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Information on EC 3.1.3.75 - phosphoethanolamine/phosphocholine phosphatase
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3.1.3.75 phosphoethanolamine/phosphocholine phosphataseIUBMB Comments
Requires active site Mg2+ but also works, to a lesser extent, with Co2+ and Mn2+. The enzyme is highly specific for phosphoethanolamine and phosphocholine.
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Word Map
- 3.1.3.75
-
tissue-nonspecific
-
haloacid
-
dehalogenase
-
endochondral
-
mineralisation
-
srebf1
- medicine
- osteomalacia
-
hypophosphatasia
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
phospho1, phosphorylcholine phosphatase, atpecp1, phosphoethanolamine/phosphocholine phosphatase, phosphatase phospho1, 3x11a, phospho1-3a, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PChP
phosphatase PHOSPHO1
PHOSPHO1
phosphoethanolamine/phosphocholine phosphatase
phosphorylcholine phosphatase
additional information
phosphorylcholine phosphatase
-
additional information
PHOSPHO1 is a member of the haloacid dehalogenase superfamily of hydrolases
additional information
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PHOSPHO1 is a member of the haloacid dehalogenase superfamily of hydrolases
additional information
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PHOSPHO1 is a member of the haloacid dehalogenase superfamily of Mg2+-dependent hydrolases
additional information
PHOSPHO1 belongs to the haloacid dehalogenase superfamily
additional information
PHOSPHO1 is a member of the haloacid dehalogenase superfamily of magnesium-dependent hydrolases
additional information
the phosphatase PHOSPHO1 is a member of the haloacid dehalogenase, HAD, superfamily of Mg2+-dependent hydrolases
additional information
the phosphatase PHOSPHO1 is a member of the haloacid dehalogenase, HAD, superfamily of Mg2+-dependent hydrolases
-
additional information
the enzyme belongs to the haloacid dehalogenase superfamily
additional information
the enzyme belongs to the haloacid dehalogenase superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
O-phosphoethanolamine + H2O = ethanolamine + phosphate
requires active site Mg2+ but also works, to a lesser extend, with Co2+ and Mn2+, the enzyme is highly specific for phosphoethanolamine and phosphocholine
-
O-phosphoethanolamine + H2O = ethanolamine + phosphate
residues D32 and D203 of catalytic motifs are essential for catalytic activity, residues D43 and D123 are important for substrate binding and specificity
O-phosphoethanolamine + H2O = ethanolamine + phosphate
-
-
-
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phosphocholine + H2O = choline + phosphate
requires active site Mg2+ but also works, to a lesser extend, with Co2+ and Mn2+, the enzyme is highly specific for phosphoethanolamine and phosphocholine
-
phosphocholine + H2O = choline + phosphate
catalytic mechanism, overview
phosphocholine + H2O = choline + phosphate
-
-
-
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phosphoethanolamine + H2O = ethanolamine + phosphate
catalytic mechanism, overview
phosphoethanolamine + H2O = ethanolamine + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
phosphoethanolamine phosphohydrolase
Requires active site Mg2+ but also works, to a lesser extent, with Co2+ and Mn2+. The enzyme is highly specific for phosphoethanolamine and phosphocholine.
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CAS REGISTRY NUMBER
COMMENTARY
52227-92-6
-
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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
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
O-phosphoethanolamine + H2O
ethanolamine + phosphate
-
likely a natural substrate, phosphoethanolamine metabolism, PHOSPHO1 is upregulated in mineralizing cells, enzyme is implicated in the generation of phosphate for matrix mineralization
-
-
?
O-phosphoethanolamine + H2O
ethanolamine + phosphate
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PHOSPHO1 exhibits high specific activities toward phosphoethanolamine and phosphocholine, phosphoethanolamine is hydrolyzed 1.5times faster than phosphocholine
-
-
?
p-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
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-
-
?
phosphocholine + H2O
choline + phosphate
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likely a natural substrate, phosphocholine metabolism, PHOSPHO1 is upregulated in mineralizing cells, enzyme is implicated in the generation of phosphate for matrix mineralization
-
-
?
phosphocholine + H2O
choline + phosphate
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PHOSPHO1 exhibits high specific activities toward phosphoethanolamine and phosphocholine, phosphocholine is hydrolyzed 1.5times slower than phosphoethanolamine
-
-
?
phosphocholine + H2O
choline + phosphate
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D31, D33, D262, D267, S166 or K242 are important residues for catalysis
-
-
?
phosphocholine + H2O
choline + phosphate
substrate docking assay and structure, the oxygen atom of the carboxyl group of D31 is involved in nucleophilic attack on the phosphorus atom of the substrate, the D33 residue is important for catalysis because it participates in the phosphorylation of D31, overview. D262 and D267 are the aspartyl residues involved in catalysis
-
-
?
phosphoethanolamine + H2O
ethanolamine + phosphate
-
-
-
?
phosphoethanolamine + H2O
ethanolamine + phosphate
substrate docking assay and structure, the oxygen atom of the carboxyl group of D31 is involved in nucleophilic attack on the phosphorus atom of the substrate, the D33 residue is important for catalysis because it participates in the phosphorylation of D31, overview. D262 and D267 are the aspartyl residues involved in catalysis
-
-
?
additional information
?
-
no substrates are 4-nitrophenyl phosphate, diphosphate, phospho-L-serine, phospho-L-tyrosine
-
-
?
additional information
?
-
-
no substrates are 4-nitrophenyl phosphate, diphosphate, phospho-L-serine, phospho-L-tyrosine
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-
?
additional information
?
-
-
phosphoethanolamine, but not phosphocholine is the substrate of PECP1 in vivo
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-
?
additional information
?
-
3X11A participates in a biochemical pathway that is particularly active in differentiating chondrocytes, it may be involved in the generation of inorganic phosphate during matrix mineralization
-
-
?
additional information
?
-
PHOSPHO1 may be involved in the mineralization process, plays a role in bone and cartilage matrix mineralization
-
-
?
additional information
?
-
PHOSPHO1 expression is upregulated in mineralizing cells and is implicated in the generation of inorganic phosphate for matrix mineralization
-
-
?
additional information
?
-
-
PHOSPHO1 expression is upregulated in mineralizing cells and is implicated in the generation of inorganic phosphate for matrix mineralization
-
-
?
additional information
?
-
-
PHOSPHO1 may be involved in the mineralization process
-
-
?
additional information
?
-
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not: diphosphate, phospho-L-serine, glycone phosphate, fructose 6-phosphate, phospho-L-tyrosine, ATP
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-
?
additional information
?
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three-dimensional model of PHOSPHO1, Asp-43 and Asp-123 may contribute to substrate specificity
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-
?
additional information
?
-
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three-dimensional model of PHOSPHO1, Asp-43 and Asp-123 may contribute to substrate specificity
-
-
?
additional information
?
-
high substrate specificity of PHOSPHO1, residual activity with beta-glycerol phosphate, 4-nitrophenyl phosphate, and ribose 5-phosphate, no activity with phospho-L-serine, diphosphate, fructose 6-phosphate, phospho-L-tyrosine, and ATP, overview
-
-
?
additional information
?
-
-
high substrate specificity of PHOSPHO1, residual activity with beta-glycerol phosphate, 4-nitrophenyl phosphate, and ribose 5-phosphate, no activity with phospho-L-serine, diphosphate, fructose 6-phosphate, phospho-L-tyrosine, and ATP, overview
-
-
?
additional information
?
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phosphorylcholine phosphatase catalyzes the hydrolysis of 4-nitrophenylphosphate
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-
?
additional information
?
-
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phosphorylcholine phosphatase catalyzes the hydrolysis of 4-nitrophenylphosphate
-
-
?
additional information
?
-
phosphorylcholine phosphatase catalyzes the hydrolysis of 4-nitrophenylphosphate
-
-
?
additional information
?
-
-
phosphorylcholine phosphatase catalyzes the hydrolysis of 4-nitrophenylphosphate
-
-
?
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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
O-phosphoethanolamine + H2O
ethanolamine + phosphate
-
likely a natural substrate, phosphoethanolamine metabolism, PHOSPHO1 is upregulated in mineralizing cells, enzyme is implicated in the generation of phosphate for matrix mineralization
-
-
?
phosphocholine + H2O
choline + phosphate
-
likely a natural substrate, phosphocholine metabolism, PHOSPHO1 is upregulated in mineralizing cells, enzyme is implicated in the generation of phosphate for matrix mineralization
-
-
?
phosphoethanolamine + H2O
ethanolamine + phosphate
-
-
-
?
additional information
?
-
-
phosphoethanolamine, but not phosphocholine is the substrate of PECP1 in vivo
-
-
?
additional information
?
-
3X11A participates in a biochemical pathway that is particularly active in differentiating chondrocytes, it may be involved in the generation of inorganic phosphate during matrix mineralization
-
-
?
additional information
?
-
PHOSPHO1 may be involved in the mineralization process, plays a role in bone and cartilage matrix mineralization
-
-
?
additional information
?
-
PHOSPHO1 expression is upregulated in mineralizing cells and is implicated in the generation of inorganic phosphate for matrix mineralization
-
-
?
additional information
?
-
-
PHOSPHO1 expression is upregulated in mineralizing cells and is implicated in the generation of inorganic phosphate for matrix mineralization
-
-
?
additional information
?
-
-
PHOSPHO1 may be involved in the mineralization process
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Cu2+
Fe2+
divalent metal ions required, highest activity with 1.5 mM Mg2+
Mg2+
Mn2+
-
stimulates to a lesser extend than Mg2+, higher activity with phosphocholine than with phosphoethanolamine in the presence of Co2+ and Mn2+ most probably due to an allosteric effect caused by a difference in the metal-binding properties of each enzyme-substrate complex
Ni2+
Zn2+
additional information
Co2+
divalent metal ions required, highest activity with 1.5 mM Mg2+
Co2+
-
stimulates to a lesser extend than Mg2+, higher activity with phosphocholine than with phosphoethanolamine in the presence of Co2+ and Mn2+ most probably due to an allosteric effect caused by a difference in the metal-binding properties of each enzyme-substrate complex
Cu2+
-
activator, the wild type recombinant phosphorylcholine phosphatase has higher affinity for Zn2+ and Cu2+ than for Mg2+, Cu2+ is able to diminish almost 3times the affinity of the enzyme for p-nitrophenyl with respect to the addition of Zn2+ or Mg2+
Cu2+
activates, Zn2+ and Cu2+ are better activators than Mg2+ at pH 5.0
Mg2+
divalent metal ions required, highest activity with 1.5 mM Mg2+
Mg2+
-
activator, the wild type recombinant phosphorylcholine phosphatase has higher affinity for Zn2+ and Cu2+ than for Mg2+
Mg2+
activates, Zn2+ and Cu2+ are better activators than Mg2+ at pH 5.0
Mg2+
Mg2+ is an equal activator for the enzyme at pH 5.0 and at pH 7.4. Mg2+ produces a relaxed or open conformation
Ni2+
divalent metal ions required, highest activity with 1.5 mM Mg2+
Zn2+
-
activator, the wild type recombinant phosphorylcholine phosphatase has higher affinity for Zn2+ and Cu2+ than for Mg2+
Zn2+
activates, Zn2+ and Cu2+ are better activators than Mg2+ at pH 5.0. Zn2+ induces a pH-dependent a conformational change in the active center, at pH 5.0, that is communicated to the inhibitory site, producing a compact or closed structure. However, at pH 7.4, this effect is not observed because to the hydrolysis of the [Zn2+L-12 L02(H2O)2] complex, which causes a change from octahedral to tetrahedral in the metal coordination geometry
Zn2+
Zn2+ is an activator at pH 5.0 but an reversible inhibitor at pH 7.4. Activation or inhibition of PchP by Zn2+ is caused by the transition from octahedral to tetrahedral geometry in the coordination sphere of the metal ion
additional information
Zn2+ has 1000fold stronger affinity for PchP compared to Mg2+
additional information
-
Zn2+ has 1000fold stronger affinity for PchP compared to Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-[2-(morpholin-4-yl)-5-(morpholin-4-ylsulfonyl)phenyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[5-(morpholin-4-ylsulfonyl)-2-(pyrrolidin-1-yl)phenyl]-1,2-benzothiazol-3(2H)-one
-
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betaine
-
32% inhibition of wild-type enzyme in vivo at 5 mM, at lower concentrations betaine induces the enzyme expression in vivo
choline
-
12% inhibition of wild-type enzyme in vivo at 5 mM, at lower concentrations choline induces the enzyme expression in vivo
lansoprazole
-
1 mM decreases calcifying potential in the presence of phosphoethanolamine by 10%
lansoprazole
-
inhibits the mineralization of matrix vesicles from tissue-nonspecific alkaline phosphatase deficient Akp2(-/-) osteoblasts by 56.8%
phosphocholine
substrate inhibition at high concentration
SCH202676
-
1 mM decreases calcifying potential in the presence of phosphoethanolamine by 10%
SCH202676
-
inhibits the mineralization of matrix vesicles from tissue-nonspecific alkaline phosphatase deficient Akp2(-/-) osteoblasts by 70.7%
Zn2+
inhibition produced by Zn2+ at pH 7.4 represents a change from octahedral to tetrahedral coordination geometry which is produced by hydrolysis of the Zn-hexacoordinated complex
Zn2+
Zn2+ is an activator at pH 5.0 but an reversible inhibitor at pH 7.4. Activation or inhibition of PchP by Zn2+ is caused by the transition from octahedral to tetrahedral geometry in the coordination sphere of the metal ion
additional information
-
no inhibition by high concentrations of phosphorylcholine
-
additional information
the enzyme contains two sites for alkylammonium compounds, one of which is located in the catalytic site near the metal ion-phosphoester pocket, while the other one is located in an inhibitory site responsible for the binding of the alkylammonium moiety. Both sites are close to each other and interact through the residues 42E, 43E and 82YYY84
-
additional information
-
the enzyme contains two sites for alkylammonium compounds, one of which is located in the catalytic site near the metal ion-phosphoester pocket, while the other one is located in an inhibitory site responsible for the binding of the alkylammonium moiety. Both sites are close to each other and interact through the residues 42E, 43E and 82YYY84
-
additional information
inhibition mechanism of alkylammonium compounds, enzyme PchP contains two sites for alkylammonium compounds: one in the catalytic site near the metal ion-phosphoester pocket, and the other in an inhibitory site responsible for the binding of the alkylammonium moiety
-
additional information
-
inhibition mechanism of alkylammonium compounds, enzyme PchP contains two sites for alkylammonium compounds: one in the catalytic site near the metal ion-phosphoester pocket, and the other in an inhibitory site responsible for the binding of the alkylammonium moiety
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbic acid
-
increases PHOSPHO1 expression in matrix vesicles after 12 days in culture
additional information
-
PHOSPHO1 expression is not influenced by presence of tissue-nonspecific alkaline phosphatase
-
additional information
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the enzyme is induced by growth on choline, betaine, dimethylglycine, or carnitine, choline and betaine are inhibitory at high concentrations
-
additional information
-
signal peptide alters the low-affinity site of recombinant PChP expressed in Escherichia coli
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Diabetes Mellitus, Type 2
DNA methylation of loci within ABCG1 and PHOSPHO1 in blood DNA is associated with future type 2 diabetes risk.
Diabetes Mellitus, Type 2
Epigenome-wide association of DNA methylation markers in peripheral blood from Indian Asians and Europeans with incident type 2 diabetes: a nested case-control study.
Fractures, Spontaneous
A distinctive patchy osteomalacia characterises Phospho1-deficient mice.
Fractures, Spontaneous
Phospho1 deficiency transiently modifies bone architecture yet produces consistent modification in osteocyte differentiation and vascular porosity with ageing.
Fractures, Spontaneous
PHOSPHO1 is essential for mechanically competent mineralization and the avoidance of spontaneous fractures.
Infections
Preparation and biophysical characterization of recombinant Pseudomonas aeruginosa phosphorylcholine phosphatase.
Infections
Pseudomonas aeruginosa cholinesterase and phosphorylcholine phosphatase: two enzymes contributing to corneal infection.
Insulin Resistance
Phosphocholine accumulation and PHOSPHO1 depletion promote adipose tissue thermogenesis.
Metabolic Syndrome
Phosphocholine accumulation and PHOSPHO1 depletion promote adipose tissue thermogenesis.
Obesity
PHOSPHO1 Gene DNA Methylations Are Associated with a Change in HDL-C Response to Simvastatin Treatment.
Obesity
Phosphocholine accumulation and PHOSPHO1 depletion promote adipose tissue thermogenesis.
Osteoarthritis
Lansoprazole is an uncompetitive inhibitor of tissue-nonspecific alkaline phosphatase.
Osteogenesis Imperfecta
An investigation of the mineral in ductile and brittle cortical mouse bone.
Osteomalacia
Phospho1 deficiency transiently modifies bone architecture yet produces consistent modification in osteocyte differentiation and vascular porosity with ageing.
phosphoethanolamine/phosphocholine phosphatase deficiency
Ablation of Osteopontin Improves the Skeletal Phenotype of Phospho1(-/-) Mice.
phosphoethanolamine/phosphocholine phosphatase deficiency
Phospho1 deficiency transiently modifies bone architecture yet produces consistent modification in osteocyte differentiation and vascular porosity with ageing.
phosphoethanolamine/phosphocholine phosphatase deficiency
PHOSPHO1 is essential for normal bone fracture healing: An Animal Study.
Pseudomonas Infections
Preparation and biophysical characterization of recombinant Pseudomonas aeruginosa phosphorylcholine phosphatase.
Scoliosis
Phospho1 deficiency transiently modifies bone architecture yet produces consistent modification in osteocyte differentiation and vascular porosity with ageing.
Starvation
Expression Profiles of 2 Phosphate Starvation-Inducible Phosphocholine/Phosphoethanolamine Phosphatases, PECP1 and PS2, in Arabidopsis.
Starvation
Pi starvation-dependent regulation of ethanolamine metabolism by phosphoethanolamine phosphatase PECP1 in Arabidopsis roots.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.51
4-nitrophenyl phosphate
pH 5.0, 37°C, recombinant mutant Y82A/Y83A/Y84A
0.56
4-nitrophenyl phosphate
pH 5.0, 37°C, recombinant mutant E43A
1.5 - 2
4-nitrophenyl phosphate
pH 5.0, 37°C, recombinant wild-type enzyme
1.9
4-nitrophenyl phosphate
pH 5.0, 37°C, recombinant mutant E42A
1.4
p-nitrophenyl phosphate
-
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
2.5
p-nitrophenyl phosphate
-
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
2.6
p-nitrophenyl phosphate
-
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+