica acid
-
identical kinetic parameters for wild type and cleavage site mutant S911A
7.41
K1 antigen
-
37°C, pH 6.5, an alpha-2,8-linked homopolymer of N-acetylneuraminic acid
-
1.2
oligo(sialic) acid
-
pH 7.5, isolated from Escherichia coli K1, phage-bound enzyme
-
1.6
oligo(sialic) acid
-
pH 7.5, from Escherichia coli K1, soluble enzyme
-
0.0066
polysialic acid
-
pH 7.5, capsule isolated from Escherichia coli N67, soluble enzyme
0.051
polysialic acid
-
pH 7.5, capsule isolated from Escherichia coli K1, soluble enzyme
0.071
polysialic acid
-
pH 7.5, capsule isolated from Escherichia coli K1, phage-bound enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.37
tetrameric silica acid
-
identical kinetic parameters for wild type and cleavage site mutant S911A
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
intravitreal endo-N injection and axotomy of optical nerve in wild-type mice: 4 days after treatment no difference in retinal ganglion cell density compared with untreated/uninjured, and vehicle treated/axotomy controls, at day 7 50% reduced density in vehicle treated/axotomy group compared to untreated/uninjured group, an additional 27% density reduction in endo-N treatment group
additional information
-
intravitreal vehicle injection and axotomy of optical nerve in NCAM-/-mice: 4 days after treatment reduced density in vehicle injection/axotomy group compared to untreated/uninjured group, no neuroprotective effect of injection
additional information
-
no differences in retinal ganglion cell densities after 14 days in NCAM-/-mice with or without endo-N treatment, shows non-toxicity of endo-N treatment itself
additional information
-
polysialic acid is degraded from inner retina in vivo within 6 hours by intravitreal injection of 1 microl (6.7 U/microl) endo-N in 50% phosphate buffered saline with glycerol, from the outer retina within 24 hours, and remains absent at day 14l
additional information
-
polysialic acid is degraded in vitro (neonatal cell culture) within 1 day by 1 microl and 3 microl endo-N, not by 0.5 microl (6.7 U/microl) in 50% phosphate buffered saline with glycerol
additional information
-
polysialylated neural cell adhesion molecules are degraded in vitro (neonatal cell culture) within 12 hours after treatment with 1 microl (6.7 U/microl) in 50% phosphate buffered saline with glycerol, and remains absent 5 days after treatment, fewer retinal ganglion cells (54%) than control or vehicle control (96%)
additional information
-
treatment with 1 microl (6.7 U/microl) in 50% phosphate buffered saline with glycerol, no significant difference in retinal ganglion cell densities 7 days after treatment, at day 14 reduction by approximately one third compared with control and vehicle control
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bacteriophage PK1A
bacteriophage PK1E
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
density of mouse retinal ganglion cells after removal of polysialic acid by endo-N treatment to investigate possible toxic effects of endo-N treatment
brenda
additional information
-
neonatal rat Schwann cell culture (1-3 days postnatal), adult rat Schwann cell culture from 3 months old females, neural stem cells of fetal rat cell culture (gestational day 12), dorsal ganglionic cells of neonatal rat cell culture (2-3 days postnatal)
brenda
additional information
-
retinal ganglion cell cultures prepared from Long-Evans rat litters at postnatal day 7-8, and from 10-15 weeks old rats, for in vitro experiments
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
recombinant capsule depolymerase, endosialidase E, selectively removes polysialic acid from the bacterial surface
physiological function
Zindervirus SP6
-
the enzyme allows bacteriophage SP6 to infect Escherichia coli strain K1
physiological function
-
the enzyme inhibits the migration and enhances the differentiation of neural progenitor cells. Interruption of neuroblast chain pathway with the enzyme facilitates ectopic migration of subventricular zone-derived neural progenitor cells into the lesioned striatum, and migrated neural progenitor cells can differentiate into neurons and astrocytes
physiological function
-
recombinant capsule depolymerase, endosialidase E, selectively removes polysialic acid from the bacterial surface
-
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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). FIBER_BPK1E
Escherichia phage K1E
811
0
90524
Swiss-Prot
other Location (Reliability: 5)
FIBER_BPK1F
1064
0
118905
Swiss-Prot
other Location (Reliability: 3)
A4UUQ0_9VIRU
811
0
90352
TrEMBL
other Location (Reliability: 5)
A0A085GBQ4_9GAMM
794
0
83793
TrEMBL
-
A0A499PTF8_9CAUD
674
0
70303
TrEMBL
Mitochondrion (Reliability: 5)
B7MGW6_ECO45
Escherichia coli O45:K1 (strain S88 / ExPEC)
981
0
109485
TrEMBL
-
A5VW57_9CAUD
981
0
109378
TrEMBL
other Location (Reliability: 3)
A0A499Q6R7_9CAUD
762
0
81759
TrEMBL
other Location (Reliability: 2)
A0A220NTZ3_9CAUD
599
0
65839
TrEMBL
other Location (Reliability: 2)
Q2WC58_BPK1E
Escherichia phage K1E
811
0
90638
TrEMBL
other Location (Reliability: 5)
A0A0H3MN25_ECO7I
Escherichia coli O7:K1 (strain IAI39 / ExPEC)
200
0
22694
TrEMBL
-
A0A7L8YT42_9CAUD
951
0
103611
TrEMBL
other Location (Reliability: 3)
A0A3S7N8M5_9CAUD
832
0
91317
TrEMBL
other Location (Reliability: 2)
A0A7I8JV07_9CAUD
688
0
73443
TrEMBL
other Location (Reliability: 2)
A0A2H4N093_9CAUD
811
0
90280
TrEMBL
other Location (Reliability: 5)
A0A0H3MN12_ECO7I
Escherichia coli O7:K1 (strain IAI39 / ExPEC)
1039
0
115734
TrEMBL
-
A0A7I8JW71_9CAUD
674
0
70323
TrEMBL
Mitochondrion (Reliability: 4)
A0A2P1MXB7_9CAUD
848
0
92542
TrEMBL
other Location (Reliability: 1)
A0A085APX7_9ENTR
690
0
72756
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
208000
-
enzyme complex, SDS-PAGE, solubilized in SDS-mercaptoethanol-containing sample buffer at 37°C
74000
76000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotrimer
trimer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
proteolysis of the C-terminal domain that functions as an intramolecular chaperone and is released during enzyme maturation of wild-type enzyme
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with a dimer of alpha-2,9-linked sialic acid, hanging drop vapor diffusion method, using 6% (w/v) PEG3350, 70 mM CHES buffer, pH 9.5 and 70 mM SrCl2
crystal structure of the catalytic domain of endoN from caliphate K1F reveals a functional trimer, folding is mediated by an intramolecular C-terminal chaperone domain
-
hanging drop vapor diffusion method, using 16% (w/v) PEG 8000, 0.1 M Tris-HCl pH 7.2, 3% (v/v) 2-propanol
-
wild type endoNF cocrystallized with oligomeric sialic acid and mutant enzymes H350A and R647A are crystallized by the hanging drop vapor diffusion method, using
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R596A
-
exhibits a more than 95% decreased activity compared to wild-type endoNF, but binds polysialic acid
D489N
back-mutations, partial reduction of enzymic activity. Single amino acid substitution do not inactivate the catalytic activity totally
Y417H
back-mutations, partial reduction of enzymic activity. Single amino acid substitution do not inactivate the catalytic activity totally
E581A
K410A
Q853A
-
binding site mutation, active within control range with soluble polysialic acid
R547A/E581A
inactive, but no effect on expression, maturation or comlex formation
R596A
behaves like wild-type in terms of expression level, maturation by proteolytic cleavage and trimer formation
R596A/E581A
inactive, but no effect on expression, maturation or comlex formation
R596A/R647A
R596A/R647A/Q853A
-
active site mutation plus binding site mutation, EC50: 5.0 nM surface bound polysialic acid
R596A/R647A/R837A
-
active site mutation plus binding site mutation, 5-fold increased EC50: 11 nM polysialic acid
R596A/R647A/R837A/S848A
-
active site mutation plus binding site mutation, EC50: 30 nM surface bound polysialic acid, increased EC50: 30 nM polysialic acid
R596A/R647A/S848A
-
active site mutation plus binding site mutation, only binding site mutant with SDS resistance which is a criterion for kinetic stabilization of the enzyme, EC50: 4.1 nM surface bound polysialic acid
R596A/R647A/S848A/Q853A
-
active site mutation plus binding site mutation, increased EC50: 6.2 nM polysialic acid
R596A/R647A/S911A
-
active site mutation plus cleavage site mutation, tremendously increased EC50: 360 nM polysialic acid
R647A
R837A
-
binding site mutation, increased molar activity with soluble polysialic acid
R837A/S848A
-
binding site mutation, increased molar activity with soluble polysialic acid
S848A
-
binding site mutation, active within control range with soluble polysialic acid
S848A/Q853A
-
binding site mutation, active within control range with soluble polysialic acid
S911A
additional information
E581A
behaves like wild-type in terms of expression level, maturation by proteolytic cleavage and trimer formation
R596A/R647A
inactive, but no effect on expression, maturation or comlex formation
R596A/R647A
-
control active site mutation without affecting maturation or binding, EC50: 1.9 nM polysialic acid
R647A
behaves like wild-type in terms of expression level, maturation by proteolytic cleavage and trimer formation
S911A
-
mutant deltaN-endoNF lacking the capsid binding domain but retaining the C-terminal domain, prevents cleavage but not assembly into active trimers
S911A
-
cleavage site mutation: prevents proteolysis of the C-terminal domain that functions as an intramolecular chaperone and is normally released during enzyme maturation. Substrate binding is reduced similarly to binding site mutations. Altered activities: 3times higher activity with soluble polycialic acid as substrate, 190fold reduced activity with immobilized polysialic acid as substrate, no difference in activity with minimal substrate tetrameric sialic acid
additional information
N-terminal deletion mutants are catalytically active, whereas all C-terminally truncated mutants are inactive
additional information
-
mutant deltaN-endoNF lacking the capsid binding domain, forms trimeric complexes
additional information
Vectrevirus K1E
-
point mutation located on or near the putative active site, exhibits greatly reduced activity
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme displays outstanding stability and resistance to SDS
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by gel filtration, affinity chromatography and a Ni2+-chelating column
-
description in Schwarzer, D. et al. (2007) J.Biol. Chem. 282, 2821-2831
-
HiTrap Q HP anion exchange column chromatography and Superdex 200 gel filtration
recombinant enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
mutant proteins harbouring single amino acid substitutions expressed as GFP-fusion proteins
protein expression in Escherichia coli BL21-Gold(DE3) in the presence of 100 microgram/ml Carbenicillin, 30°C
-
subcloned into the NdeI and XhoI restriction sites of pET22b, resulting in a construct encoding the C-terminal domain of endoNF with a C-terminal His6 tag, expressed in Escherichia coli BL21-Gold(DE3)
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
degradation
medicine
molecular biology
-
removal of target molecules to investigate their function
additional information
biotechnology
-
degradation of non-toxic modified polysialic acid hydrogel scaffold in neuro-regenerative tissue engineering (4.26 microgram enzyme + 39 mg hydrogel), in phosphate buffered saline (400 microl, pH 7.4), at 37°C, degradation speed 2-11 days depending on cross-linker amount (0.6, 0.8, 2 equivalents diepoxyoctane, no activity with 3 equivalents diepoxyoctane), hydrogel was coated with collagen I, poly-L-lysine/collagen I, or diluted matrigel for neurite formation in PC12 cells
biotechnology
-
degradation of non-toxic modified polysialic acid hydrogel scaffold in neuro-regenerative tissue engineering: no degradation in 12 days with 1 microg/ml active enzyme + 105 cubic mm hydrogel in phosphate buffered saline (pH 7.4), at room temperature, increase to 4 microg/ml at end of week 2 initiates degradation, total degradation after 4 weeks, hydrogel was coated with poly-L-lysine, poly-L-ornithine-laminin or collagen for neurite formation in neonatal and adult rat Schwann cells, neural rat stem cells, and dorsal root ganglionic cells from rats
degradation
-
degradation of non-toxic modified polysialic acid hydrogel scaffold in neuro-regenerative tissue engineering (4.26 microgram enzyme + 39 mg hydrogel), in phosphate buffered saline (400 microl, pH 7.4), at 37°C, degradation speed 2-11 days depending on cross-linker amount (0.6, 0.8, 2 equivalents diepoxyoctane, no activity with 3 equivalents diepoxyoctane), hydrogel was coated with collagen I, poly-L-lysine/collagen I, or diluted matrigel for neurite formation in PC12 cells
degradation
-
degradation of non-toxic modified polysialic acid hydrogel scaffold in neuro-regenerative tissue engineering: no degradation in 12 days with 1 microg/ml active enzyme + 105 cubic mm hydrogel in phosphate buffered saline (pH 7.4), at room temperature, increase to 4 microg/ml at end of week 2 initiates degradation, total degradation after 4 weeks, hydrogel was coated with poly-L-lysine, poly-L-ornithine-laminin or collagen for neurite formation in neonatal and adult rat Schwann cells, neural rat stem cells, and dorsal root ganglionic cells from rats
medicine
-
degradation of non-toxic modified polysialic acid hydrogel scaffold in neuro-regenerative tissue engineering (4.26 microgram enzyme + 39 mg hydrogel), in phosphate buffered saline (400 microl, pH 7.4), at 37°C, degradation speed 2-11 days depending on cross-linker amount (0.6, 0.8, 2 equivalents diepoxyoctane, no activity with 3 equivalents diepoxyoctane), hydrogel was coated with collagen I, poly-L-lysine/collagen I, or diluted matrigel for neurite formation in PC12 cells
medicine
-
degradation of non-toxic modified polysialic acid hydrogel scaffold in neuro-regenerative tissue engineering: no degradation in 12 days with 1 microg/ml active enzyme + 105 cubic mm hydrogel in phosphate buffered saline (pH 7.4), at room temperature, increase to 4 microg/ml at end of week 2 initiates degradation, total degradation after 4 weeks, hydrogel was coated with poly-L-lysine, poly-L-ornithine-laminin or collagen for neurite formation in neonatal and adult rat Schwann cells, neural rat stem cells, and dorsal root ganglionic cells from rats
medicine
-
investigation of possible role of polysialic neural cell adhesion molecules in the pathophysiology of epilepsy
medicine
-
a noncatalytic enzyme is used for detecting small-cell lung cancer circulating tumor cells
medicine
O04830
the enzyme recognizes polysialic acid, an oncofetal antigen characteristic for high malignant tumors of neuroendocrine origin
additional information
-
the C-terminal domain plays a crucial role in folding and assembling not only the C-terminal domain of endosialidases but also of other, unrelated phage proteins
additional information
-
almost complete removal of polysialic acid by endo-N injection into the brain 5 days after stimulation (return to normal polysialic acid levels after 11 weeks): no effect on proliferation, neurogenesis, and the fate of newborn cells in the hippocampus of rats without status epileptics. Increase of newborn cells in status epileptics rats compared to controls without significant difference between endo-N and vehicle treatment. However, endo-N treatment reduces the total number of newborn neurons (64%) upon induction of the status epileptics compared to vehicle treatment. No endo-N effect on hilar basal dendrite generation compared to vehicle control. No effect on doublecortin-expressing neuronal progenitor cells, and no effect on subpopulation of these cells with persistent basal dendrites compared to vehicle control. No difference in number, severity and duration of seizures between groups. Spatial learning deficit of status epilepticus mice is reduced by end-N treatment compared to vehicle control
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kitajima, K.; Inoue, S.; Inoue, Y.; Troy, F.A.
Use of a bacteriophage-derived endo-N-acetylneuraminidase and an equine antipolysialyl antibody to characterize the polysialyl residues in salmonid fish egg polysialoglycoproteins. Substrate and immunospecificity studies
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1988
Escherichia phage K1F
brenda
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Common cleavage pattern of polysialic acid by bacteriophage endosialidases of different properties and origins
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63
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bacteriophage PK1A, bacteriophage PK1E
brenda
Kwiatowski, B.; Boschek, B.; Thiele, H.; Stirm, S.
endo-N-Acetylneuraminidase associated with bacteriophage particles
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43
697-704
1982
bacteriophage phi1.2
brenda
Finne, J.; Mkel, P.H.
Cleavage of the polysialosyl units of brain glycoproteins by a bacteriophage endosialidase. Involvement of a long oligosaccharide segment in molecular interactions of polysialic acid
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260
1265-1270
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bacteriophage PK1A
brenda
Tomlinson, S.; Taylor, P.W.
Neuraminidase associated with coliphage E that specifically depolymerizes the Escherichia coli K1 capsular polysaccharide
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55
374-378
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Phage E
brenda
Hallenbeck, P.C.; Vimr, E.R.; Yu, F.; Bassler, B.; Troy, F.A.
Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-alpha-2,8-sialosyl carbohydrate units
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262
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Escherichia phage K1F
brenda
Vimr, E.R.; McCoy, R.D.; Vollger, H.F.; Wilkinson, N.C.; Troy, F.A.
Use of prokaryotic-derived probes to identify poly(sialic acid) in neonatal neuronal membranes
Proc. Natl. Acad. Sci. USA
81
1971-1975
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Escherichia phage K1F
brenda
Muhlenhoff, M.; Stummeyer, K.; Grove, M.; Sauerborn, M.; Gerardy-Schahn, R.
Proteolytic processing and oligomerization of bacteriophage-derived endosialidases
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278
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Escherichia phage K1F, Vectrevirus K1E
brenda
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Complete nucleotide sequence of the gene encoding bacteriophage E endosialidase: implications for K1E endosialidase structure and function
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309
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Vectrevirus K1E
brenda
Leggate, D.R.; Bryant, J.M.; Redpath, M.B.; Head, D.; Taylor, P.W.; Luzio, J.P.
Expression, mutagenesis and kinetic analysis of recombinant K1E endosialidase to define the site of proteolytic processing and requirements for catalysis
Mol. Microbiol.
44
749-760
2002
Vectrevirus K1E
brenda
Gerardy-Schahn, R.; Bethe, A.; Brennecke, T.; Muhlenhoff, M.; Eckhardt, M.; Ziesing, S.; Lottspeich, F.; Frosch, M.
Molecular cloning and functional expression of bacteriophage PK1E-encoded endoneuraminidase Endo NE
Mol. Microbiol.
16
441-450
1995
bacteriophage PK1E
brenda
Stummeyer, K.; Dickmanns, A.; Mhlenhoff, M.; Gerardy-Schahn, R.; Ficner, R.
Crystal structure of the polysialic acid-degrading endosialidase of bacteriophage K1F
Nat. Struct. Mol. Biol.
12
90-96
2005
Escherichia phage K1F (Q04830), Escherichia phage K1F
brenda
Jakobsson, E.; Jokilammi, A.; Aalto, J.; Ollikka, P.; Lehtonen, J.V.; Hirvonen, H.; Finne, J.
Identification of amino acid residues at the active site of endosialidase that dissociate the polysialic acid binding and cleaving activities in Escherichia coli K1 bacteriophages
Biochem. J.
405
465-472
2007
Vectrevirus K1E, Enterobacteria phage K1A (A4UUQ0)
brenda
Haselhorst, T.; Stummeyer, K.; Muhlenhoff, M.; Schaper, W.; Gerardy-Schahn, R.; von Itzstein, M.
Endosialidase NF appears to bind polySia DP5 in a helical conformation
Chembiochem
7
1875-1877
2006
Bacteriophage sp.
brenda
Schwarzer, D.; Stummeyer, K.; Gerardy-Schahn, R.; Muehlenhoff, M.
Characterization of a Novel Intramolecular Chaperone Domain Conserved in Endosialidases and Other Bacteriophage Tail Spike and Fiber Proteins
J. Biol. Chem.
282
2821-2831
2007
Escherichia phage K1F
brenda
Berski, S.; van Bergeijk, J.; Schwarzer, D.; Stark, Y.; Kasper, C.; Scheper, T.; Grothe, C.; Gerardy-Schahn, R.; Kirschning, A.; Draeger, G.
Synthesis and biological evaluation of a polysialic acid-based hydrogel as enzymatically degradable scaffold material for tissue engineering
Biomacromolecules
9
2353-2359
2008
Escherichia phage K1F
brenda
Haile, Y.; Berski, S.; Draeger, G.; Nobre, A.; Stummeyer, K.; Gerardy-Schahn, R.; Grothe, C.
The effect of modified polysialic acid based hydrogels on the adhesion and viability of primary neurons and glial cells
Biomaterials
29
1880-1891
2008
Escherichia phage K1F
brenda
Murphy, J.A.; Hartwick, A.T.; Rutishauser, U.; Clarke, D.B.
Endogenous polysialylated neural cell adhesion molecule enhances the survival of retinal ganglion cells
Invest. Ophthalmol. Vis. Sci.
50
861-869
2009
Escherichia phage K1F
brenda
Schwarzer, D.; Stummeyer, K.; Haselhorst, T.; Freiberger, F.; Rode, B.; Grove, M.; Scheper, T.; von Itzstein, M.; Muehlenhoff, M.; Gerardy-Schahn, R.
Proteolytic release of the intramolecular chaperone domain confers processivity to endosialidase f
J. Biol. Chem.
284
9465-9474
2009
Escherichia phage K1F
brenda
Pekcec, A.; Fuest, C.; Muehlenhoff, M.; Gerardy-Schahn, R.; Potschka, H.
Targeting epileptogenesis-associated induction of neurogenesis by enzymatic depolysialylation of NCAM counteracts spatial learning dysfunction but fails to impact epilepsy development
J. Neurochem.
105
389-400
2008
Escherichia phage K1F
brenda
Schulz, E.C.; Neumann, P.; Gerardy-Schahn, R.; Sheldrick, G.M.; Ficner,R.
Structure analysis of endosialidase NF at 0.98 A resolution
Acta Crystallogr. Sect. D
66
176-180
2010
Escherichia phage K1F
brenda
Morley, T.J.; Willis, L.M.; Whitfield, C.; Wakarchuk, W.W.; Withers, S.G.
A new sialidase mechanism: bacteriophage K1F endo-sialidase is an inverting glycosidase
J. Biol. Chem.
284
17404-17410
2009
Escherichia phage K1F
brenda
Schulz, E.C.; Schwarzer, D.; Frank, M.; Stummeyer, K.; Muehlenhoff, M.; Dickmanns, A.; Gerardy-Schahn, R.; Ficner, R.
Structural basis for the recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein endoNF
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397
341-351
2010
Escherichia phage K1F (Q04830)
brenda
Zelmer, A.; Martin, M.J.; Gundogdu, O.; Birchenough, G.; Lever, R.; Wren, B.W.; Luzio, J.P.; Taylor, P.W.
Administration of capsule-selective endosialidase E minimizes upregulation of organ gene expression induced by experimental systemic infection with Escherichia coli K1
Microbiology
156
2205-2215
2010
Escherichia coli, Escherichia coli A192PP
brenda
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Molecular characterization, structural analysis and determination of host range of a novel bacteriophage LSB-1
Virol. J.
7
255
2010
Phage LSB-1
brenda
Schwarzer, D.; Browning, C.; Stummeyer, K.; Oberbeck, A.; Muehlenhoff, M.; Gerardy-Schahn, R.; Leiman, P.G.
Structure and biochemical characterization of bacteriophage phi92 endosialidase
Virology
477
133-143
2015
Enterobacteria phage phi92 (I7HXG2)
brenda
Hsu, H.J.; Palka-Hamblin, H.; Bhide, G.P.; Myung, J.H.; Cheong, M.; Colley, K.J.; Hong, S.
Noncatalytic endosialidase enables surface capture of small-cell lung cancer cells utilizing strong dendrimer-mediated enzyme-glycoprotein interactions
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90
3670-3675
2018
Homo sapiens
brenda
Martin, N.T.; Wrede, C.; Niemann, J.; Brooks, J.; Schwarzer, D.; Kuehnel, F.; Gerardy-Schahn, R.
Targeting polysialic acid-abundant cancers using oncolytic adenoviruses with fibers fused to active bacteriophage borne endosialidase
Biomaterials
158
86-94
2018
Escherichia phage K1F (O04830), Escherichia phage K1F
brenda
Li, C.; Zhang, Y.X.; Yang, C.; Hao, F.; Chen, S.S.; Hao, Q.; Lu, T.; Qu, T.Y.; Zhao, L.R.; Duan, W.M.
Intraventricular administration of endoneuraminidase-N facilitates ectopic migration of subventricular zone-derived neural progenitor cells into 6-OHDA lesioned striatum of mice
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277
139-149
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Mus musculus
brenda
Gebhart, D.; Williams, S.R.; Scholl, D.
Bacteriophage SP6 encodes a second tailspike protein that recognizes Salmonella enterica serogroups C2 and C3
Virology
507
263-266
2017
Zindervirus SP6
brenda
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