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
Biosynthesis of antibiotics
-
Glycine, serine and threonine metabolism
-
L-serine biosynthesis
-
Metabolic pathways
-
Methane metabolism
-
Microbial metabolism in diverse environments
-
serine metabolism
BRENDA
BRENDA
BRENDA
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
Mus musculus C57BL/6
Q99LS3
-
-
phosphoserine phosphatase
-
-
phosphoserine phosphatase
Q5M819
-
phosphoserine:homoserine phosphotransferase
-
-
PSP
-
-
-
-
pspA
D3DFG8
gene name
pspA
Hydrogenobacter thermophilus DSM 6534
D3DFG8
-
-
pspA
D3DFG8
gene name
-
PSPase
-
-
-
-
pspB
D3DFP8
gene name
pspB
Hydrogenobacter thermophilus DSM 6534
D3DFP8
gene name
-
PSPH
-
-
SerB2
Mycobacterium tuberculosis ATCC 25618
O53289
-
-
SerB653
-
is a HAD-family phosphatase
TON_1161
B6YX36
locus name
CAS REGISTRY NUMBER
COMMENTARY
9025-73-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Hydrogenobacter thermophilus DSM 6534
-
UniPro
Manually annotated by BRENDA team
Hydrogenobacter thermophilus DSM 6534
isoform pspB
UniProt
Manually annotated by BRENDA team
C57BL/6
UniProt
Manually annotated by BRENDA team
Mus musculus C57BL/6
C57BL/6
UniProt
Manually annotated by BRENDA team
isoform SerB2
UniProt
Manually annotated by BRENDA team
Mycobacterium tuberculosis ATCC 25618
isoform SerB2
UniProt
Manually annotated by BRENDA team
Streptomyces azureus ATCC14921
ATCC14921
-
-
Manually annotated by BRENDA team
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
physiological function
-
the embryo-lethal phenotype of isoform psp1 mutants can be complemented with PSP1 cDNA under the control of Pro35S. However, this construct is poorly expressed in the anther tapetum, and does not complement mutant fertility. Microspore development in psp1.1/psp1.1 mutants expressing Pro35S:PSP1 arrest at the polarized stage. The tapetum from these lines displays delayed and irregular development. In addition to embryo death and male sterility, conditional psp1 mutants display a short-root phenotype, which is reverted in the presence of serine
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
-
-
-
?
L-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
-
-
?
L-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
-
-
-
?
L-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
D3DFP8, -
-
strict substrate specificity for L-phosphoserine
-
?
L-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
Hydrogenobacter thermophilus DSM 6534
D3DFG8, D3DFP8
-
strict substrate specificity for L-phosphoserine
-
?
O-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
P42941
-
-
-
?
O-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
B6YX36, -
-
-
-
ir
O-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
-, O53289
-
-
-
?
O-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
B6YX36, -
the enzyme catalyzes the final and irreversible step of L-serine synthesis
-
-
ir
O-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
Mycobacterium tuberculosis ATCC 25618
O53289
-
-
-
?
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
Hydrogenobacter thermophilus DSM 6534
-
-
-
-
?
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
-
?
additional information
?
-
-, O53289
no substrate: O-phospho-L-threonine
-
-
-
additional information
?
-
D3DFP8, -
poor substrates: D-phosphoserine, DL-phosphothreonine, 3-phosphoglycerate, 4-nitrophenylphosphate, and fructose-6-phosphate. Enzyme does not display phosphoglycerate mutase activity
-
-
-
additional information
?
-
Mycobacterium tuberculosis ATCC 25618
O53289
no substrate: O-phospho-L-threonine
-
-
-
additional information
?
-
Hydrogenobacter thermophilus DSM 6534
D3DFG8, D3DFP8
poor substrates: D-phosphoserine, DL-phosphothreonine, 3-phosphoglycerate, 4-nitrophenylphosphate, and fructose-6-phosphate. Enzyme does not display phosphoglycerate mutase activity
-
-
-
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
-
-
-
?
O-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
B6YX36, -
the enzyme catalyzes the final and irreversible step of L-serine synthesis
-
-
ir
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+
O53289
optimum activity upon inclusion of 5 mM Mg2+ or Mn2+ ions in the assay buffer
Mg2+
-
required
Mg2+
-
required
Mg2+
-
required
Mn2+
O53289
optimum activity upon inclusion of 5 mM Mg2+ or Mn2+ ions in the assay buffer
Ni2+
-
can substitute for Mg2+ in activation
Zn2+
-
can substitute for Mg2+ in activation
Mn2+
-
divalent cation required
additional information
D3DFP8, -
no divalent metal ion required; no divalent metal ion required
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-(1-pyridinio)-1-propanesulfonate
B6YX36, -
-
-
BeF3-
-
at 50C, the hydrolytic activity of is markedly inhibited (more than 95%) in the presence of both BeCl2 and NaF. The latter is provided at concentrations that yield predominantly BeF3- in situ. Either BeCl2 or NaF alone has a much smaller inhibitory effect (35 or 20%, respectively). Similar inhibition by BeF3- is observed at room temperature or at 70C
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
-
-
Clorobiocin
O53289
displays bactericidal activity and kills intracellular bacteria in a dose-dependent manner, highly specific in the ability to inhibit isoform SerB2 in comparison with human phosphoserine phosphatase
D-2-amino-3-phosphonopropionic acid
-
-
D-alanine
-
-
D-serine
-
-
DL-2-amino-3-phosphonopropionic acid
O53289
-
-
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
-
-
rosaniline
O53289
displays bactericidal activity and kills intracellular bacteria in a dose-dependent manner
-
sodium orthovanadate
O53289
-
Trifluorperazine
-
-
vanadate
-
-
additional information
D3DFP8, -
not inhibitory: EDTA at 10 mM; not inhibitory: EDTA at 10 mM
-
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
Triton X-100
O53289
presence of 0.01% Triton X-100 enhances isoform SerB2 activity by 15-20%
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
1.5
-
L-phosphoserine
D3DFP8, -
pH 8.0, 70C
1.5
-
L-phosphoserine
-
pH 8.0, 22C, wild-type
1.6
-
L-phosphoserine
D3DFP8, -
pH 8.0, 70C
2.041
-
L-phosphoserine
-
at 30C, in 50 mM Tris (pH 7.5), with 5 mM MgCl2
3.3
-
L-phosphoserine
-
pH 8.0, 22C, mutant delI211
15.2
-
L-phosphoserine
-
pH 8.0, 22C, mutant delVal2-I211
20
-
L-phosphoserine
-
above 20 mM, pH 8.0, 22C, mutant H85A
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
0.081
-
O-phospho-L-serine
B6YX36, -
pH 6.5, 65C
0.088
-
O-phospho-L-serine
B6YX36, -
pH 6.5, 37C
0.0927
-
O-phospho-L-serine
O53289
pH 7.4, 37C
0.1
-
O-phospho-L-serine
B6YX36, -
pH 6.5, 65C, in presence of 20 mM 3-(1-pyridinio)-1-propanesulfonate
0.14
-
O-phospho-L-serine
B6YX36, -
pH 6.5, 65C, in presence of 100 mM 3-(1-pyridinio)-1-propanesulfonate
0.181
-
O-phospho-L-serine
B6YX36, -
pH 6.5, 65C, in presence of 200 mM 3-(1-pyridinio)-1-propanesulfonate
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
0.0073
-
O-phospho-L-serine
B6YX36, -
pH 6.5, 37C
0.143
-
O-phospho-L-serine
B6YX36, -
pH 6.5, 65C
0.15
-
O-phospho-L-serine
O53289
pH 7.4, 37C
0.168
-
O-phospho-L-serine
B6YX36, -
pH 6.5, 65C, in presence of 20 mM 3-(1-pyridinio)-1-propanesulfonate
0.179
-
O-phospho-L-serine
B6YX36, -
pH 6.5, 65C, in presence of 100 mM 3-(1-pyridinio)-1-propanesulfonate
0.182
-
O-phospho-L-serine
B6YX36, -
pH 6.5, 65C, in presence of 200 mM 3-(1-pyridinio)-1-propanesulfonate
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.24
-
L-phosphoserine
-
pH 8.0, 22C, mutant delVal2-I211
2994
2
-
L-phosphoserine
-
pH 8.0, 22C, mutant delI211
2994
98
-
L-phosphoserine
-
pH 8.0, 22C, wild-type
2994
0.00159
-
O-phospho-L-serine
O53289
pH 7.4, 37C
1189
0.0824
-
O-phospho-L-serine
B6YX36, -
pH 6.5, 37C
1189
1.01
-
O-phospho-L-serine
B6YX36, -
pH 6.5, 65C, in presence of 200 mM 3-(1-pyridinio)-1-propanesulfonate
1189
1.32
-
O-phospho-L-serine
B6YX36, -
pH 6.5, 65C, in presence of 100 mM 3-(1-pyridinio)-1-propanesulfonate
1189
1.69
-
O-phospho-L-serine
B6YX36, -
pH 6.5, 65C, in presence of 20 mM 3-(1-pyridinio)-1-propanesulfonate
1189
1.81
-
O-phospho-L-serine
B6YX36, -
pH 6.5, 65C
1189
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0168
-
Clorobiocin
O53289
pH 7.4, 37C
0.67
-
DL-2-amino-3-phosphonopropionic acid
O53289
pH 7.4, 37C
-
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
0.0315
-
rosaniline
O53289
pH 7.4, 37C
-
0.458
-
sodium orthovanadate
O53289
pH 7.4, 37C
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+
28
-
D3DFP8, -
substrate L-phosphoserine, pH 8.0, 70C
58
-
D3DFP8, -
substrate L-phosphoserine, pH 8.0, 70C
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
-
-
6.5
-
B6YX36, -
assay at
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
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60
75
B6YX36, -
60C: about 50% of maximal activity, 75C: about 75% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
cortex, brain stem, cerebellum, striatum, thalamus hippocampus
Manually annotated by BRENDA team
-
highly expressed in periventricular neural progenitors in the embryonic brain
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
-
enzyme plays a crucial role in embry, pollen and root development
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
-
enzyme plays a crucial role in embry, pollen and root development
Manually annotated by BRENDA team
-
enzyme plays a crucial role in embry, pollen and root development
Manually annotated by BRENDA team
-
highly induced in squamous cell carcinoma
Manually annotated by BRENDA team
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)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Thermococcus onnurineus (strain NA1)
Thermococcus onnurineus (strain NA1)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37000
-
D3DFP8, -
gel filtration
46000
-
D3DFP8, -
gel filtration
47000
-
-
mouse, gel filtration
65000
-
-
bovine, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-, O82796
x * 37000, SDS-PAGE
?
-
x * 38000, SerB gene product, SDS-PAGE
?
Q5M819
x * 25000, Western blot analysis
?
O53289
x * 45000, SDS-PAGE, His-tagged recombinant protein
?
Mycobacterium tuberculosis ATCC 25618
-
x * 45000, SDS-PAGE, His-tagged recombinant protein
-
dimer
D3DFP8, -
1 * 24500, protein PspA, plus 1 * 24000, protein PspB, SDS-PAGE
dimer
D3DFP8, -
2 * 24300, SDS-PAGE
dimer
Hydrogenobacter thermophilus DSM 6534
-
2 * 24300, SDS-PAGE, 1 * 24500, protein PspA, plus 1 * 24000, protein PspB, 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+
-
apo-form and in complex with its substrate L-phosphoserine, to 1.5 A and 1.8 A resolution, respectively. In the crystal structure of the enzyme-substrate complex, oxygen atoms of the carboxyl group of L-phosphoserine form hydrogen bonds with main-chain amides of Gln21 and Gly22, and Nepsilon2 of Gln21, and partly form a hydrogen or an ionic bond withNepsilon2 of His85. The nitrogen atom of amino group of L-phosphoserine forms a hydrogen or an ionic bond with oxygen atoms of the side-chain carboxyl group of Glu82, and forms hydrogen bonds with Nepsilon2 of His85 and Ogamma1 of Thr15
-
two diffraction data sets with resolution ranges of 45.0-2.50 and 45.0-1.50 A. The space group of the crystal is orthorhombic P212121, with unit-cell parameters a = 49.8, b = 73.6, c = 124.3 A
-
crystals are grown by using the hanging drop vapor diffusion method with seeding.1.5 A resolution the X-ray crystal structure of the complex of BeF3 2 with phosphoserine phosphatase. The structure is comparable to that of a phosphoenzyme intermediate: BeF3- is bound to Asp11 with the tetrahedral geometry of a phosphoryl group, is coordinated to Mg2+, and is bound to residues surrounding the active site that are conserved in the haloacid dehalogenase (HAD) superfamily
-
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
-
construction of a homology model and molecular docking of O-phospho-L-serine. Residues Asp185, Ser273, Lys-318, and Asp-341 are part of the substrate binding pocket. Val186 and Ser188 might also interact with O-phospho-L-serine
O53289
hanging-drop vapour diffsuion method
-
sitting drop method at 18 C, crystal structure of the enzyme at 1.8 A resolution
B6YX36, -
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
expression in Escherichia coli
-
expression in Escherichia coli; expression in Escherichia coli
D3DFP8, -
expression in Eschericia coli
O53289
expressed in Escherichia coli strain DH5alpha
-
expressed in Escherichia coli BL21(DE3) Gold pLysS and in HEK-293 cell
Q5M819
expression in Escherichia coli
B6YX36, -
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
in liver in response to a low protein diet
Mus musculus C57BL/6
-
-
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
delI211
-
50fold decrease in catalytic efficiency
delVal2-I211
-
400fold decrease in catalytic efficiency
H85A
-
almost complete loss of activity
H9A
-
almost complete loss of activity
delI211
Hydrogenobacter thermophilus DSM 6534
-
50fold decrease in catalytic efficiency
-
delVal2-I211
Hydrogenobacter thermophilus DSM 6534
-
400fold decrease in catalytic efficiency
-
H85A
Hydrogenobacter thermophilus DSM 6534
-
almost complete loss of activity
-
H9A
Hydrogenobacter thermophilus DSM 6534
-
almost complete loss of activity
-
D185G
O53289
complete loss of activity
D341G
O53289
about 10% residual activity, no change in secondary structure compared to wild-type
K318E
O53289
complete loss of activity
S188A
O53289
activity similar to wild-type
S273A
O53289
about 30% residual activity, no change in secondary structure compared to wild-type
V186Q
O53289
about 55% residual activity
D185G
Mycobacterium tuberculosis ATCC 25618
-
complete loss of activity
-
D341G
Mycobacterium tuberculosis ATCC 25618
-
about 10% residual activity, no change in secondary structure compared to wild-type
-
K318E
Mycobacterium tuberculosis ATCC 25618
-
complete loss of activity
-
S188A
Mycobacterium tuberculosis ATCC 25618
-
activity similar to wild-type
-
S273A
Mycobacterium tuberculosis ATCC 25618
-
about 30% residual activity, no change in secondary structure compared to wild-type
-
D198N
-
9% activity of the wild type enzyme
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
O53289
development of a malachite green-based high throughput assay system to identify isoform SerB2 inhibitors
analysis
Mycobacterium tuberculosis ATCC 25618
-
development of a malachite green-based high throughput assay system to identify isoform SerB2 inhibitors
-