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alpha-2,8-glycosidically linked sialic acid + H2O
?
37°C
-
-
?
alpha-2,8-linked polysialic acid + H2O
?
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
-
-
?
capsular polysaccharides + H2O
?
-
-
-
?
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
-
?
oligo(sialic) acid + H2O
fragments of oligo(sialic) acid
-
-
-
-
?
poly(sialic) acid + H2O
?
poly(sialic) acid + H2O
fragments of poly(sialic) 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
-
-
?
polysialylated neural cell adhesion molecule + H2O
?
tetrameric silica acid + H2O
?
-
-
-
-
?
trifluoromethylumbelliferyl sialotetraoside + H2O
trifluoromethylumbelliferone + sialotetraoside
-
-
-
-
?
trifluoromethylumbelliferyl sialotrioside + H2O
trifluoromethylumbelliferone + sialotrioside
-
-
-
-
?
additional information
?
-
alpha-2,8-linked polysialic acid + H2O
?
-
-
-
-
?
alpha-2,8-linked polysialic acid + H2O
?
O04830
-
-
-
?
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
-
-
?
alpha-2,8-linked polysialic acid + H2O
?
-
-
-
-
?
K1 antigen
?
-
-
-
-
?
K1 antigen
?
Vectrevirus K1E
-
-
-
-
?
poly(sialic) acid + H2O
?
-
all sialic acid residues (Sia1-5) are bound by endoNF
-
-
?
poly(sialic) acid + H2O
?
-
-
-
?
poly(sialic) acid + H2O
?
-
-
-
-
?
poly(sialic) acid + H2O
?
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
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
?
-
-
-
-
?
polysialylated neural cell adhesion molecule + H2O
?
-
polysialic acid is an unbranched homopolymer of 100-300 alpha-2,8-linked silica acid residues
-
-
?
polysialylated neural cell adhesion molecule + H2O
?
-
-
-
-
?
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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alpha-2,8-linked polysialic acid + H2O
?
alpha-2,8-linked polysialic acid + H2O
oligomers of polysialic acid
-
-
-
-
?
capsular polysaccharides + H2O
?
-
-
-
?
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
-
-
?
polysialylated neural cell adhesion molecule + H2O
?
alpha-2,8-linked polysialic acid + H2O
?
O04830
-
-
-
?
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
-
-
?
alpha-2,8-linked polysialic acid + H2O
?
-
-
-
-
?
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
?
-
-
-
-
?
polysialylated neural cell adhesion molecule + H2O
?
-
polysialic acid is an unbranched homopolymer of 100-300 alpha-2,8-linked silica acid residues
-
-
?
polysialylated neural cell adhesion molecule + H2O
?
-
-
-
-
?
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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
H332N/N489D
complete inactivation
H417Y/N489D
complete inactivation
R614G
displays full endosialidase activity
Y417H
back-mutations, partial reduction of enzymic activity. Single amino acid substitution do not inactivate the catalytic activity totally
G956A
-
completely loses enzymatic activity
H350A
1.2% relative activity compared to the wild type enzyme
H350N
3.4% relative activity compared to the wild type enzyme
H350Q
4.4% relative activity compared to the wild type enzyme
H542A
36% relative activity compared to the wild type enzyme
H954A
-
completely loses enzymatic activity
N912A
-
completely loses enzymatic activity
Q853A
-
binding site mutation, active within control range with soluble polysialic acid
R1035A
-
completely loses enzymatic activity
R547A/E581A
inactive, but no effect on expression, maturation or comlex formation
R549A
0.6% relative activity compared to the wild type enzyme
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/R647
O04830
inactive
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/Q853A
-
binding site mutation, insoluble enzyme
R837A/S848A
-
binding site mutation, increased molar activity with soluble polysialic acid
R837A/S848A/Q853A
-
binding site mutation, insoluble enzyme
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
W328R
6.0% relative activity compared to the wild type enzyme
D138A
Vectrevirus K1E
-
lower Km than wild-type enzyme
D154A
Vectrevirus K1E
-
lower Km than wild-type enzyme
DELTA DI
Vectrevirus K1E
-
insoluble enzyme
DELTA DII
Vectrevirus K1E
-
insoluble enzyme
DELTA P-loop
Vectrevirus K1E
-
higher Km than wild-type enzyme
G153A
Vectrevirus K1E
-
less turnover than wild-type enzyme
R614G
Vectrevirus K1E
-
displays full endosialidase activity
Trunc N45
Vectrevirus K1E
-
lower Km than wild-type enzyme
W159A
Vectrevirus K1E
-
insoluble enzyme
E581A
behaves like wild-type in terms of expression level, maturation by proteolytic cleavage and trimer formation
E581A
1.8% relative activity compared to the wild type enzyme
E581A
-
the mutation results in complete loss of sialidase activity
K410A
20% relative activity compared to the wild type enzyme
K410A
O04830
partially active mutant
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
R647A
0.17% relative activity compared to the wild type enzyme
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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molecular biology
-
removal of target molecules to investigate their function
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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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
brenda
Pelkonen, S.; Pelkonen, J.; Finne, J.
Common cleavage pattern of polysialic acid by bacteriophage endosialidases of different properties and origins
J. Virol.
63
4409-4416
1989
bacteriophage PK1A, bacteriophage PK1E
brenda
Kwiatowski, B.; Boschek, B.; Thiele, H.; Stirm, S.
endo-N-Acetylneuraminidase associated with bacteriophage particles
J. Virol.
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
J. Biol. Chem.
260
1265-1270
1985
bacteriophage PK1A
brenda
Tomlinson, S.; Taylor, P.W.
Neuraminidase associated with coliphage E that specifically depolymerizes the Escherichia coli K1 capsular polysaccharide
J. Virol.
55
374-378
1985
Phage E
brenda
Hallenbeck, P.C.; Vimr, E.R.; Yu, F.; Bassler, B.; Troy, F.A.
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