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Information on EC 3.1.3.74 - pyridoxal phosphatase
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3.1.3.74 pyridoxal phosphataseIUBMB 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.
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Word Map
- 3.1.3.74
- phosphatases
-
vitamer
- drug development
-
dehalogenase
-
haloacid
-
actin-depolymerizing
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
plpp/cin, plp phosphatase, pyridoxal phosphatase, pyridoxal phosphate phosphatase, plpase, pyridoxine phosphate phosphatase, pyridoxal-5'-phosphate phosphatase, pyridoxal-5'-phosphate phosphatase/chronophin, pnp phosphatase, pyridoxine 5'-phosphate phosphatase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
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
-
-
-
-
?
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
-
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
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-
?
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxamine 5'-phosphate + H2O
pyridoxamine + phosphate
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low hydrolysis rate
-
-
?
pyridoxamine 5'-phosphate + H2O
pyridoxamine + phosphate
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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
second highest specificity constant after pyridoxal 5-phosphate
-
-
?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
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the catalytic efficiency decreases in the following order: pyridoxal 5-phosphate, 4-pyridoxic acid 5-phosphate, pyridoxine 5-phosphate and pyridoxamine 5-phosphate
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-
?
additional information
?
-
-
probably plays an important role in the regulation of vitamin B6 metabolism
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-
?
additional information
?
-
vitamin B6 metabolism, catabolism of pyridoxal 5-phosphate
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-
?
additional information
?
-
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vitamin B6 metabolism, catabolism of pyridoxal 5-phosphate
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-
?
additional information
?
-
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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
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-
?
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
?
-
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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
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-
?
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
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-
?
additional information
?
-
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directly dephosphorylates actin-depolymerizing factor (ADF)/cofilin
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-
?
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
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
-
-
-
-
?
additional information
?
-
-
probably plays an important role in the regulation of vitamin B6 metabolism
-
-
?
additional information
?
-
vitamin B6 metabolism, catabolism of pyridoxal 5-phosphate
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-
?
additional information
?
-
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vitamin B6 metabolism, catabolism of pyridoxal 5-phosphate
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-
?
additional information
?
-
-
directly dephosphorylates actin-depolymerizing factor (ADF)/cofilin
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Mg2+
requirement for a divalent cation, Mg2+ is most effective in catalyzing the dephosphorylation of pyridoxal 5-phosphate
Mg2+
-
similar activation as by Co2+ and Ni2+, kinetics, probably the physiological activator
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
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EDTA
-
0.2 mM, complete inhibition in the absence of Mg2+, 50% inhibition in the presence of 1 mM Mg2+
p-nitrophenyl phosphate
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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
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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
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