Any feedback?
Information on EC 3.1.3.75 - phosphoethanolamine/phosphocholine phosphatase
for references in articles please use BRENDA:EC3.1.3.75Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Word Map
- 3.1.3.75
-
tissue-nonspecific
-
haloacid
-
dehalogenase
-
endochondral
-
mineralisation
-
srebf1
- medicine
- osteomalacia
-
hypophosphatasia
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
phospho1, phosphorylcholine phosphatase, atpecp1, phosphoethanolamine/phosphocholine phosphatase, phosphatase phospho1, 3x11a, phospho1-3a, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
PHOSPHO1 is a member of the haloacid dehalogenase superfamily of hydrolases
additional information
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
-
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
-
-
-
-
phosphoethanolamine + H2O = ethanolamine + phosphate
catalytic mechanism, overview
phosphoethanolamine + H2O = ethanolamine + phosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
52227-92-6
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
-
-
?
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
-
-
?
phosphocholine + H2O
choline + phosphate
-
PHOSPHO1 exhibits high specific activities toward phosphoethanolamine and phosphocholine, phosphocholine is hydrolyzed 1.5times slower than phosphoethanolamine
-
-
?
phosphocholine + H2O
choline + phosphate
-
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
-
-
?
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
-
-
?
additional information
?
-
-
not: diphosphate, phospho-L-serine, glycone phosphate, fructose 6-phosphate, phospho-L-tyrosine, ATP
-
-
?
additional information
?
-
three-dimensional model of PHOSPHO1, Asp-43 and Asp-123 may contribute to substrate specificity
-
-
?
additional information
?
-
-
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
?
-
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
-
-
?
additional information
?
-
-
phosphorylcholine phosphatase catalyzes the hydrolysis of 4-nitrophenylphosphate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
3.2
p-nitrophenyl phosphate
-
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
3.5
p-nitrophenyl phosphate
-
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
4.3
p-nitrophenyl phosphate
-
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
5.1
p-nitrophenyl phosphate
-
recombinant mutant enzyme D267E, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
5.4
p-nitrophenyl phosphate
-
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
7.6
p-nitrophenyl phosphate
-
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
11.5
p-nitrophenyl phosphate
-
recombinant mutant enzyme D267E, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
12.2
p-nitrophenyl phosphate
-
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
13.1
p-nitrophenyl phosphate
-
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
18.7
p-nitrophenyl phosphate
-
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
22.2
p-nitrophenyl phosphate
-
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.7
4-nitrophenyl phosphate
pH 5.0, 37°C, recombinant mutant Y82A/Y83A/Y84A
38.8
4-nitrophenyl phosphate
pH 5.0, 37°C, recombinant mutant E42A
79.6
4-nitrophenyl phosphate
pH 5.0, 37°C, recombinant mutant E43A
87.1
4-nitrophenyl phosphate
pH 5.0, 37°C, recombinant wild-type enzyme
0.2
p-nitrophenyl phosphate
-
recombinant mutant enzyme D267E, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
0.7
p-nitrophenyl phosphate
-
recombinant mutant enzyme D267E, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
1100
p-nitrophenyl phosphate
-
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
1400
p-nitrophenyl phosphate
-
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
19000
p-nitrophenyl phosphate
-
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
21000
p-nitrophenyl phosphate
-
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
22000
p-nitrophenyl phosphate
-
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
29000
p-nitrophenyl phosphate
-
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
120000
p-nitrophenyl phosphate
-
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
650000
p-nitrophenyl phosphate
-
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
1600000
p-nitrophenyl phosphate
-
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
2500000
p-nitrophenyl phosphate
-
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
5500000
p-nitrophenyl phosphate
-
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
7900000
p-nitrophenyl phosphate
-
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13.3
4-nitrophenyl phosphate
purified recombinant mutant Y82A/Y83A/Y84A, pH 5.0, 37°C
21.4
4-nitrophenyl phosphate
purified recombinant mutant E42A, pH 5.0, 37°C
57.2
4-nitrophenyl phosphate
purified recombinant wild-type enzyme, pH 5.0, 37°C
141
4-nitrophenyl phosphate
purified recombinant mutant E43A, pH 5.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
inhibition kinetics for alkylammonium compounds trimethylamine, tetramethylammonium chloride, choline, chlorocholine, hexamethonium, and decamethonium, in presence of Zn2+ or Mg2+, overview
-
additional information
additional information
-
inhibition kinetics for alkylammonium compounds trimethylamine, tetramethylammonium chloride, choline, chlorocholine, hexamethonium, and decamethonium, in presence of Zn2+ or Mg2+, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00081
2-(([3-(3-oxo-1,2-benzothiazol-2(3H)-yl)phenyl]sulfonyl)amino)benzoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0047
2-(2,3-dimethylphenyl)-6-fluoro-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.004
2-(2,5-dimethylphenyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.003
2-(2,5-dimethylphenyl)-6-fluoro-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0018
2-(3-chloro-4-fluorophenyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0052
2-(3-chlorophenyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0027
2-(3-methylphenyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0049
2-(4-fluorophenyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0013
2-(4-methylphenyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00094
2-phenyl-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0012
2-[2-(morpholin-4-yl)-5-(morpholin-4-ylsulfonyl)phenyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.011
2-[4-(dimethylamino)phenyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
2-[4-chloro-3-(morpholin-4-ylsulfonyl)phenyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0018
2-[4-methyl-3-(morpholin-4-ylsulfonyl)phenyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0075
2-[5-(morpholin-4-ylsulfonyl)-2-(pyrrolidin-1-yl)phenyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
3-(3-oxo-1,2-benzothiazol-2(3H)-yl)benzoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00094
5-fluoro-2-phenyl-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.01
6-fluoro-2-(4-fluorophenyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0067
6-fluoro-2-(4-methoxyphenyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00074
6-fluoro-2-phenyl-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0012
ethyl 4-(3-oxo-1,2-benzothiazol-2(3H)-yl)benzoate
Homo sapiens
-
pH and temperature not specified in the publication
0.00082
methyl 3-(3-oxo-1,2-benzothiazol-2(3H)-yl)benzoate
Homo sapiens
-
pH and temperature not specified in the publication
0.00056
N,N-diethyl-3-(3-oxo-1,2-benzothiazol-2(3H)-yl)benzenesulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00014
N,N-dimethyl-3-(3-oxo-1,2-benzothiazol-2(3H)-yl)benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0005
N,N-dimethyl-3-(3-oxo-1,2-benzothiazol-2(3H)-yl)benzenesulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0023
N-benzyl-3-(3-oxo-1,2-benzothiazol-2(3H)-yl)benzamide
Homo sapiens
-
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.092
purified recombinant mutant D43N enzyme fragment M19-C267, substrate O-phosphoethanolamine
0.28
purified recombinant mutant D123N enzyme fragment M19-C267, substrate O-phosphoethanolamine
0.48
substrate phosphocholine, 50 mM Hepes/NaOH buffer, pH 7.0, 37°C
1.3
-
mutant D262E, at pH 5, with p-nitrophenyl phosphate as substrate
1.5
-
mutant D267E, at pH 5, with p-nitrophenyl phosphate as substrate
10.1
purified recombinant mutant Y82A/Y83A/Y84A, pH 5.0, 37°C, substrate 4-nitrophenyl phosphate
100
-
wild-type with motif 166S, motif 242K or motif 161GDTPDSD267, at pH 5, with p-nitrophenyl phosphate as substrate and at pH 5 and pH 7.4 with phosphocholine as substrate
106.7
-
mutant K242R, at pH 5, with p-nitrophenyl phosphate as substrate
114
-
wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
121
purified recombinant mutant E43A, pH 5.0, 37°C, substrate 4-nitrophenyl phosphate
132.7
purified recombinant wild-type enzyme, pH 5.0, 37°C, substrate 4-nitrophenyl phosphate
142
-
wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
3.67
substrate phosphoethanolamine, 50 mM Hepes/NaOH buffer, pH 7.0, 37°C
4.96
purified recombinant wild-type enzyme fragment M19-C267, substrate O-phosphoethanolamine
59
purified recombinant mutant E42A, pH 5.0, 37°C, substrate 4-nitrophenyl phosphate
63.4
-
mutant G261A, at pH 5, with p-nitrophenyl phosphate as substrate
74.5
-
wild-type with motif 31DMDNT35, at pH 5, with p-nitrophenyl phosphate as substrate
75
-
wild type enzyme, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
86.9
-
wild-type with motif 31DMDNT35, at pH 7.4, with phosphocholine as substrate
88.4
-
wild-type with motif 31DMDNT35, at pH 5, with phosphocholine as substrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.7
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7.5
-
above 70% of maximum activity between pH 6 and 7.2, activity with phosphocholine declines significantly above pH 7.2, activity with phosphoethanolamine declines above pH 7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
presence in the enamel layer, ameloblast Tomes' processes, and in the walls of ameloblast secretory vesicles
brenda
from 17 days old embryonic chickens, PHOSPHO1 gene expression
brenda
from 3 weeks old male chickens, from tibia, growth plate cartilage, expression pattern, PHOSPHO1 is specifically expressed at sites of mineralization in bone and cartilage
brenda
from growth plates of proximal tibiotarsi, 3X11A expression at high levels in differentiating growth plate chondrocytes, 3X11A expression is upregulated 5fold during chondrocyte terminal differentiation and its expression is approximately 100fold higher in hypertrophic chondrocytes than in non-chondrogenic tissues
brenda
-
PHOSPHO1 expression occurs prior to E6.5 and is initially restricted to the bone collar within the mid-shaft of the diaphysis of long bones. By E11.5, expression is observed over the entire length of the diaphysis
brenda
-
by far strongest activity in roots of phosphate-starved plants
brenda
additional information
from 3 weeks old male chickens, from tibia, diaphyseal cortical and trabecular bone, expression pattern, PHOSPHO1 is specifically expressed at sites of mineralization in bone and cartilage
brenda
-
PHOSPHO1 is restricted to mineralizing regions of bone and growth plate. 120fold higher level of PHOSPHO1 expression in bone compared with liver. Enzyme present within matrix vesicles is in an active state. Present in early hypertrophic chondrocytes of the growth plate, and in osteoblasts of trabecular surfaces and infilling primary osteons of cortical bone
brenda
expressed by active alveolar bone osteoblasts and cementoblasts during cellular cementum formation
brenda
-
mineralizing osteoblast-like cells, PHOSPHO1 gene expression profile
brenda
additional information
not in heart, liver, lung, abdominal fat, kidney, skeletal and heart muscle
brenda
additional information
-
no PHOSPHO1 gene expression in non-mineralizing MG-63 osteoblast-like cells
brenda
additional information
growth on choline, betaine, dimethylglycine, or carnitine
brenda
additional information
-
growth on choline, betaine, dimethylglycine, or carnitine
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please 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 regulation of choline metabolism and consequently PchP synthesis may reflect an adaptive response of Pseudomonas aeruginosa to environmental conditions. Regulation of pchP gene expression, overview
physiological function
additional information
malfunction
both male and female Phospho1-/- mice are smaller than age-matched heterozygous and wild-type controls and exhibit growth retardation, where bones from 1-month-old male mice are shorter, phenotypes, overview
malfunction
long bones from Phospho1-/- mice do not fracture during 3-point bending but deform plastically. With dynamic loading nanoindentation the elastic modulus and hardness of Phospho1-/- tibiae are significantly lower than wild-type tibia. Mutant mice show significantly lower mineral:matrix ratios and lower carbonate substitutions in Phospho1-/- tibia, phenotype, overview
malfunction
-
both male and female Phospho1-/- mice are smaller than age-matched heterozygous and wild-type controls and exhibit growth retardation, where bones from 1-month-old male mice are shorter, phenotypes, overview
-
physiological function
PHOSPHO1 is a phosphoethanolamine/phosphocholine phosphatase involved in the generation of inorganic phosphate for bone mineralization
physiological function
possible importance of PchP in the pathogenesis of Pseudomonas aeruginosa
physiological function
role of PHOSPHO1 during endochondral ossification, overview
physiological function
calli of Phospho1-/- mice display a mild reduction of bone volume and an increase in trabecular number and a decrease in trabecular thickness and separation. There is a marked increase of osteoid volume over bone volume in the Phospho1-/- callus. Phospho1-/- fractured bone is more elastic than the wild-type bone
physiological function
cell line MC3T3-E1 clone 14 cells express high levels of Phospho1 and low levels of tissue-nonspecific alkalinephosphatase TNAP and they mineralize their matrix strongly. Clone 24 cells express high levels of TNAP and low levels of Phospho1 and mineralize their matrix poorly. Lentiviral Phospho1 overexpression in clone 24 cells results in higher Phospho1 and TNAP protein expression and increased levels of matrix mineralization. specific inhibition of Phospho1 individually reduces mineralization levels of Phospho1 overexpressing C24 cells, whereas the simultaneous addition of inhibitors of both Phospho1 and TNAP essentially abolishes matrix mineralization
physiological function
in Phospho1-/- mice, acellular cementum formation and mineralization are unaffected, whereas cellular cementum deposition increases despite delayed mineralization and cementoid. Phospho1-/- mice feature disturbances in alveolar bone mineralization. Parallel to other skeletal sites, deposition of mineral-regulating protein osteopontin is increased in alveolar bone in Phospho1-/- mice. Genetic ablation of Spp1, the gene encoding osteopontin, does not ameliorate dentoalveolar defects in Phospho1-/- mice
physiological function
-
loss of PECP1 activity exacerbates biochemical and morphological effects of phosphate starvation. Constitutive ectopic expression of PECP1 reduces phosphoethanolamine and phosphocholine levels
physiological function
Phospho1-/- mice lack sharp incisal tips, show a 25% increase in total enamel volume, and a 2fold reduction in silver grain density of von Kossa stained ground sections. Phospho1-/- mouse enamel reveals a loss of the prominent enamel prism picket fence structure, a loss of parallel crystal organization within prisms, and a 1.56fold increase in enamel prism width. Phospho1-/- mice display a significant decrease in phosphate incorporation in the enamel layer when compared to controls
physiological function
transcription of PHOSPHO1 is strongly upregulated during the terminal stages of erythropoiesis, concomitant with increased catabolism of phosphatidylcholine and phosphocholine. Depletion of PHOSPHO1 impairs differentiation of fetal erythroblasts
physiological function
transcription of PHOSPHO1 is strongly upregulated during the terminal stages of erythropoiesis, concomitant with increased catabolism of phosphatidylcholine and phosphocholine. Depletion of PHOSPHO1 impairs differentiation of fetal erythroblasts, and in adult mice depletion impairs phenylhydrazine-induced stress erythropoiesis. Loss of PHOSPHO1 also impairs phosphocholine catabolism in mouse fetal liver progenitors and results in accumulation of several lipids, and ATP production is reduced as a result of decreased oxidative phosphorylation. Glycolysis replaces oxidative phosphorylation in PHOSPHO1 knockout erythroblasts and the increased glycolysis is used for the production of serine or glycine
physiological function
-
role of PHOSPHO1 during endochondral ossification, overview
-
additional information
catalytic mechanism of phosphocholine with Pcho as the substrate, Mg2+ or Zn2+ as activators, and alkylammonium compounds as inhibitors, overview. Zn2+ induces a conformational change in the active center that is communicated to the inhibitory site, producing a compact or closed structure. In contrast, Mg2+ produces a relaxed or open conformation
additional information
-
catalytic mechanism of phosphocholine with Pcho as the substrate, Mg2+ or Zn2+ as activators, and alkylammonium compounds as inhibitors, overview. Zn2+ induces a conformational change in the active center that is communicated to the inhibitory site, producing a compact or closed structure. In contrast, Mg2+ produces a relaxed or open conformation
additional information
combination of molecular modeling, directed mutagenesis and enzyme kinetics to study the mode of interaction of PchP phosphatase with the choline moiety of the substrate
additional information
-
combination of molecular modeling, directed mutagenesis and enzyme kinetics to study the mode of interaction of PchP phosphatase with the choline moiety of the substrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PHOP1_CHICK
268
0
30443
Swiss-Prot
other Location (Reliability: 4)
PHOP1_DANRE
279
0
31403
Swiss-Prot
other Location (Reliability: 5)
PHOP1_HUMAN
267
0
29713
Swiss-Prot
Mitochondrion (Reliability: 3)
PHOP1_MOUSE
267
0
29911
Swiss-Prot
Mitochondrion (Reliability: 3)
PCHP_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
349
0
39118
Swiss-Prot
-
Q4K494_PSEF5
Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
351
0
39192
TrEMBL
-
B9SN56_RICCO
274
0
30918
TrEMBL
other Location (Reliability: 4)
B9T693_RICCO
263
0
29717
TrEMBL
Secretory Pathway (Reliability: 5)
B9RKA9_RICCO
253
0
28460
TrEMBL
other Location (Reliability: 3)
Q88CQ0_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
351
0
39088
TrEMBL
-
B9SN55_RICCO
274
0
31080
TrEMBL
other Location (Reliability: 4)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28600
x * 33000, recombinant PHOSPHO1, SDS-PAGE, x * 28600, x * 30400, alternative transcripts for PHOSPHO1 in growth cartilage, Western blot analysis
30400
x * 33000, recombinant PHOSPHO1, SDS-PAGE, x * 28600, x * 30400, alternative transcripts for PHOSPHO1 in growth cartilage, Western blot analysis
32000
33000
x * 33000, recombinant PHOSPHO1, SDS-PAGE, x * 28600, x * 30400, alternative transcripts for PHOSPHO1 in growth cartilage, Western blot analysis
37000
2 * 37000, about, recombinant His6-tagged enzyme, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
1 * 32000, monomer-dimer equilibrium, both the monomer and the dimer are active
additional information
?
x * 33000, recombinant PHOSPHO1, SDS-PAGE, x * 28600, x * 30400, alternative transcripts for PHOSPHO1 in growth cartilage, Western blot analysis
dimer
2 * 32000, monomer-dimer equilibrium, both the monomer and the dimer are active
dimer
2 * 37000, about, recombinant His6-tagged enzyme, SDS-PAGE
additional information
structure motif analysis using the amino acid sequence structural modelling and ligand docking
additional information
-
structure motif analysis using the amino acid sequence structural modelling and ligand docking
additional information
the active enzyme is a dimer, enzyme structure molecular modeling and molecular dynamics, with substrate and inhibitor binding sites, overview
additional information
-
the active enzyme is a dimer, enzyme structure molecular modeling and molecular dynamics, with substrate and inhibitor binding sites, overview
additional information
the enzyme contains three HAD motifs, sequence comparisons, overview
additional information
-
the enzyme contains three HAD motifs, sequence comparisons, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
D31 is phosphorylated during phosphoester hydrolysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, sitting drop vapour diffusion method, 250 nl of 10 mg/ml protein in 200 mM NaCl, 10 mM Tris-HCl, pH 8.0, are mixed with 250 nl well solution and are equilibrated against 0.5 ml well solution containing 0.1 M Bis-Tris, pH 5.5, 0.2 M MgCl2, 25% PEG 3350, producing clustered plate-like microcrystals, or by microbatch method mixing 0.001 ml of protein solution containing 10 mg/ml in 200 mM NaCl, 20 mM Bis-Tris, pH 5.5, with 0.002 ml precipitant solution, cryoprotection by a quick soak in 0.1 M Bis-Tris pH 5.5, 0.2 M MgCl2, 25% PEG 3350, 15% glycerol, X-ray diffraction structure determination and analysis at 2.7 A resolution
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D123N
site-directed mutagenesis, the mutant enzyme fragment shows reduced activity compared to the wild-type enzyme fragment
D43N
site-directed mutagenesis, the mutant enzyme fragment shows reduced activity compared to the wild-type enzyme fragment
D262E
D267E
S166T
T35S
additional information
D262E
-
mutant shows activity less than 2% with respect to native recombinant enzyme
D267E
-
mutant shows activity less than 2% with respect to native recombinant enzyme and is not activated by Cu2+
S166T
-
mutant shows activity less than 2% with respect to native recombinant enzyme
T35S
-
mutant shows activity less than 2% with respect to native recombinant enzyme
additional information
generation of phospho1-R74X-null mutant, i.e. Phospho1-/-, mice by N-ethyl-N-nitrosourea mutagenesis
additional information
generation of phospho1-R74X-null mutant, i.e. Phospho1-/-, mice by N-ethyl-N-nitrosourea mutagenesis
additional information
-
generation of phospho1-R74X-null mutant, i.e. Phospho1-/-, mice by N-ethyl-N-nitrosourea mutagenesis
-
additional information
-
Tn5-751 transposon mutagenesis is used to construct an enzyme-deficient, inactive mutant JUF8-00 of Pseudomonas aeruginosa, the mutant can be complemented by expression of the wild-type enzyme
additional information
site-directed mutagenesis of the aspartyl, D31, D33, and threonyl, T35, residues of motif I, of the seryl, S166, residue of motif II, and of the lysyl, K242, glycyl, G261, and aspartyl residues, D262, D265, and D267, of motif III
additional information
-
site-directed mutagenesis of the aspartyl, D31, D33, and threonyl, T35, residues of motif I, of the seryl, S166, residue of motif II, and of the lysyl, K242, glycyl, G261, and aspartyl residues, D262, D265, and D267, of motif III
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM Tris-HCl, pH 8, containing 30% glycerol, more than 1 year, no loss of activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from solubilized inclusion bodies, ion-exchange chromatography (Q-Sepharose), dialysis, gel filtration
recombinant enzyme from Escherichia coli by chitin affinity chromatography
-
recombinant His-tagged wild-type and mutant fragments M19-C267 from Escherichia coli by nickel affinity chromatography to homogeneity
recombinant N-terminally His6-tagged PchP from Escherichia coli by nickel affinity chromatography
recombinant PchP from Escherichia coli, as an N-terminal fusion to intein or a histidine tag, in the folded state
recombinant PHOSPHO1
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type and mutant fragment comprising residues M19-C267 in Escherichia coli
expression of wild-type and mutant enzymes in Escherichia coli strain BL21
gene PA5292, expression in Escherichia coli, expression in and complementation of a Pseudomonas aeruginosa mutant strain JUF8-00
-
gene pchP, expression of His-tagged enzyme in Escherichia coli strain BL21
gene pchP, phylogenetic tree, regulation of pchP gene expression is under the control of GbdR and NtrC. PchP expression in Escherichia coli as an N-terminal fusion to intein or a histidine tag
gene pchP327, recombinant expression with a N-terminal fusion to an MGSSHHHHHHSSGLVPRGSH tag in Escherichia coli BL21, expression of N-terminal His6-tagged PchP in Escherichia coli
overexpression of the wild-type and mutant enzymes in Escherichia coli ER2566, transformed with pTY-pchP327, pTYpchP349, or the mutated expression plasmids
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
dimethylglycine is likely the metabolite directly involved in the induction of PchP. Induction of pchP transcription by glycine betaine, a product of choline oxidation, via betaine aldehyde, mediated by GbdR, an AraC family transcription factor
PECP1 expression is tightly regulated by phosphate supply. The transcript level increases strongly after onset of phosphate deprivation
-
the regulation of pchP gene expression is under the control of GbdR and NtrC
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
may have implications for the diagnosis of hypophosphatasia and treatment of bone mineralization abnormalities such as osteomalacia and pathological soft-tissue ossification, a process clinically significant in atheroscleosis and heart failure
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Roberts, S.J.; Stewart, A.J.; Sadler, P.J.; Farquharson, C.
Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities
Biochem. J.
382
59-65
2004
Homo sapiens
brenda
Houston, B.; Seawright, E.; Jefferies, D.; Hoogland, E.; Lester, D.; Whitehead, C.; Farquharson, C.
Identification and cloning of a novel phosphatase expressed at high levels in differentiating growth plate chondrocytes
Biochim. Biophys. Acta
1448
500-506
1999
Gallus gallus (O73884)
brenda
Houston, B.; Stewart, A.J.; Farquharson, C.
PHOSPHO1-a novel phosphatase specifically expressed at sites of mineralisation in bone and cartilage
Bone
34
629-637
2004
Homo sapiens, Gallus gallus (O73884)
brenda
Stewart, A.J.; Schmid, R.; Blindauer, C.A.; Paisey, S.J.; Farquharson, C.
Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily
Protein Eng.
16
889-895
2003
Homo sapiens (Q8TCT1), Homo sapiens
brenda
Roberts, S.J.; Stewart, A.J.; Schmid, R.; Blindauer, C.A.; Bond, S.R.; Sadler, P.J.; Farquharson, C.
Probing the substrate specificities of human PHOSPHO1 and PHOSPHO2
Biochim. Biophys. Acta
1752
73-82
2005
Homo sapiens (Q8TCT1), Homo sapiens
brenda
Massimelli, M.J.; Beassoni, P.R.; Forrellad, M.A.; Barra, J.L.; Garrido, M.N.; Domenech, C.E.; Lisa, A.T.
Identification, cloning, and expression of Pseudomonas aeruginosa phosphorylcholine phosphatase gene
Curr. Microbiol.
50
251-256
2005
Pseudomonas aeruginosa
brenda
Stewart, A.J.; Roberts, S.J.; Seawright, E.; Davey, M.G.; Fleming, R.H.; Farquharson, C.
The presence of PHOSPHO1 in matrix vesicles and its developmental expression prior to skeletal mineralization
Bone
39
1000-1007
2006
Gallus gallus
brenda
Beassoni, P.R.; Otero, L.H.; Massimelli, M.J.; Lisa, A.T.; Domenech, C.E.
Critical active-site residues identified by site-directed mutagenesis in Pseudomonas aeruginosa phosphorylcholine phosphatase, a new member of the haloacid dehalogenases hydrolase superfamily
Curr. Microbiol.
53
534-539
2006
Pseudomonas aeruginosa
brenda
Roberts, S.; Narisawa, S.; Harmey, D.; Millan, J.L.; Farquharson, C.
Functional involvement of PHOSPHO1 in matrix vesicle-mediated skeletal mineralization
J. Bone Miner. Res.
22
617-627
2007
Gallus gallus, Homo sapiens, Mus musculus
brenda
Beassoni, P.R.; Otero, L.H.; Lisa, A.T.; Domenech, C.E.
Using a molecular model and kinetic experiments in the presence of divalent cations to study the active site and catalysis of Pseudomonas aeruginosa phosphorylcholine phosphatase
Biochim. Biophys. Acta
1784
2038-2044
2008
Pseudomonas aeruginosa
brenda
Roberts, S.J.; Owen, H.C.; Farquharson, C.
Identification of a novel splice variant of the haloacid dehalogenase: PHOSPHO1
Biochem. Biophys. Res. Commun.
371
872-876
2008
Homo sapiens
brenda
Otero, L.H.; Beassoni, P.R.; Lisa, A.T.; Domenech, C.E.
Transition from octahedral to tetrahedral geometry causes the activation or inhibition by Znf2+ of Pseudomonas aeruginosa phosphorylcholine phosphatase
Biometals
23
307-314
2010
Pseudomonas aeruginosa
brenda
MacRae, V.E.; Davey, M.G.; McTeir, L.; Narisawa, S.; Yadav, M.C.; Millan, J.L.; Farquharson, C.
Inhibition of PHOSPHO1 activity results in impaired skeletal mineralization during limb development of the chick
Bone
46
1146-1155
2010
Gallus gallus (O73884)
brenda
Beassoni, P.R.; Berti, F.P.; Otero, L.H.; Risso, V.A.; Ferreyra, R.G.; Lisa, A.T.; Domenech, C.E.; Ermacora, M.R.
Preparation and biophysical characterization of recombinant Pseudomonas aeruginosa phosphorylcholine phosphatase
Protein Expr. Purif.
71
153-159
2010
Pseudomonas aeruginosa (Q9HTR2), Pseudomonas aeruginosa
brenda
Otero, L.H.; Beassoni, P.R.; Domenech, C.E.; Lisa, A.T.; Albert, A.
Crystallization and preliminary X-ray diffraction analysis of Pseudomonas aeruginosa phosphorylcholine phosphatase
Acta Crystallogr. Sect. F
66
957-960
2010
Pseudomonas aeruginosa (Q9HTR2), Pseudomonas aeruginosa
brenda
Beassoni, P.R.; Otero, L.H.; Boetsch, C.; Domenech, C.E.; Gonzalez-Nilo, F.D.; Lisa, A.T.
Site-directed mutations and kinetic studies show key residues involved in alkylammonium interactions and reveal two sites for phosphorylcholine in Pseudomonas aeruginosa phosphorylcholine phosphatase
Biochim. Biophys. Acta
1814
858-863
2011
Pseudomonas aeruginosa (Q9HTR2), Pseudomonas aeruginosa
brenda
May, A.; Spinka, M.; Koeck, M.
Arabidopsis thaliana PECP1 - Enzymatic characterization and structural organization of the first plant phosphoethanolamine/phosphocholine phosphatase
Biochim. Biophys. Acta
1824
319-325
2012
Arabidopsis thaliana (Q9FZ62), Arabidopsis thaliana
brenda
Huesa, C.; Yadav, M.; Finnilae, M.; Goodyear, S.; Robins, S.; Tanner, K.; Aspden, R.; Millan, J.; Farquharson, C.
PHOSPHO1 is essential for mechanically competent mineralization and the avoidance of spontaneous fractures
Bone
48
1066-1074
2011
Mus musculus (Q8R2H9)
brenda
Domenech, C.E.; Otero, L.H.; Beassoni, P.R.; Lisa, A.T.
Phosphorylcholine phosphatase: A peculiar enzyme of Pseudomonas aeruginosa
Enzyme Res.
2011
561841
2011
Pseudomonas aeruginosa (Q9HTR2), Pseudomonas aeruginosa
brenda
Otero, L.H.; Beassoni, P.R.; Boetsch, C.; Lisa, A.T.; Domenech, C.E.
Different effects of Mg2+ and Zn2+ on the two sites for alkylammonium compounds in Pseudomonas aeruginosa phosphorylcholine phosphatase
Enzyme Res.
2011
918283
2011
Pseudomonas aeruginosa (Q9HTR2), Pseudomonas aeruginosa
brenda
Yadav, M.; Simao, A.; Narisawa, S.; Huesa, C.; McKee, M.; Farquharson, C.; Millan, J.
Loss of skeletal mineralization by the simultaneous ablation of PHOSPHO1 and alkaline phosphatase function: A unified model of the mechanisms of initiation of skeletal calcification
J. Bone Miner. Res.
26
286-297
2011
Mus musculus (Q8R2H9), Mus musculus C57BL/6 (Q8R2H9)
brenda
Bravo, Y.; Teriete, P.; Dhanya, R.P.; Dahl, R.; Lee, P.S.; Kiffer-Moreira, T.; Ganji, S.R.; Sergienko, E.; Smith, L.H.; Farquharson, C.; Millan, J.L.; Cosford, N.D.
Design, synthesis and evaluation of benzoisothiazolones as selective inhibitors of PHOSPHO1
Bioorg. Med. Chem. Lett.
24
4308-4311
2014
Homo sapiens
brenda
Huesa, C.; Houston, D.; Kiffer-Moreira, T.; Yadav, M.M.; Millan, J.L.; Farquharson, C.
The functional co-operativity of tissue-nonspecific alkaline phosphatase (TNAP) and PHOSPHO1 during initiation of skeletal mineralization
Biochem. Biophys. Rep.
4
196-201
2015
Mus musculus (Q8R2H9)
brenda
Huang, N.J.; Lin, Y.C.; Lin, C.Y.; Pishesha, N.; Lewis, C.A.; Freinkman, E.; Farquharson, C.; Millan, J.L.; Lodish, H.
Enhanced phosphocholine metabolism is essential for terminal erythropoiesis
Blood
131
2955-2966
2018
Homo sapiens (Q8TCT1), Homo sapiens, Mus musculus (Q8R2H9), Mus musculus
brenda
Morcos, M.W.; Al-Jallad, H.; Li, J.; Farquharson, C.; Millan, J.L.; Hamdy, R.C.; Murshed, M.
PHOSPHO1 is essential for normal bone fracture healing an animal study
Bone Joint Res.
7
397-405
2018
Mus musculus (Q8R2H9)
brenda
Pandya, M.; Rosene, L.; Farquharson, C.; Millan, J.; Diekwisch, T.
Intravesicular phosphatase PHOSPHO1 function in enamel mineralization and prism formation
Front. Physiol.
8
805
2017
Mus musculus (Q8R2H9)
brenda
Zweifler, L.E.; Ao, M.; Yadav, M.; Kuss, P.; Narisawa, S.; Kolli, T.N.; Wimer, H.F.; Farquharson, C.; Somerman, M.J.; Millan, J.L.; Foster, B.L.
Role of PHOSPHO1 in periodontal development and function
J. Dent. Res.
95
742-751
2016
Mus musculus (Q8R2H9)
brenda
Tannert, M.; May, A.; Ditfe, D.; Berger, S.; Balcke, G.U.; Tissier, A.; Koeck, M.
Pi starvation-dependent regulation of ethanolamine metabolism by phosphoethanolamine phosphatase PECP1 in Arabidopsis roots
J. Exp. Bot.
69
467-481
2018
Arabidopsis thaliana
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.1.3.75)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
