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Information on EC 3.1.3.74 - pyridoxal phosphatase
for references in articles please use BRENDA:EC3.1.3.74
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.3 Phosphoric-monoester hydrolases
3.1.3.74 pyridoxal phosphatase
IUBMB Comments
Requires Mg2+. This enzyme is specific for phosphorylated vitamin B6 compounds: it acts not only on pyridoxal phosphate (PLP), but also on pyridoxine phosphate (PNP), pyridoxamine phosphate (PMP), 4-pyridoxic acid phosphate and 4-deoxypyridoxine phosphate. This reaction can also be carried out by EC 3.1.3.1 (alkaline phosphatase) and EC 3.1.3.2 (acid phosphatase), but these enzymes have very broad substrate specificities.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 3.1.3.74
- phosphatases
-
vitamer
- drug development
-
dehalogenase
-
haloacid
-
actin-depolymerizing
showSynonyms
plpp/cin, plp phosphatase, pyridoxal phosphatase, pyridoxal phosphate phosphatase, pyridoxine phosphate phosphatase, plpase, pyridoxal-5'-phosphate phosphatase/chronophin, pyridoxal-5'-phosphate phosphatase, pnp phosphatase, pyridoxine 5'-phosphate phosphatase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PDXP
PLP phosphatase
PLPP
PLPP/CIN
PNP phosphatase
pyridoxal phosphatase
pyridoxal phosphate phosphatase
pyridoxal-5'-phosphate phosphatase
pyridoxal-5'-phosphate phosphatase/chronophin
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate
requires Mg2+, this enzyme is specific for phosphorylated vitamin B6 compounds: it acts not only on pyridoxal phosphate (PLP), but also on pyridoxine phosphate (PNP), pyridoxamine phosphate (PMP), 4-pyridoxic acid phosphate and 4-deoxypyridoxine phosphate, this reaction can also be carried out by EC 3.1.3.1 (alkaline phosphatase) and EC 3.1.3.2 (acid phosphatase), but these enzymes have very broad substrate specificities
-
pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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PATHWAY SOURCE
PATHWAYS
MetaCyc
ginkgotoxin biosynthesis, pyridoxal 5'-phosphate salvage II (plants)
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SYSTEMATIC NAME
IUBMB Comments
pyridoxal-5'-phosphate phosphohydrolase
Requires Mg2+. This enzyme is specific for phosphorylated vitamin B6 compounds: it acts not only on pyridoxal phosphate (PLP), but also on pyridoxine phosphate (PNP), pyridoxamine phosphate (PMP), 4-pyridoxic acid phosphate and 4-deoxypyridoxine phosphate. This reaction can also be carried out by EC 3.1.3.1 (alkaline phosphatase) and EC 3.1.3.2 (acid phosphatase), but these enzymes have very broad substrate specificities.
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CAS REGISTRY NUMBER
COMMENTARY
9076-92-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-deoxypyridoxine 5'-phosphate + H2O
4-deoxypyridoxine + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
-
Substrates: 55.93% compared to the activity with pyridoxal 5'-phosphate
Products: -
Products: -
?
adenosine-5'-triphosphate + H2O
?
-
Substrates: 22.43% compared to the activity with pyridoxal 5'-phosphate
Products: -
Products: -
?
flavin mononucleotide + H2O
?
-
Substrates: 31.24% compared to the activity with pyridoxal 5'-phosphate
Products: -
Products: -
?
N-(5'-phospho-4'-pyridoxyl)benzylamine + H2O
4'-pyridoxylbenzylamine + phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5'-phospho-4'-pyridoxyl)ethanolamine + H2O
4'-pyridoxylethanolamine + phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5'-phospho-4'-pyridoxyl)glycine + H2O
4'-pyridoxylglycine + phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5'-phospho-4'-pyridoxyl)phenylalanine + H2O
4'-pyridoxylphenylalanine + phosphate
-
Substrates: much higher catalytic efficiency than with pyridoxine 5-phosphate
Products: -
Products: -
?
p-nitrophenyl-phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
phenylphosphate + H2O
phenol + phosphate
-
Substrates: 31.69% compared to the activity with pyridoxal 5'-phosphate
Products: -
Products: -
?
pyridoxal 5'phosphate + H2O
pyridoxal + phosphate
Substrates: -
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?
pyridoxine phosphate + H2O
pyridoxine + phosphate
-
Substrates: -
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?
pyridoxine-5'-phosphate + H2O
pyridoxine + phosphate
-
Substrates: -
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?
sodium phytate + H2O
?
-
Substrates: 36.02% compared to the activity with pyridoxal 5'-phosphate
Products: -
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?
4-pyridoxic acid 5'-phosphate + H2O
4-pyridoxic acid + phosphate
-
Substrates: highest catalytic efficiency with 4-pyridoxic acid 5-phosphate and pyridoxal 5-phosphate
Products: -
Products: -
?
4-pyridoxic acid 5'-phosphate + H2O
4-pyridoxic acid + phosphate
-
Substrates: the catalytic efficiency decreases in the following order: pyridoxal 5-phosphate, 4-pyridoxic acid 5-phosphate, pyridoxine 5-phosphate and pyridoxamine 5-phosphate
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: slow hydrolysis
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?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
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?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: 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
Products: -
Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: best substrate, a cysteinyl residue at or near the active site is essential for activity, there may be only one free Cys per subunit
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?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: highest catalytic efficiency with pyridoxal 5-phosphate and 4-pyridoxic acid 5-phosphate
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?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: best substrate
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?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
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?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
Substrates: highest specificity constant followed by pyridoxine 5-phosphate
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?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: the catalytic efficiency decreases in the following order: pyridoxal 5-phosphate, 4-pyridoxic acid 5-phosphate, pyridoxine 5-phosphate and pyridoxamine 5-phosphate
Products: -
Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: kinetic mechanism, random binding of pyridoxal phosphate and Mg2+, formation of a dead-end complex of phosphate with the enzyme-Mg complex
Products: -
Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: mechanism, a covalent phosphoenzyme intermediate is formed during catalysis, may be an acylphosphate intermediate
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?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
Substrates: -
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Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
Substrates: -
Products: -
Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
Substrates: -
Products: -
Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
Substrates: -
Products: -
Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: phosphatase activity of YZGD is highly specific on pyridoxal 5-phosphate
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Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: 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
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Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
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Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
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Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
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Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
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Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
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Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
Substrates: -
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Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
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Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
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Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
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Products: -
?
pyridoxamine 5'-phosphate + H2O
pyridoxamine + phosphate
-
Substrates: low hydrolysis rate
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?
pyridoxamine 5'-phosphate + H2O
pyridoxamine + phosphate
-
Substrates: the catalytic efficiency decreases in the following order: pyridoxal 5-phosphate, 4-pyridoxic acid 5-phosphate, pyridoxine 5-phosphate and pyridoxamine 5-phosphate
Products: -
Products: -
?
pyridoxamine 5'-phosphate + H2O
pyridoxamine + phosphate
Substrates: -
Products: -
Products: -
?
pyridoxamine 5'-phosphate + H2O
pyridoxamine + phosphate
-
Substrates: 75.1% compared to the activity with pyridoxal 5'-phosphate
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?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
-
Substrates: -
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Products: -
?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
Substrates: second highest specificity constant after pyridoxal 5-phosphate
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?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
-
Substrates: the catalytic efficiency decreases in the following order: pyridoxal 5-phosphate, 4-pyridoxic acid 5-phosphate, pyridoxine 5-phosphate and pyridoxamine 5-phosphate
Products: -
Products: -
?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
-
Substrates: -
Products: -
Products: -
?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
Substrates: -
Products: -
Products: -
?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
Substrates: -
Products: -
Products: -
?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
-
Substrates: 77.69% compared to the activity with pyridoxal 5'-phosphate
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Products: -
?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: vitamin B6 metabolism, catabolism of pyridoxal 5-phosphate
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?
additional information
?
-
-
Substrates: vitamin B6 metabolism, catabolism of pyridoxal 5-phosphate
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Products: -
?
additional information
?
-
-
Substrates: probably plays an important role in the regulation of vitamin B6 metabolism
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?
additional information
?
-
-
Substrates: 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
Products: -
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?
additional information
?
-
-
Substrates: hydrolyzes ten organic phosphates, but has maximum activity against pyridoxal phosphate
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?
additional information
?
-
Substrates: very low activity with with p-nitrophenyl phosphate
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?
additional information
?
-
-
Substrates: very low activity with with p-nitrophenyl phosphate
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?
additional information
?
-
-
Substrates: specifically dephosphorylates vitamin B6-phosphates, not: phenylphosphate, nucleotide phosphates, such as ATP, ADP, AMP, cAMP, FMN, phosphoamino acids, such as phosphoserine, phosphothreonine, phosphotyrosine, phosphoglycolate
Products: -
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?
additional information
?
-
-
Substrates: enzyme has phosphotransferase activity and transfers 20-25% of the phosphoryl group from either substrate to ethanol
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: directly dephosphorylates actin-depolymerizing factor (ADF)/cofilin
Products: -
Products: -
?
additional information
?
-
Substrates: PNP phosphatase does not act on pyridoxamine 5'-phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: PNP phosphatase does not act on pyridoxamine 5'-phosphate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyridoxal 5'phosphate + H2O
pyridoxal + phosphate
Substrates: -
Products: -
Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: 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
Products: -
Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: 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
Products: -
Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
Substrates: -
Products: -
Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: vitamin B6 metabolism, catabolism of pyridoxal 5-phosphate
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?
additional information
?
-
-
Substrates: vitamin B6 metabolism, catabolism of pyridoxal 5-phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: probably plays an important role in the regulation of vitamin B6 metabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: directly dephosphorylates actin-depolymerizing factor (ADF)/cofilin
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Mg2+
-
similar activation as by Co2+ and Ni2+, kinetics, probably the physiological activator
Mg2+
requirement for a divalent cation, Mg2+ is most effective in catalyzing the dephosphorylation of pyridoxal 5-phosphate
Mn2+
-
less activatory than Mg2+, Co2+ or Ni2+, inhibits above 0.05 mM, kinetics
Zn2+
-
activates somewhat at low concentrations, inhibits at higher concentrations
additional information
-
not activated by 100 mM NaCl, KCl, NaBr, NaI, NaNO3 or sodium acetate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-pyridoxic acid 5'-phosphate
-
very effective inhibitor, 0.02 mM, 50% inhibition of pyridoxine 5-phosphate hydrolysis
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
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
-
p-nitrophenyl phosphate
-
poor, 4 mM, 50% inhibition 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
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
diethyldicarbonate
-
inactivates by reacting with a group with a pKalpha of 6.7, kinetics, pyridoxine 5-phosphate protects, 100 mM neutral hydroxylamine partially reactivates
EDTA
-
0.2 mM, complete inhibition in the absence of Mg2+, 50% inhibition in the presence of 1 mM Mg2+
iodoacetate
-
0.075 mM, 50% inhibition, incorporation of 0.6 mol per mol of subunit leads to complete inactivation, phosphate protects, inhibition kinetics
Mn2+
-
Mn2+ lowers activity of the Co2+-supported phosphatase activity, but does not eliminate it
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
-
0.1 mM, 50% inhibition, incorporation of 0.6 mol per mol of subunit leads to complete inactivation, inhibition kinetics, phosphate protects
Phenylglyoxal
-
the incorporation of 1 mol per subunit inactivates, pyridoxal 5-phosphate protects, kinetics
phosphate
-
competitive inhibitor with respect to pyridoxine 5-phosphate, product inhibition
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the presence of glucose in the growth medium increases the amount of pyridoxal phosphate phosphatase compared with pyridoxamine oxidase activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Autoimmune Diseases
Pyridoxal phosphatase is a novel cancer autoantigen in the central nervous system.
Carcinoma, Hepatocellular
Azo dye-induced alterations in vitamin B-6 metabolism and in pyridoxal 5'-phosphate-binding proteins in rat liver.
Epilepsy
PLPP/CIN-mediated Mdm2 dephosphorylation increases seizure susceptibility via abrogating PSD95 ubiquitination.
Epilepsy
PLPP/CIN-mediated NEDD4-2 S448 dephosphorylation regulates neuronal excitability via GluA1 ubiquitination.
Lung Neoplasms
Pyridoxal phosphatase is a novel cancer autoantigen in the central nervous system.
Neoplasms
Chronophin is a glial tumor modifier involved in the regulation of glioblastoma growth and invasiveness.
Neoplasms
Pyridoxal phosphatase is a novel cancer autoantigen in the central nervous system.
Nervous System Diseases
Pyridoxal phosphatase is a novel cancer autoantigen in the central nervous system.
Seizures
PLPP/CIN Regulates Seizure Activity by the Differential Modulation of Calsenilin Binding to GluN1 and Kv4.2 in Mice.
Seizures
PLPP/CIN-mediated Mdm2 dephosphorylation increases seizure susceptibility via abrogating PSD95 ubiquitination.
Status Epilepticus
Potential role of pyridoxal-5'-phosphate phosphatase/chronopin in epilepsy.
Status Epilepticus
Pyridoxal-5'-phosphate phosphatase/chronophin induces astroglial apoptosis via actin-depolymerizing factor/cofilin system in the rat brain following status epilepticus.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.33
pyridoxal-5'-phosphate
-
5 mM CoCl2, 1 mM dithiothreitol, 50 mM Tris/maleate pH 5.0, 37°C
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19
pyridoxal-5'-phosphate
-
5 mM CoCl2, 1 mM dithiothreitol, 50 mM Tris/maleate pH 5.0, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.246
[(E)-2-(4-formyl-5-hydroxy-6-methylpyridin-3-yl)ethenyl]phosphonic acid
Mus musculus
pH 7.4, 22°C
0.079
[2-(4-formyl-5-hydroxy-6-methylpyridin-3-yl)ethyl]phosphonic acid
Mus musculus
pH 7.4, 22°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.4
20
-
5 mM CoCl2, 1 mM dithiothreitol, 50 mM Tris/maleate pH 5.0, 37°C
additional information
1.4
pH 7.4, 37°C, hydrolysis of pyridoxal 5-phosphate, recombinant enzyme
7
-
5 mM CoCl2, 1 mM dithiothreitol, 50 mM Tris/maleate pH 5.0, 37°C
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
additional information
-
alkaline and acid pyridoxal phosphate phosphatase, not identical with alkaline and acid phosphatase
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8.5
-
pH 7.0: about 55% of maximal activity, pH 8.5: about 55% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
high relative expression in intravascular schistosome life stages
brenda
additional information
-
4-5 days after ischemia PLP-P expressed in glial components
brenda
highly abundant in, most highly represented in all the regions of central nerve system except the spinal cord
brenda
-
activity measurement over a 6-week period in rats fed pyridoxine-sufficient and pyridoxine-deficient diets
brenda
-
after 3 h after ischemia/reperfusion, PLP-P decreases significantly in the CA1 region. 12 h after ischemia PLP-P in the CA1 region slightly increases, thereafter time-dependent increase. PLP-P protein level highest 2 days after ischemia, whereas 4 days after ischemia PLP-P decreases/disappears
brenda
-
activity measurement over a 6-week period in rats fed pyridoxine-sufficient and pyridoxine-deficient diets
brenda
additional information
mRNA is differentially expressed in a tissue-specific manner, tissue distribution
brenda
additional information
-
mRNA is differentially expressed in a tissue-specific manner, tissue distribution
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
-
subcellular localization in polymorphonuclear leukocytes
-
brenda
additional information
-
localization of PLPP/CIN in the rat hippocampus: PLPP/CIN is mainly localized in postsynaptic compartments, but not in presynaptic compartments (immunohistochemistry)
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
the enzyme is involved in intracellular vitamin B6 metabolism
physiological function
malfunction
-
inhibition and knockdown of the enzyme (PDXP) in HEK293 cells results in normalization of cellular pyridoxal 5'-phosphate and decreased pyridoxal content
malfunction
-
down-regulation has a great impact on the transcription of genes encoding vitamin B6 metabolic enzymes
physiological function
-
pyridoxal-5'-phosphate phosphatase/chronophin, i.e. PLPP/CIN, regulates phosphorylation of ADF/cofilin levels. PLPP/CIN level show a direct proportionality to nuclear translocation of ADF/cofilin. Nuclear accumulation of ADF/cofilin itself may not induce apoptogenic events, but may play a synergic role in apoptosis-like astroglial loss following status epilepticus, detailed analysis, overview
physiological function
PDXP transgenic mice have immature spines with small heads, while PDXP knockout mice have gigantic spines. PDXP transgenic mice exhibit enhanced synaptic plasticity, while knockout mice show abnormal synaptic plasticity. PDXP also enhances N-methyl-D-aspartate receptor (GluN) functionality by regulating the coupling of GluN2A with interacting proteins, particularly postsynaptic density-95
physiological function
-
the enzyme contributes to the regulation of cellular pyridoxal 5'-phosphate concentration
physiological function
-
the enzyme plays an important role for maintaining homeostasis of pyridoxal 5'-phosphate within the chloroplast in plants
physiological function
-
pyridoxal-5'-phosphate phosphatase/chronophin, i.e. PLPP/CIN, regulates phosphorylation of ADF/cofilin levels. PLPP/CIN level show a direct proportionality to nuclear translocation of ADF/cofilin. Nuclear accumulation of ADF/cofilin itself may not induce apoptogenic events, but may play a synergic role in apoptosis-like astroglial loss following status epilepticus, detailed analysis, overview
-
Show AA Sequence and Transmembrane Helices (842 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31698
2 * 31698, sequence calculation, 2 * 32000, recombinant enzyme, SDS-PAGE
32000
33000
45000
64000
32000
2 * 31698, sequence calculation, 2 * 32000, recombinant enzyme, SDS-PAGE
45000
-
2 * 45000, gel filtration compared to deduced molecular weight from sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
2 * 31698, sequence calculation, 2 * 32000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 45000, gel filtration compared to deduced molecular weight from sequence
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure in presence of inhibitor [2-[5-hydroxy-4-(hydroxymethyl)-6-methylpyridin-3-yl]ethyl]phosphonic acid. The overall structure of murine PDXP remains unaltered by ligand binding
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D12N
E324Q
-
no difference in the expression, solubility or PLPase activity between the mutant or the wild-type enzyme
D12N
-
complete loss of activity, the corresponding Asp residue is part of the active site in other HAD superfamily members
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme is unstable at low protein concentration, 0.002% Triton X-100 stabilizes, enzyme is unstable to freezing in the absence of glycerol
-
recombinant PEP-1-PLPP fusion protein transduced into PC12 cells is stable for 36 h
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, storage at concentrations of 0.3 mg/ml or greater, 30 mM phosphate, at least 6 months, stable
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by gel filtration
lysed by French Press Cell and by sonication in binding buffer (5 mM imidazole, 500 mM NaCl, and 20 mMTris-HCl, pH 7.9)., Ni2+-IDA column, desalting with PD10 column
-
Ni-affinity chromatography
sonication of cells in binding buffer (5 mM imidazole, 0.5 M NaCl, 20 mM Tris-HCl, pH 7.9), centrifugation, Ni2+-nitrilotriacetic acid Sepharose affinity column, salt removed with PD10 column
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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)
-
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.
-
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
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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression level in adult males is set at 100%. Lowest relative expression is seen in the cercarial life stage and robust expression is seen in all intravascular life stages (adults and schistosomula). SmPLP-Ph exhibits notably high relative expression in schistosomula
lactoferrin activates expression of PDXP, which significantly up-regulates the synthesis of vitamin B6 and the phosphoinositide 3-kinase/serine/threonine-protein kinase/extracellular regulated protein kinases 1/2 pathway
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
additional information
drug development
possibility of development of the pyridoxine production process by a metabolic engineering approach. In the future, overexpression of the pdxP gene in combination with another pyridoxine gene will be necessary to develop even more efficient processes for production of vitamin B6
drug development
transduction of the PEP-1-PLPP fusion protein into cells would be useful as therapeutic agent for various disorders related to this enzyme and vitamin B6
additional information
hypothetical protein Q8CHP8 shows 44-47% sequence identity to pyridoxal phosphate phosphatase
additional information
-
hypothetical protein Q8CHP8 shows 44-47% sequence identity to pyridoxal phosphate phosphatase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gao, G.J.; Fonda, M.L.
Evidence for a phosphoenzyme intermediate formed during catalysis by pyridoxal phosphatase from human erythrocytes
Arch. Biochem. Biophys.
313
166-172
1994
Homo sapiens
brenda
Fonda, M.L.; Zhang, Y.N.
Kinetic mechanism and divalent metal activation of human erythrocyte pyridoxal phosphatase
Arch. Biochem. Biophys.
320
345-352
1995
Homo sapiens
brenda
Turner, J.M.; Happold, F.C.
Pyridoxamine oxidase and pyridoxal phosphate phosphatase activities in Escherichia coli
Biochem. J.
78
364-372
1961
Escherichia coli
brenda
Smith, G.P.; Peters, T.J.
Subcellular localization and properties of pyridoxal phosphate phosphatases of human polymorphonuclear leukocytes and their relationship to acid and alkaline phosphatase
Biochim. Biophys. Acta
661
287-294
1981
Homo sapiens
brenda
Fonda, M.L.
Purification and characterization of vitamin B6-phosphate phosphatase from human erythrocytes
J. Biol. Chem.
267
15978-15983
1992
Homo sapiens
brenda
Gao, G.J.; Fonda, M.L.
Kinetic analysis and chemical modification of vitamin B6 phosphatase from human erythrocytes
J. Biol. Chem.
269
7163-7168
1994
Homo sapiens
brenda
Gao, G.J.; Fonda, M.L.
Identification of an essential cysteine residue in pyridoxal phosphatase from human erythrocytes
J. Biol. Chem.
269
8234-8239
1994
Homo sapiens
brenda
Jang, Y.M.; Kim, D.W.; Kang, T.C.; Won, M.H.; Baek, N.I.; Moon, B.J.; Choi, S.Y.; Kwon, O.S.
Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution
J. Biol. Chem.
278
50040-50046
2003
Homo sapiens (Q96GD0), Homo sapiens, Mus musculus (P60487), Mus musculus
brenda
Saraswathi, S.; Bachhawat, B.K.
Phosphatases from human brain. I. Purification and properties of pyridoxal phosphate phosphatase
J. Neurochem.
10
127-133
1963
Homo sapiens
brenda
Meisler, N.T.; Thanassi, J.W.
Pyridoxine kinase, pyridoxine phosphate phosphatase and pyridoxine phosphate oxidase activities in control and B-6-deficient rat liver and brain
J. Nutr.
110
1965-1975
1980
Rattus norvegicus
brenda
Tirrell, I.M.; Wall, J.L.; Daley, C.J.; Denial, S.J.; Tennis, F.G.; Galens, K.G.; O'Handley, S.F.
YZGD from Paenibacillus thiaminolyticus, a pyridoxal phosphatase of the HAD (haloacid dehalogenase) superfamily and a versatile member of the Nudix (nucleoside diphosphate x) hydrolase superfamily
Biochem. J.
394
665-674
2006
Paenibacillus thiaminolyticus
brenda
Tazoe, M.; Ichikawa, K.; Hoshino, T.
Purification and characterization of pyridoxine 5'-phosphate phosphatase from Sinorhizobium meliloti
Biosci. Biotechnol. Biochem.
69
2277-2284
2005
Sinorhizobium meliloti
brenda
Boe, A.S.; Bredholt, G.; Knappskog, P.M.; Storstein, A.; Vedeler, C.A.; Husebye, E.S.
Pyridoxal phosphatase is a novel cancer autoantigen in the central nervous system
Br. J. Cancer
91
1508-1514
2004
Homo sapiens (Q96GD0), Homo sapiens
brenda
Kim, D.W.; Eum, W.S.; Choi, H.S.; Kim, S.Y.; An, J.J.; Lee, S.H.; Sohn, E.J.; Hwang, S.I.; Kwon, O.S.; Kang, T.C.; Won, M.H.; Cho, S.W.; Lee, K.S.; Park, J.; Choi, S.Y.
Human brain pyridoxal-5'-phosphate phosphatase: production and characterization of monoclonal antibodies
J. Biochem. Mol. Biol.
38
703-708
2005
Bos taurus, Brachylagus idahoensis, Canis lupus familiaris, Felis catus, Gallus gallus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
brenda
Nagahashi, Y.; Tazoe, M.; Hoshino, T.
Cloning of the pyridoxine 5-phosphate phosphatase gene (pdxP) and vitamin B(6) production in pdxP recombinant Sinorhizobium meliloti
Biosci. Biotechnol. Biochem.
72
421-427
2008
Sinorhizobium meliloti (A7BK78), Sinorhizobium meliloti
brenda
Hwang, I.K.; Yoo, K.Y.; Kim, d.o.H.; Lee, B.H.; Kwon, Y.G.; Won, M.H.
Time course of changes in pyridoxal 5-phosphate (vitamin B6 active form) and its neuroprotection in experimental ischemic damage
Exp. Neurol.
206
114-125
2007
Meriones unguiculatus
brenda
Afjehi-Sadat, L.; Yang, J.W.; Pollak, A.; Kim, D.W.; Choi, S.Y.; Lubec, G.
Structural and functional analysis of hypothetical proteins in mouse hippocampus from two-dimensional gel electrophoresis
J. Proteome Res.
6
711-723
2007
Homo sapiens (Q96GD0), Mus musculus (Q8CHP8), Mus musculus
brenda
Lee, Y.P.; Kim, D.W.; Lee, M.J.; Jeong, M.S.; Kim, S.Y.; Lee, S.H.; Jang, S.H.; Park, J.; Kang, T.C.; Won, M.H.; Cho, S.W.; Kwon, O.S.; Eum, W.S.; Choi, S.Y.
Human brain pyridoxal-5-phosphate phosphatase (PLPP):protein transduction of PEP-1-PLPP into PC12 cells
BMB Rep.
41
408-413
2008
Homo sapiens (Q96GD0), Homo sapiens
brenda
Kim, J.E.; Kim, D.W.; Kwak, S.E.; Kwon, O.S.; Choi, S.Y.; Kang, T.C.
Potential role of pyridoxal-5-phosphate phosphatase/chronopin in epilepsy
Exp. Neurol.
211
128-140
2008
Rattus norvegicus
brenda
Kim, J.E.; Kim, D.W.; Kwak, S.E.; Ryu, H.J.; Yeo, S.I.; Kwon, O.S.; Choi, S.Y.; Kang, T.C.
Pyridoxal-5-phosphate phosphatase/chronophin inhibits long-term potentiation induction in the rat dentate gyrus
Hippocampus
19
1078-1089
2009
Rattus norvegicus
brenda
Kim, J.E.; Ryu, H.J.; Kim, M.J.; Kim, D.W.; Kwon, O.S.; Choi, S.Y.; Kang, T.C.
Pyridoxal-5'-phosphate phosphatase/chronophin induces astroglial apoptosis via actin-depolymerizing factor/cofilin system in the rat brain following status epilepticus
Glia
58
1937-1948
2010
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Knobloch, G.; Jabari, N.; Stadlbauer, S.; Schindelin, H.; Koehn, M.; Gohla, A.
Synthesis of hydrolysis-resistant pyridoxal 5-phosphate analogs and their biochemical and X-ray crystallographic characterization with the pyridoxal phosphatase chronophin
Bioorg. Med. Chem.
23
2819-2827
2015
Mus musculus (P60487), Mus musculus
brenda
Li, H.; Wang, Y.; Yang, H.; Liu, L.; Wang, J.; Zheng, N.
Lactoferrin induces the synthesis of vitamin B6 and protects HUVEC functions by activating PDXP and the PI3K/AKT/ERK1/2 pathway
Int. J. Mol. Sci.
20
587
2019
Homo sapiens (Q96GD0)
brenda
Kim, J.E.; Kim, Y.J.; Lee, D.S.; Kim, J.Y.; Ko, A.R.; Hyun, H.W.; Kim, M.J.; Kang, T.C.
PLPP/CIN regulates bidirectional synaptic plasticity via GluN2A interaction with postsynaptic proteins
Sci. Rep.
6
26576
2016
Homo sapiens (Q96GD0)
brenda
Dadara, A.A.; Elzoheiry, M.; El-Beshbishi, S.N.; Skelly, P.J.
Vitamin B6 acquisition and metabolism in Schistosoma mansoni
Front. Immunol.
11
622162
2020
Schistosoma mansoni (A0A3Q0KDU9)
brenda
Ciapaite, J.; van Roermund, C.; Bosma, M.; Gerrits, J.; Houten, S.; IJlst, L.; Waterham, H.; van Karnebeek, C.; Wanders, R.; Zwartkruis, F.; Jans, J.; Verhoeven-Duif, N.
Maintenance of cellular vitamin B6 levels and mitochondrial oxidative function depend on pyridoxal 5'-phosphate homeostasis protein
J. Biol. Chem.
299
105047
2023
Homo sapiens
brenda
ShuoHao, H.; Jing, L.; Jie, Z.; JianYun, Z.; LongQuan, H.
Identification and characterization of a pyridoxal 5'-phosphate phosphatase in tobacco plants
Plant Sci.
278
88-95
2019
Nicotiana tabacum
brenda
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