Information on EC 3.1.3.3 - phosphoserine phosphatase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
3.1.3.3
-
RECOMMENDED NAME
GeneOntology No.
phosphoserine phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Glycine, serine and threonine metabolism
-
Metabolic pathways
-
Methane metabolism
-
Microbial metabolism in diverse environments
-
serine biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
O-phosphoserine phosphohydrolase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-phosphoserine phosphatase
-
-
-
-
CTD phosphatase fcp1
-
-
-
-
HPSP
-
-
L-phosphoserine phosphatase
-
-
O-phosphoserine phosphohydrolase
-
-
-
-
phosphatase, phosphoserine
-
-
-
-
phosphoserine phosphatase
-
-
phosphoserine phosphatase
Q99LS3
-
phosphoserine phosphatase
-
-
phosphoserine phosphatase
Q5M819
-
phosphoserine:homoserine phosphotransferase
-
-
PSP
-
-
-
-
PSPase
-
-
-
-
PSPH
-
-
SerB653
-
is a HAD-family phosphatase
CAS REGISTRY NUMBER
COMMENTARY
9025-73-4
-
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
in a rat model of periodontal disease using a SerB mutant strain it is shown that the SerB phosphatase of Porphyromonas gingivalis is required for maximal alveolar bone resorption, and in the absence of SerB, more polymorphonuclear neutrophils are recruited into the gingival tissues
malfunction
-
knock down of PSPH dramatically diminishes squamous cell carcinoma cell proliferation and cyclin D1 levels in the presence of exogenous of L-serine production suggesting a non-canonical role for PSPH in epithelial carcinogenesis
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
?
D-phosphoserine + H2O
D-Ser + phosphate
show the reaction diagram
-
-
-
?
D-phosphoserine + H2O
D-Ser + phosphate
show the reaction diagram
-
-
-
?
D-phosphoserine + H2O
D-Ser + phosphate
show the reaction diagram
-
-
-
?
D-phosphoserine + H2O
D-Ser + phosphate
show the reaction diagram
-
-
-
?
D-phosphoserine + H2O
D-Ser + phosphate
show the reaction diagram
-
-
-
?
D-phosphoserine + H2O
D-Ser + phosphate
show the reaction diagram
-
-
-
?
D-phosphoserine + H2O
D-Ser + phosphate
show the reaction diagram
-
-
-
?
D-phosphoserine + H2O
D-Ser + phosphate
show the reaction diagram
-
-
-
?
DL-phosphoserine + H2O
DL-Ser + phosphate
show the reaction diagram
-
-
-
?
DL-phosphoserine + H2O
DL-Ser + phosphate
show the reaction diagram
-
-
-
?
DL-phosphoserine + H2O
DL-Ser + phosphate
show the reaction diagram
-
-
-
ir
DL-phosphoserine + H2O
DL-Ser + phosphate
show the reaction diagram
-
-
-
?
DL-phosphoserine + H2O
DL-Ser + phosphate
show the reaction diagram
-
-
-
?
glycerinaldehyde-3-phosphate-dehydrogenase + H2O
?
show the reaction diagram
-
-
-
-
?
heat-shock protein 90 + H2O
?
show the reaction diagram
-
-
-
-
?
L-3-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
-
-
-
?
L-3-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-, O82796
biosynthesis of serine, terminal enzyme in the plastidic pathway
-
-
-
L-3-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
final step in serine biosynthesis
-
-
-
L-3-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
final step in serine biosynthesis
-
-
-
L-3-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
final step in serine biosynthesis
-
-
-
L-3-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
final step in serine biosynthesis
-
-
-
L-O-phospho-serine + H2O
L-serine + phosphate
show the reaction diagram
P42941
-
-
-
?
L-O-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
-, enzyme is responsible for the third and final step of the L-serine biosynthetic pathway
-
?
L-phosphoserine + H2O
L-Ser + phosphate
show the reaction diagram
-
-
-
?
L-phosphoserine + H2O
L-Ser + phosphate
show the reaction diagram
-
-
-
?
L-phosphoserine + H2O
L-Ser + phosphate
show the reaction diagram
-
-
-
-
L-phosphoserine + H2O
L-Ser + phosphate
show the reaction diagram
-
-
-
-
?
L-phosphoserine + H2O
L-Ser + phosphate
show the reaction diagram
-
-
-
ir
L-phosphoserine + H2O
L-Ser + phosphate
show the reaction diagram
-
-
-
?
L-phosphoserine + H2O
L-Ser + phosphate
show the reaction diagram
-
-
-
?
L-phosphoserine + H2O
L-Ser + phosphate
show the reaction diagram
-
-
-
?
L-phosphoserine + H2O
L-Ser + phosphate
show the reaction diagram
-
-
-
?
L-phosphoserine + H2O
L-Ser + phosphate
show the reaction diagram
-
-
-
?
L-phosphoserine + H2O
L-Ser + phosphate
show the reaction diagram
-
-
-
?
L-phosphoserine + H2O
L-Ser + phosphate
show the reaction diagram
-, O82796
-
-
?
L-phosphoserine + H2O
L-Ser + phosphate
show the reaction diagram
-
-
-
?
L-phosphoserine + H2O
L-Ser + phosphate
show the reaction diagram
-
-
-
-
?
L-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
-
-
?
O-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
P42941
-
-
-
?
O-phospho-L-tyrosine + H2O
L-Tyr + phosphate
show the reaction diagram
-
-
-
?
O-phospho-L-tyrosine + H2O
L-Tyr + phosphate
show the reaction diagram
-
-
-
-
-
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
P42941
-
-
-
?
L-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
-
the enzyme may play a role in altered neuronal function in Alzheimers disease via enhancing glutamate-induced neurotoxicity by D-serine and the IL-11 receptor system
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-3-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-, O82796
biosynthesis of serine, terminal enzyme in the plastidic pathway
-
-
-
L-3-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
final step in serine biosynthesis
-
-
-
L-3-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
final step in serine biosynthesis
-
-
-
L-3-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
final step in serine biosynthesis
-
-
-
L-3-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
final step in serine biosynthesis
-
-
-
O-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
P42941
-
-
-
?
L-O-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
enzyme is responsible for the third and final step of the L-serine biosynthetic pathway
-
?
additional information
?
-
-
the enzyme may play a role in altered neuronal function in Alzheimers disease via enhancing glutamate-induced neurotoxicity by D-serine and the IL-11 receptor system
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Al3+
-
at near-physiological ratios of aluminum to magnesium, aluminum can dominate over magnesium in the enzyme-metal fluoride inhibitory TSA complexes, aluminium is the more likely origin of some of the physiological effects of fluoride
Co2+
-
divalent cation required
Co2+
-
divalent cation required
Cu2+
-
activation
Fe2+
-
can substitute for Mg2+ in activation
Mg2+
-
dependent on
Mg2+
-
-
Mg2+
-
at near-physiological ratios of aluminum to magnesium, aluminum can dominate over magnesium in the enzyme-metal fluoride inhibitory TSA complexes
Mg2+
-
required
Mg2+
-
required
Mg2+
-
required
Mn2+
-
divalent cation required
Ni2+
-
can substitute for Mg2+ in activation
Zn2+
-
can substitute for Mg2+ in activation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
inhibition even in presence of Mg2+, replacement of sixfold coordinated Mg2+ in active site by Ca2+ results in sevenfold coordinated metal ion, explaining the inhibitory effect of Ca2+
Chlorpromazine
-
-
D-2-amino-3-phosphonopropionic acid
-
-
D-alanine
-
-
D-serine
-
-
DL-2-Amino-4-phosphonobutyric acid
-
-
Glycerophosphorylcholine
-
-
glycine
-, O82796
not inhibitory
hexadecylphosphocholine
-
-
iodoacetate
-
-
L-2-amino-3-phosphonopropionic acid
-
-
L-alanine
-
-
L-alanine
-
-
L-serine
-
inhibition of L-phosphoserine hydrolysis
L-serine
-, O82796
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
p-chloromercuribenzoate
-
-
p-chloromercuriphenylsulfanate
-
-
-
phosphonoalanine
-
-
phosphorylcholine
-
-
Trifluorperazine
-
-
vanadate
-
-
additional information
-
not inhibitory: ethanolamine, L-Thr, L-Asp, L-Phe, beta-alanine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Chlordiazepoxide
-
activation
diazepam
-
activation
Sucrose
-
activation
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
D-phosphoserine
-
-
0.8
-
D-phosphoserine
-
tumor cell enzyme
1.2
-
D-phosphoserine
-
liver enzyme
4.2
-
D-phosphoserine
-
-
0.05
-
DL-phosphoserine
-
unassociated enzyme form
0.1
-
DL-phosphoserine
-
associated enzyme form
0.11
-
DL-phosphoserine
-
-
3.5
-
L-3-phosphoserine
-, O82796
-
0.02
-
L-phosphoserine
-
-
0.036
-
L-phosphoserine
-
-
0.05
-
L-phosphoserine
-
liver enzyme
0.056
-
L-phosphoserine
-
tumor cell enzyme
0.058
-
L-phosphoserine
-
-
0.207
-
L-phosphoserine
-
pH 8.0, 30C
2.041
-
L-phosphoserine
-
at 30C, in 50 mM Tris (pH 7.5), with 5 mM MgCl2
0.117
-
L-phosphothreonine
-
at 30C, in 50 mM Tris (pH 7.5), with 5 mM MgCl2
0.047
-
L-phosphotyrosine
-
at 30C, in 50 mM Tris (pH 7.5), with 5 mM MgCl2
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.508
-
L-phosphoserine
-
at 30C, in 50 mM Tris (pH 7.5), with 5 mM MgCl2
2.94
-
L-phosphoserine
-
at 30C, in 50 mM Tris (pH 7.5), with 5 mM MgCl2
804
-
L-phosphoserine
-
pH 8.0, 30C
0.0004
-
L-phosphothreonine
-
at 30C, in 50 mM Tris (pH 7.5), with 5 mM MgCl2
0.00003
-
L-phosphotyrosine
-
at 30C, in 50 mM Tris (pH 7.5), with 5 mM MgCl2
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.4
-
EDTA
-
at 30C, in 50 mM Tris (pH 7.5), with 5 mM MgCl2
1.3
-
Na3VO4
-
at 30C, in 50 mM Tris (pH 7.5), with 5 mM MgCl2
5.9
-
NaF
-
at 30C, in 50 mM Tris (pH 7.5), with 5 mM MgCl2
0.005
-
okadaic acid
-
IC50: above 0.005 mM, at 30C, in 50 mM Tris (pH 7.5), with 5 mM MgCl2
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.018
-
-
-
0.13
-
-
-
3
-
-, O82796
-
5.3
-
P42941
substrate L-O-phosphoserine, presence of 1 mM Mn2+
17.3
-
P42941
substrate L-O-phosphoserine, presence of 5 mM Mg2+
additional information
-
-
aluminum fluoride transition state analogs (TSA) complexes analyzed, NMR spectra indicated, pH titration, chemical shifts of the 19F NMR resonances not markedly affected by pH
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
6.6
-
-
5.6
6.6
-
-
5.8
6.2
-
unassociated enzyme form
6
6.4
-
associated enzyme form
6.2
-
-
-
6.3
-
-
-
6.5
7
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.4
9.2
-
fluoride chemical shifts constant throughout the pH range examined
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
cytoplasmic protein in keratinocytes that primarily localizes to endosomes
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6)
Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Mycobacterium avium (strain 104)
Thermococcus onnurineus (strain NA1)
Thermococcus onnurineus (strain NA1)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
47000
-
-
mouse, gel filtration
65000
-
-
bovine, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q5M819
x * 25000, Western blot analysis
?
-
x * 38000, SerB gene product, SDS-PAGE
?
-, O82796
x * 37000, SDS-PAGE
homodimer
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapour-diffusion method. A resolution of 1.53 A provides a detailed model of the active site in a completely open conformation and the water molecules bound to it
-
hanging-drop vapour diffusion method
-
hanging-drop vapour-diffusion method
-
replacement of sixfold coordinated Mg2+ in active site by Ca2+ results in sevenfold coordinated metal ion, explaining the inhibitory effect of Ca2+
-
hanging-drop vapor-diffusion method, crystal structure determined at 1.8 A resolution
-
high-resolution, 1.5-1.9 A structures which define the open state prior to substrate binding, the complex with phosphoserine substrate bound, and the complex with AlF3, a transition-state analog for the phospho-transfer steps in the reaction
-
hanging-drop vapour diffsuion method
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
extremely unstable
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-9C, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partially
-
partially
-
partially
-
partially, copurifies with serine phosphotransferase
-
BioLogic DuoFlow chromatography system loaded with an IMAC column
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli strain DH5alpha
-
expressed in Escherichia coli BL21(DE3) Gold pLysS and in HEK-293 cell
Q5M819
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in MDA-MB-231(SA) cell
-
highly induced in squamous cell carcinoma
-
in liver in response to a low protein diet
Q99LS3
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E29D
-
less than 5% of the activity of wild-type enzyme with L-phosphoserine as substrate
E29Q
-
inactive mutant enzyme
N133A
-
about 25% of the activity of wild-type enzyme with L-phosphoserine as substrate
N133D
-
about 130% of the activity of wild-type enzyme with L-phosphoserine as substrate
R202A
-
inactive mutant enzyme
R202K
-
less than 5% of the activity of wild-type enzyme with L-phosphoserine as substrate
R65A
-
inactive mutant enzyme
R65K
-
inactive mutant enzyme
S23A
-
about 50% of the activity of wild-type enzyme with L-phosphoserine as substrate
S23T
-
about 20% of the activity of wild-type enzyme with L-phosphoserine as substrate
T182S
-
about 5% of the activity of wild-type enzyme with L-phosphoserine as substrate
T182V
-
about 75% of the activity of wild-type enzyme with L-phosphoserine as substrate
D198N
-
9% activity of the wild type enzyme