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Information on EC 3.1.3.75 - phosphoethanolamine/phosphocholine phosphatase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9FZ62

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EC Tree
IUBMB 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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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9FZ62
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
phospho1, phosphorylcholine phosphatase, atpecp1, phosphoethanolamine/phosphocholine phosphatase, phosphatase phospho1, 3x11a, phospho1-3a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
52227-92-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphocholine + H2O
choline + phosphate
show the reaction diagram
-
-
-
?
phosphoethanolamine + H2O
ethanolamine + phosphate
show the reaction diagram
-
-
-
?
O-phosphoethanolamine + H2O
ethanolamine + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphocholine + H2O
choline + phosphate
show the reaction diagram
-
-
-
?
phosphoethanolamine + H2O
ethanolamine + phosphate
show the reaction diagram
-
-
-
?
O-phosphoethanolamine + H2O
ethanolamine + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
phosphoethanolamine, but not phosphocholine is the substrate of PECP1 in vivo
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
divalent metal ions required, highest activity with 1.5 mM Mg2+
Fe2+
divalent metal ions required, highest activity with 1.5 mM Mg2+
Mg2+
divalent metal ions required, highest activity with 1.5 mM Mg2+
Ni2+
divalent metal ions required, highest activity with 1.5 mM Mg2+
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.44
phosphocholine
50 mM Hepes/NaOH buffer, pH 7.0, 37°C
1.16
Phosphoethanolamine
50 mM Hepes/NaOH buffer, pH 7.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.04
phosphocholine
50 mM Hepes/NaOH buffer, pH 7.0, 37°C
13
Phosphoethanolamine
50 mM Hepes/NaOH buffer, pH 7.0, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.34
phosphocholine
50 mM Hepes/NaOH buffer, pH 7.0, 37°C
1.06
Phosphoethanolamine
50 mM Hepes/NaOH buffer, pH 7.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.48
substrate phosphocholine, 50 mM Hepes/NaOH buffer, pH 7.0, 37°C
3.67
substrate phosphoethanolamine, 50 mM Hepes/NaOH buffer, pH 7.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
theoretical value
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
by far strongest activity in roots of phosphate-starved plants
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
loss of PECP1 activity exacerbates biochemical and morphological effects of phosphate starvation. Constitutive ectopic expression of PECP1 reduces phosphoethanolamine and phosphocholine levels
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PPSP2_ARATH
279
0
31570
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31570
calculated from amino acid sequence
32000
gel filtration, SDS-PAGE
64000
native gel elelctrophoresis, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 32000, monomer-dimer equilibrium, both the monomer and the dimer are active
monomer
1 * 32000, monomer-dimer equilibrium, both the monomer and the dimer are active
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+-Sepharose activated column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
PECP1 expression is tightly regulated by phosphate supply. The transcript level increases strongly after onset of phosphate deprivation
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team