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Information on EC 3.2.1.129 - endo-alpha-sialidase and Organism(s) Escherichia phage K1F and UniProt Accession Q04830
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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 taxonomic range for the selected organisms is: Escherichia phage K1F
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
endoneuraminidase, endoneuraminidase-n, endo-n-acetylneuraminidase, endosialidase e, endosialidase nf, endont, endosialidasenf, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-2,8-sialosylhydrolase
-
-
-
-
endo-N-acetylneuraminidase
endoneuraminidase
endoNF
endosialidase
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY
91195-87-8
-
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
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
-
-
-
?
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
-
-
-
-
?
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
-
-
?
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
-
-
-
-
?
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)
-
?
polysialylated neural cell adhesion molecule + H2O
?
-
polysialic acid is an unbranched homopolymer of 100-300 alpha-2,8-linked silica acid residues
-
-
?
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
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
-
-
-
?
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
-
-
?
polysialylated neural cell adhesion molecule + H2O
?
-
polysialic acid is an unbranched homopolymer of 100-300 alpha-2,8-linked silica acid residues
-
-
?
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
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
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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
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)
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
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_BPK1F
1064
0
118905
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild type endoNF cocrystallized with oligomeric sialic acid and mutant enzymes H350A and R647A are crystallized by the hanging drop vapor diffusion method, using
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E581A
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
inactive, but no effect on expression, maturation or comlex formation
R647A
Q853A
-
binding site mutation, active within control range with soluble polysialic acid
R596A/R647A
-
control active site mutation without affecting maturation or binding, EC50: 1.9 nM polysialic acid
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
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
-
mutant deltaN-endoNF lacking the capsid binding domain, forms trimeric complexes
E581A
behaves like wild-type in terms of expression level, maturation by proteolytic cleavage and trimer formation
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
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme displays outstanding stability and resistance to SDS
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
-
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
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
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
J. Biol. Chem.
263
18269-18276
1988
Escherichia phage K1F
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
J. Biol. Chem.
262
3553-3561
1987
Escherichia phage K1F
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
1984
Escherichia phage K1F
Muhlenhoff, M.; Stummeyer, K.; Grove, M.; Sauerborn, M.; Gerardy-Schahn, R.
Proteolytic processing and oligomerization of bacteriophage-derived endosialidases
J. Biol. Chem.
278
12634-12644
2003
Escherichia phage K1F, Vectrevirus K1E
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
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
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
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
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
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
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
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
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
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
J. Mol. Biol.
397
341-351
2010
Escherichia phage K1F (Q04830)
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
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