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4-deoxypyridoxine 5'-phosphate + H2O
4-deoxypyridoxine + phosphate
-
-
-
-
?
4-pyridoxic acid 5'-phosphate + H2O
4-pyridoxic acid + phosphate
N-(5'-phospho-4'-pyridoxyl)benzylamine + H2O
4'-pyridoxylbenzylamine + phosphate
-
-
-
-
?
N-(5'-phospho-4'-pyridoxyl)ethanolamine + H2O
4'-pyridoxylethanolamine + phosphate
-
-
-
-
?
N-(5'-phospho-4'-pyridoxyl)glycine + H2O
4'-pyridoxylglycine + phosphate
-
-
-
-
?
N-(5'-phospho-4'-pyridoxyl)phenylalanine + H2O
4'-pyridoxylphenylalanine + phosphate
-
much higher catalytic efficiency than with pyridoxine 5-phosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
p-nitrophenyl-phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
pyridoxal 5'phosphate + H2O
pyridoxal + phosphate
-
-
-
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
pyridoxamine 5'-phosphate + H2O
pyridoxamine + phosphate
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
pyridoxine phosphate + H2O
pyridoxine + phosphate
-
-
-
-
?
pyridoxine-5'-phosphate + H2O
pyridoxine + phosphate
-
-
-
-
?
additional information
?
-
4-pyridoxic acid 5'-phosphate + H2O
4-pyridoxic acid + phosphate
-
highest catalytic efficiency with 4-pyridoxic acid 5-phosphate and pyridoxal 5-phosphate
-
-
?
4-pyridoxic acid 5'-phosphate + H2O
4-pyridoxic acid + phosphate
-
the catalytic efficiency decreases in the following order: pyridoxal 5-phosphate, 4-pyridoxic acid 5-phosphate, pyridoxine 5-phosphate and pyridoxamine 5-phosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
slow hydrolysis
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
best substrate
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
enzyme probably plays an important role in the hydrolysis of pyridoxal 5-phosphate to pyridoxal in erythrocytes, may be important in the regulation of pyridoxal 5-phosphate concentration
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
best substrate, a cysteinyl residue at or near the active site is essential for activity, there may be only one free Cys per subunit
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
highest catalytic efficiency with pyridoxal 5-phosphate and 4-pyridoxic acid 5-phosphate
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
highest specificity constant followed by pyridoxine 5-phosphate
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
kinetic mechanism, random binding of pyridoxal phosphate and Mg2+, formation of a dead-end complex of phosphate with the enzyme-Mg complex
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
mechanism, a covalent phosphoenzyme intermediate is formed during catalysis, may be an acylphosphate intermediate
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
the catalytic efficiency decreases in the following order: pyridoxal 5-phosphate, 4-pyridoxic acid 5-phosphate, pyridoxine 5-phosphate and pyridoxamine 5-phosphate
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
phosphatase activity of YZGD is highly specific on pyridoxal 5-phosphate
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
directly dephosphorylates actin-depolymerizing factor (ADF)/cofilin, PLPP/CIN-mediated actin dynamics may play an important role in the changes of morphological properties and excitability of the epileptic hippocampus
-
-
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxamine 5'-phosphate + H2O
pyridoxamine + phosphate
-
-
-
?
pyridoxamine 5'-phosphate + H2O
pyridoxamine + phosphate
-
low hydrolysis rate
-
-
?
pyridoxamine 5'-phosphate + H2O
pyridoxamine + phosphate
-
the catalytic efficiency decreases in the following order: pyridoxal 5-phosphate, 4-pyridoxic acid 5-phosphate, pyridoxine 5-phosphate and pyridoxamine 5-phosphate
-
-
?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
-
-
-
-
?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
-
-
-
?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
second highest specificity constant after pyridoxal 5-phosphate
-
-
?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
-
the catalytic efficiency decreases in the following order: pyridoxal 5-phosphate, 4-pyridoxic acid 5-phosphate, pyridoxine 5-phosphate and pyridoxamine 5-phosphate
-
-
?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
-
-
-
?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
-
-
-
?
additional information
?
-
-
probably plays an important role in the regulation of vitamin B6 metabolism
-
-
?
additional information
?
-
-
vitamin B6 metabolism
-
-
?
additional information
?
-
vitamin B6 metabolism, catabolism of pyridoxal 5-phosphate
-
-
?
additional information
?
-
-
vitamin B6 metabolism, catabolism of pyridoxal 5-phosphate
-
-
?
additional information
?
-
-
enzyme has phosphotransferase activity and transfers 20-25% of the phosphoryl group from either substrate to ethanol
-
-
?
additional information
?
-
-
hydrolyzes ten organic phosphates, but has maximum activity against pyridoxal phosphate
-
-
?
additional information
?
-
-
specifically dephosphorylates vitamin B6-phosphates, not: phenylphosphate, nucleotide phosphates, such as ATP, ADP, AMP, cAMP, FMN, phosphoamino acids, such as phosphoserine, phosphothreonine, phosphotyrosine, phosphoglycolate
-
-
?
additional information
?
-
-
specificity and active site properties, enzyme also catalyzes the dephosphorylation of 4-secondary amine derivatives of vitamin B6 phosphate, enzyme has the greatest catalytic efficiency with substrates that contain a negatively charged group on the 4-position of the pyridine ring, one or two positively charged groups at the active site of enzyme interacts with the substrates phosphate ester and 4-substituent, Arg and His residues are at or near the active site and may play roles in substrate binding and/or catalysis, very low activity with p-nitrophenylphosphate
-
-
?
additional information
?
-
very low activity with with p-nitrophenyl phosphate
-
-
?
additional information
?
-
-
very low activity with with p-nitrophenyl phosphate
-
-
?
additional information
?
-
-
pyridoxamine 5-phosphate, casein, serine phosphate, threonine phosphate, tyrosine phosphate, histidine phosphate, arginine phosphate, glycolate 2-phosphate, trehalose 6-phosphate, phosphoethanolamine and phosphocholine are not substrates
-
-
?
additional information
?
-
-
directly dephosphorylates actin-depolymerizing factor (ADF)/cofilin
-
-
?
additional information
?
-
PNP phosphatase does not act on pyridoxamine 5'-phosphate
-
-
?
additional information
?
-
-
PNP phosphatase does not act on pyridoxamine 5'-phosphate
-
-
?
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2,2'-dithiodipyridine
-
0.005 mM, 50% inhibition
2-ethyl-5-phenylisoxazolium-3'-sulfonate
4,4'-dithiodipyridine
-
0.005 mM, 50% inhibition
4-pyridoxic acid 5'-phosphate
-
very effective inhibitor, 0.02 mM, 50% inhibition of pyridoxine 5-phosphate hydrolysis
5,5'-dithiobis(2-nitrobenzoate)
5,5'-dithiobis(2-nitrobenzoic acid)
-
50 nM, 50% inhibition, incorporation of 1 mol per mol of subunit leads to complete inactivation, phosphate or dithiothreitol protects
Ca2+
-
competitive inhibition versus Mg2+, noncompetitive versus substrate
disulfide reagent
-
reactivation by excess dithiothreitol, inactivation is due to formation of a mixed disulfide between the reagent and a free cysteinyl residue at or near the active site of enzyme
-
EDTA
-
0.2 mM, complete inhibition in the absence of Mg2+, 50% inhibition in the presence of 1 mM Mg2+
fluoride
-
2 mM, 50% inhibition
iodacetate
-
52% inhibition at 5 mM
KH2PO4
-
56% inhibition at 5 mM
levamisole
-
26% inhibition at 5 mM
N-(5'-phospho-4'-pyridoxyl)ethanolamine
-
0.05 mM, 12% inhibition
N-(5'-phospho-4'-pyridoxyl)glycine
-
0.05 mM, 32% inhibition
N-(5'-phospho-4'-pyridoxyl)phenylalanine
-
0.05 mM, 51% inhibition
NaF
-
24% inhibition at 5 mM
p-nitrophenyl phosphate
-
poor, 4 mM, 50% inhibition of pyridoxine 5-phosphate hydrolysis
Phenyl phosphate
-
very poor inhibitor of pyridoxine 5-phosphate hydrolysis
pyridoxal
-
weak, 11 mM, 50% inhibition of hydrolysis of pyridoxal 5-phosphate or pyridoxine 5-phosphate
pyridoxal 5'-phosphate
-
very effective inhibitor, 0.03 mM, 50% inhibition of pyridoxine 5-phosphate hydrolysis
pyridoxamine 5'-phosphate
-
0.5 mM, 50% inhibition of pyridoxine 5-phosphate hydrolysis, less effective than pyridoxal 5-phosphate or 4-pyridoxic acid 5-phosphate
pyridoxine 5'-phosphate
-
0.05 mM, 45% inhibition
Sodium molybdate
-
79% inhibition at 5 mM
Tetranitromethane
-
inactivates in a time-dependent manner, 10 mM, 70% inhibition in the absence of pyridoxal 5-phosphate and 30% in the presence of 0.15 mM pyridoxal 5-phosphate
thiol-specific reagent
-
a variety of thiol-specific reagents inactivate in a time- and concentration-dependent manner, pyridoxal phosphate or phosphate protects
-
[(E)-2-(4-formyl-5-hydroxy-6-methylpyridin-3-yl)ethenyl]phosphonic acid
compound increases the Km up to 6fold at 2 mM. The catalytic efficiency is reduced to 10% in the presence of 2 mM of the compound
[2-(4-formyl-5-hydroxy-6-methylpyridin-3-yl)ethyl]phosphonic acid
compound increases the Km up to 6fold at 2 mM. The catalytic efficiency is reduced to 10% in the presence of 2 mM of the compound
[2-[5-hydroxy-4-(hydroxymethyl)-6-methylpyridin-3-yl]ethyl]phosphonic acid
-
2-ethyl-5-phenylisoxazolium-3'-sulfonate
-
0.25 mM, 5 min at 22°C, 60% loss of activity, inactivates in a concentration- and time-dependent manner, which follows pseudo-first-order kinetics, pyridoxal 5-phosphate, pyridoxine 5-phosphate or phosphate protects
2-ethyl-5-phenylisoxazolium-3'-sulfonate
-
inhibition is potentiated by MgCl2
5,5'-dithiobis(2-nitrobenzoate)
-
inhibition is potentiated by MgCl2
5,5'-dithiobis(2-nitrobenzoate)
-
-
diethyldicarbonate
-
inhibition is not potentiated by MgCl2
diethyldicarbonate
-
inactivates by reacting with a group with a pKalpha of 6.7, kinetics, pyridoxine 5-phosphate protects, 100 mM neutral hydroxylamine partially reactivates
iodoacetate
-
inhibition is potentiated by MgCl2
iodoacetate
-
enzyme is very sensitive to
iodoacetate
-
0.075 mM, 50% inhibition, incorporation of 0.6 mol per mol of subunit leads to complete inactivation, phosphate protects, inhibition kinetics
Mn2+
-
inhibits above 0.05 mM, activates below 0.05 mM
Mn2+
-
Mn2+ lowers activity of the Co2+-supported phosphatase activity, but does not eliminate it
molybdate
-
competitive inhibition versus substrate, noncompetitive versus Mg2+
molybdate
-
very effective inhibitor, 0.0029 mM, 50% inhibition
N-ethylmaleimide
-
inactivated by low concentrations, low concentrations of a substrate, pyridoxine phosphate, or phosphate protect from inactivation, inhibition is not potentiated by MgCl2
N-ethylmaleimide
-
enzyme is very sensitive to
N-ethylmaleimide
-
0.1 mM, 50% inhibition, incorporation of 0.6 mol per mol of subunit leads to complete inactivation, inhibition kinetics, phosphate protects
N-ethylmaleimide
-
46% inhibition at 5 mM
p-chloromercuribenzoate
-
enzyme is very sensitive to
p-chloromercuribenzoate
-
250 nM, 50% inhibition
Phenylglyoxal
-
inhibition is not potentiated by MgCl2
Phenylglyoxal
-
the incorporation of 1 mol per subunit inactivates, pyridoxal 5-phosphate protects, kinetics
phosphate
-
competitive inhibitor
phosphate
-
competitive inhibition versus substrate, noncompetitive versus Mg2+
phosphate
-
competitive inhibitor with respect to pyridoxine 5-phosphate, product inhibition
phosphate
-
competitive inhibitor
Zn2+
-
inhibits at higher concentrations, activates somewhat at low concentrations
Zn2+
-
very potent inhibitor, 50% inhibition in the presence of MgCl2 by 0.01 mM ZnCl2
additional information
-
not inhibited by nucleotide phosphates, phosphoamino acids, levamisole, L-phenylalanine, L(+)-tartrate, 5 mM ATP, 5 mM phosphoglycolate, 0.5 mM alpha- or beta-glycerophosphate, 0.5 mM 3-phosphoglycerate, 0.5 mM 2,3-bisphosphoglycerate, 5 mM pyridoxine, 5 mM pyridoxamine, 5 mM 4-pyridoxic acid, 5 mM 4-pyridine-carboxaldehyde, 5 mM isonicotinate, 5 mM 3-hydroxypyridine, 5 mM salicylaldehyde, 5 mM benzaldehyde
-
additional information
-
not inhibited by iodoacetamide or cystamine
-
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0.00112 - 0.00255
4-pyridoxic acid 5'-phosphate
0.0635
N-(5'-phospho-4'-pyridoxyl)benzylamine
-
pH 7.4, 37°C
0.0786
N-(5'-phospho-4'-pyridoxyl)ethanolamine
-
pH 7.4, 37°C
0.0143
N-(5'-phospho-4'-pyridoxyl)glycine
-
pH 7.4, 37°C
0.00824
N-(5'-phospho-4'-pyridoxyl)phenylalanine
-
pH 7.4, 37°C
0.00129 - 0.33
pyridoxal 5'-phosphate
0.33 - 0.385
pyridoxal-5'-phosphate
0.034 - 0.0806
pyridoxamine 5'-phosphate
0.0043 - 0.0434
pyridoxine 5'-phosphate
0.385
pyridoxine-5'-phosphate
-
1 mM MnCl2, 50 mM Tris-HCl pH 7.0
additional information
additional information
-
0.00112
4-pyridoxic acid 5'-phosphate
-
pH 7.4, 37°C
0.00255
4-pyridoxic acid 5'-phosphate
-
pH 7.4, 37°C
0.00129
pyridoxal 5'-phosphate
-
pH 7.4, 37°C
0.00147
pyridoxal 5'-phosphate
-
pH 7.4, 37°C
0.00154
pyridoxal 5'-phosphate
-
pH 7.4, 37°C, 0.188 mM Mg2+
0.00166
pyridoxal 5'-phosphate
-
pH 7.4, 37°C, 0.06 mM Co2+
0.0025
pyridoxal 5'-phosphate
pH 7.4, 37°C, recombinant enzyme
0.039
pyridoxal 5'-phosphate
pH 7.4, 22°C
0.33
pyridoxal 5'-phosphate
-
-
0.33
pyridoxal-5'-phosphate
-
5 mM CoCl2, 1 mM dithiothreitol, 50 mM Tris/maleate pH 5.0, 37°C
0.385
pyridoxal-5'-phosphate
-
1 mM MnCl2, 50 mM Tris-HCl pH 7.0
0.034
pyridoxamine 5'-phosphate
-
pH 7.4, 37°C
0.0547
pyridoxamine 5'-phosphate
-
pH 7.4, 37°C
0.0806
pyridoxamine 5'-phosphate
pH 7.4, 37°C, recombinant enzyme
0.0043
pyridoxine 5'-phosphate
-
pH 7.4, 37°C, 0.39 mM Mg2+
0.00519
pyridoxine 5'-phosphate
-
pH 7.4, 37°C
0.00812
pyridoxine 5'-phosphate
-
pH 7.4, 37°C, 0.13 mM Co2+
0.0106
pyridoxine 5'-phosphate
-
pH 7.4, 37°C
0.0434
pyridoxine 5'-phosphate
pH 7.4, 37°C, recombinant enzyme
additional information
additional information
-
kinetic data, effect of pH on Km for 4-pyridoxic acid 5-phosphate, pyridoxal 5-phosphate, pyridoxine 5-phosphate and pyridoxamine 5-phosphate
-
additional information
additional information
-
kinetic mechanism, kinetic properties
-
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105
-
1 mM MnCl2, 50 mM Tris-HCl pH 7.0
20
-
5 mM CoCl2, 1 mM dithiothreitol, 50 mM Tris/maleate pH 5.0, 37°C
42
-
1 mM MnCl2, 50 mM Tris-HCl pH 7.0
1.4
-
pH 7.4, 37°C
1.4
pH 7.4, 37°C, hydrolysis of pyridoxal 5-phosphate, recombinant enzyme
7
-
purified enzyme
7
-
5 mM CoCl2, 1 mM dithiothreitol, 50 mM Tris/maleate pH 5.0, 37°C
additional information
-
-
additional information
-
-
additional information
-
-
additional information
crude extract contains 0.13 units/mg, purified PEP-1-PLPP fusion protein contains 1.5 units/mg, after purification of recombinant enzyme, pH 7.4 in 40 mM triethanolamineamine-HCl, measuring absorbance reduction at 390 nm (3 min)
additional information
-
crude extract contains 0.13 units/mg, purified PEP-1-PLPP fusion protein contains 1.5 units/mg, after purification of recombinant enzyme, pH 7.4 in 40 mM triethanolamineamine-HCl, measuring absorbance reduction at 390 nm (3 min)
additional information
-
total activity of PLP-P significantly increases 2 days after ischemia, whereas the specific activity is not altered
additional information
-
21.3 units, Tat-protein transduction (200 microg/kg), long-term potentiation induced by high frequency stimulation (2000 total stimuli, delivered in two five 1 s long tetanic (400 Hz) stimulus trains, 2 min apart), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
-
22.3 units, control animals (saline-treated and without high-frequency stimulation), long-term potentiation induced by high frequency stimulation (2000 total stimuli, delivered in two five 1 s long tetanic (400 Hz) stimulus trains, 2 min apart), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
-
26.1 units, control animals (saline-treated and without high-frequency stimulation), long-term potentiation induced by high frequency stimulation (1600 total stimuli, delivered in two five 1 s long tetanic (400 Hz) stimulus trains, 2 min apart), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
-
27.8 units, Tat-protein transduction (200 microg/kg), long-term potentiation induced by high frequency stimulation (1600 total stimuli, delivered in two five 1 s long tetanic (400 Hz) stimulus trains, 2 min apart), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
-
29.1 units, Tat-protein transduction (200 microg/kg), long-term potentiation induced by high frequency stimulation (1200 total stimuli, delivered in two five 1 s long tetanic (400 Hz) stimulus trains, 2 min apart), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
-
29.4 units, control animals (saline-treated and without high-frequency stimulation), long-term potentiation induced by high frequency stimulation (1200 total stimuli, delivered in two five 1 s long tetanic (400 Hz) stimulus trains, 2 min apart), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
-
32.1 units, control animals (saline-treated and without high-frequency stimulation), long-term potentiation induced by high frequency stimulation (800 total stimuli, delivered in two five 1 s long tetanic (400 Hz) stimulus trains, 2 min apart), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
-
33.7 units, Tat-protein transduction (200 microg/kg), long-term potentiation induced by high frequency stimulation (800 total stimuli, delivered in two five 1 s long tetanic (400 Hz) stimulus trains, 2 min apart), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
-
42.1 units, control animals (saline-treated and without high-frequency stimulation), no long-term potentiation induced, pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
-
43.2 units, Tat-protein transduction (200 microg/kg), no long-term potentiation induced, pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
-
59.8 units, Tat Tat-PLPP/CIN transductions (20 microg/kg), long-term potentiation induced by high frequency stimulation (1600 total stimuli, delivered in two five 1 s long tetanic (400 Hz) stimulus trains, 2 min apart), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
-
60.4 units, Tat-PLPP/CIN transductions (20 microg/kg), long-term potentiation induced by high frequency stimulation (800 total stimuli, delivered in two five 1 s long tetanic (400 Hz) stimulus trains, 2 min apart), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
-
62.3 units, Tat-PLPP/CIN transductions (20 microg/kg), long-term potentiation induced by high frequency stimulation (2000 total stimuli, delivered in two five 1 s long tetanic (400 Hz) stimulus trains, 2 min apart), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
-
62.3 units, Tat-PLPP/CIN transductions (20 microg/kg), no long-term potentiation induced, pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
-
68.9 units, Tat-PLPP/CIN transductions (20 microg/kg), long-term potentiation induced by high frequency stimulation (1200 total stimuli, delivered in two five 1 s long tetanic (400 Hz) stimulus trains, 2 min apart), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
-
71.0 units, Tat-PLPP/CIN transductions (200 microg/kg), no long-term potentiation induced, pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
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74.2 units, Tat-PLPP/CIN transductions (200 microg/kg), long-term potentiation induced by high frequency stimulation (1200 total stimuli, delivered in two five 1 s long tetanic (400 Hz) stimulus trains, 2 min apart), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
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80.6 units, Tat-PLPP/CIN transductions (200 microg/kg), long-term potentiation induced by high frequency stimulation (800 total stimuli, delivered in two five 1 s long tetanic (400 Hz) stimulus trains, 2 min apart), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
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82.3 units, Tat Tat-PLPP/CIN transductions (200 microg/kg), long-term potentiation induced by high frequency stimulation (1600 total stimuli, delivered in two five 1 s long tetanic (400 Hz) stimulus trains, 2 min apart), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
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85.4 units, Tat-PLPP/CIN transductions (200 microg/kg), long-term potentiation induced by high frequency stimulation (2000 total stimuli, delivered in two five 1 s long tetanic (400 Hz) stimulus trains, 2 min apart), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance at 390 nm (3 min)
additional information
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approx. 42 units, control animals (saline-treated and without high-frequency stimulation), pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance reduction at 390 nm (3 min)
additional information
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approx. 48 units, PNPP/CIN, pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance reduction at 390 nm (3 min)
additional information
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approx. 50 units, control animals (saline-treated and without high-frequency stimulation), 1 week after status epilepticus, pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance reduction at 390 nm (3 min)
additional information
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approx. 62 units, Tat-PNPP/CIN, pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance reduction at 390 nm (3 min)
additional information
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approx. 65 units, control animals (saline-treated and without high-frequency stimulation), 6 weeks after statur epilepticus, pH 7.4 in 40 mM triethanolamineamine-HCl, measuring the rate of production of pyridoxal from pyridoxal-5'-phosphate, absorbance reduction at 390 nm (3 min)
additional information
Sinorhizobium meliloti IFO 14782/pVKPtacpdxP shows PNP phosphatase activity 3.5times higher than that of the parent strain, when 2 mM pyridoxine 5'-phosphate is used as substrate. When pyridoxamine 5'-phosphate is used as substrate, the phosphatase activity of Sinorhizobium meliloti IFO 14782/pVKPtacpdxP is as low as that of the parent
additional information
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Sinorhizobium meliloti IFO 14782/pVKPtacpdxP shows PNP phosphatase activity 3.5times higher than that of the parent strain, when 2 mM pyridoxine 5'-phosphate is used as substrate. When pyridoxamine 5'-phosphate is used as substrate, the phosphatase activity of Sinorhizobium meliloti IFO 14782/pVKPtacpdxP is as low as that of the parent
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cDNA, from brain, expression in Escherichia coli M15/pRER4, sequencing, ORF is located on chromosome 22q12.3, genomic organization
cloned into plasmid pET15b, expression in Escherichi coli BL21 (DE3) as His-tag fusion protein
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expression in Escherichia coli HMS174(DE3)
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full-length cDNA, from brain, sequencing, ORF is located on chromosome 15.E1, genomic organization
getting Tat-PLPP/CIN: amplification of PLPP/CIN via PCR and inserted into pGEM-T vector, subcloned into pET15b, transformation of BL21 Escherichia coli. getting PLPP: cDNA of PLPP amplified via PCR and cloned into pET15b, transformation of Escherichia coli JM109 (DE3). experiments with Sprague-Dawley (SD) rats (7 weeks old). The effect of PNP treatment on PLPP/CIN immunoreactivity in the rat hippocampus: vitamin B6 may not be directly involved in ADF/cofilin-mediated F-actin depolymerization in normal condition. Up-regulation of PLPP/CIN expression following status epilepticus may play an important role in the formation of epileptic hippocampus. Hippocampal excitability following transduction of Tat-PLPP/CIN: F-actin depolymerization induced by over-expression of PLPP/CIN may increase excitability ratio in the hippocampus via postsynaptic changes, not via impaired GABAergic inhibition (immunohistochemistry, optical density, enzyme activity, electrophysiological analysis)
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getting Tat-PLPP/CIN: amplification of PLPP/CIN via PCR and inserted into pGEM-T vector, subcloned into pET15b, transformation of BL21 Escherichia coli. getting PLPP: cDNA of PLPP amplified via PCR and cloned into pET15b, transformation of Escherichia coli JM109 (DE3). investigation whether expression of PLPP/CIN is altered following long-term potentiation (LTP) induction and whether Tat-PLPP/CIN transduction affects LTP induction in the rat Sprague-Dawley. PLPP/CIN immunoreactivity is decreased in dentate granule cells after induction of LTP (induction: stimulating electrode for high frequency stimulation and recording electrode). Tat-PLPP/CIN transduction (20 and 200 microg/kg) decreased the efficiency of high frequency stimulus-induced potentiation of populations spike amplitude as compared to saline or Tat-protein-treated animals. PLPP/CIN protein level shows inverse correlation with phosphorylated ADF/cofilin levels and F-actin content (immunohistochemistry). conclusion: PLPP/CIN-mediated actin dynamics may play important role in changes of morphological properties (dendritic spine reorganization) of the hippocampus in LTP.
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His-tag fusion, expression in Escherichia coli
into pCRII-TOPO vector, 0.86 kb SmaI fragment from TOPOpdxP ligated into the SmaI site of pKK223-3, overexpression in Escherichia coli JM109. Overexpression in Sinorhizobium meliloti IFO 14782 recombinant with pVKPtacpdxP
into pET15b vector and expressed in Escherichia coli BL21(DE3)
PLPP gene fused with a PEP-1 peptide (PEP-1-PLPP) and 6His-tag and cloned into pET-15b. Expression in Escherichia coli BL21 (DE3) transduced into PC12 cells at various times and concentrations to evaluate the transduction ability (analyzed by Western blotting, fluorescence labeled). PLP concentration in cells PC12 cells changed by transduced PEP-1-PLPP fusion protein (spectroscopic measurement)
yzgd gene subcloned from plasmid pAN13, ligated into plasmid pET11b, transformed into Escherichia coli DH5alpha for storage and Escherichia coli HMS174(DE3) for expression
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