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Information on EC 3.1.3.76 - lipid-phosphate phosphatase
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EC Tree
3.1.3.76 lipid-phosphate phosphataseIUBMB Comments
Requires Mg2+ for maximal activity. The enzyme from mammals is a bifunctional enzyme: the N-terminal domain exhibits lipid-phosphate-phosphatase activity and the C-terminal domain has the activity of EC 3.3.2.10, soluble epoxide hydrolase (sEH) . The best substrates for this enzyme are 10-hydroxy-9-(phosphooxy)octadecanoates, with the threo- form being a better substrate than the erythro- form . The phosphatase activity is not found in plant sEH or in EC 3.3.2.9, microsomal epoxide hydrolase, from mammals .
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Word Map
- 3.1.3.76
- pten
- phosphatidylinositol
-
tensin
- phosphoinositide
- 3-kinase
- phosphatases
- inositol
-
ptdins3,4,5p3
-
3,4,5-trisphosphate
-
hamartoma
- xlmtm
- inpp4b
-
3-phosphatase
- ship-1
-
myotubular
- synaptojanin
- charcot-marie-tooth
-
pten-null
- pip2
-
myotubularin-related
- myotubularins
-
pten-deficient
-
pten-mediated
-
dual-specificity
-
3,5-bisphosphate
- cowden
-
pi3k-dependent
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
lipid phosphatase, nterm-phos, epxh2, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
soluble epoxide hydrolase
-
the N-terminal domain of the soluble epoxide hydrolase demonstrates lipid phosphatase activity
additional information
additional information
-
EC 3.1.3.76 belongs to the haloacid dehalogenase superfamily of enzymes, c.f. EC 3.3.2.10
additional information
-
EC 3.1.3.76 belongs to the haloacid dehalogenase superfamily of enzymes, c.f. EC 3.3.2.10
additional information
-
EC 3.1.3.76 belongs to the haloacid dehalogenase superfamily of enzymes, see also EC 3.3.2.10
additional information
-
EC 3.1.3.76 belongs to the haloacid dehalogenase superfamily of enzymes, see also EC 3.3.2.10
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate
(9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate
-
-
-
-
(9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate
the phosphatase activity of the enzyme is located at the N-terminal part, the C-terminal part harbors the epoxide hydrolase activity of EC 3.3.2.10, both catalytic sites act independently
-
(9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate
the phosphatase activity of the enzyme is located at the N-terminal part, the C-terminal part harbors the epoxide hydrolase activity of EC 3.3.2.10, both catalytic sites act independently
-
(9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate
the phosphatase activity of the enzyme is located at the N-terminal part, the C-terminal part harbors the epoxide hydrolase activity of EC 3.3.2.10, both catalytic sites act independently
-
(9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate
the phosphatase activity of the enzyme is located at the N-terminal part, the C-terminal part harbors the epoxide hydrolase activity of EC 3.3.2.10, both catalytic sites act independently, reaction mechanism
-
(9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate
the phosphatase activity of the enzyme is located at the N-terminal part, the C-terminal part harbors the epoxide hydrolase activity of EC 3.3.2.10, both catalytic sites act independently, reaction mechanism, structure-mechanism relationship
-
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SYSTEMATIC NAME
IUBMB Comments
(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate phosphohydrolase
Requires Mg2+ for maximal activity. The enzyme from mammals is a bifunctional enzyme: the N-terminal domain exhibits lipid-phosphate-phosphatase activity and the C-terminal domain has the activity of EC 3.3.2.10, soluble epoxide hydrolase (sEH) [1]. The best substrates for this enzyme are 10-hydroxy-9-(phosphooxy)octadecanoates, with the threo- form being a better substrate than the erythro- form [1]. The phosphatase activity is not found in plant sEH or in EC 3.3.2.9, microsomal epoxide hydrolase, from mammals [1].
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CAS REGISTRY NUMBER
COMMENTARY
9025-77-8
-
9048-63-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(9E)-12-phosphonooxyoctadec-9-enoic acid + H2O
(9E)-12-hydroxyoctadec-9-enoic acid + phosphate
-
-
-
-
?
(9E)-12-sulfonooxyoctadec-9-enoic acid + H2O
(9E)-12-hydroxyoctadec-9-enoic acid + sulfate
-
-
-
-
?
(9Z)-12-phosphonooxyoctadec-9-enoic acid + H2O
(9Z)-12-hydroxyoctadec-9-enoic acid + phosphate
-
-
-
-
?
(9Z)-12-sulfonooxyoctadec-9-enoic acid + H2O
(9Z)-12-hydroxyoctadec-9-enoic acid + sulfate
-
-
-
-
?
10-sulfonooxy-octadecanoic acid + H2O
10-hydroxyoctadecanoic acid + phosphate
-
-
-
-
?
12-phosphonooxyoctadecanoic acid + H2O
12-hydroxyoctadecanoic acid + phosphate
-
-
-
-
?
2'-[2-benzothiazolyl]-6'-hydroxybenzothiazole phosphate + H2O
2'-[2-benzothiazolyl]-6'-hydroxybenzothiazole + phosphate
-
i.e. attophos
-
-
?
erythro-10-phosphonooxy-9-hydroxy-octadecanoic acid + H2O
erythro-9,10-dihydroxyoctadecanoate + phosphate
-
-
-
-
?
erythro-9-hydroxy-10-(phosphonooxy)octadecanoate + H2O
erythro-9,10-dihydroxyoctadecanoic acid + phosphate
-
-
i.e. dihydroxy elaidic acid
-
?
threo-10-phosphonooxy-9-hydroxy-octadecanoic acid + H2O
threo-9,10-dihydroxyoctadecanoate + phosphate
-
-
-
-
?
threo-9-hydroxy-10-(phosphonooxy)octadecanoate + H2O
threo-9,10-dihydroxyoctadecanoic acid + phosphate
-
preferred substrate
i.e. dihydroxy stearic acid
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
-
-
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl sulfate of the isolated recombinant N-terminal domain
-
-
?
additional information
?
-
-
the enzyme acts regioselectively, substrate specificity
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(9E)-12-phosphonooxyoctadec-9-enoic acid + H2O
(9E)-12-hydroxyoctadec-9-enoic acid + phosphate
-
-
-
-
?
(9Z)-12-phosphonooxyoctadec-9-enoic acid + H2O
(9Z)-12-hydroxyoctadec-9-enoic acid + phosphate
-
-
-
-
?
12-phosphonooxyoctadecanoic acid + H2O
12-hydroxyoctadecanoic acid + phosphate
-
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
dependent on, optimal at 1 mM MgCl2, one Mg2+ per catalytic subunit, dissociation constants, recombinant enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
poor or no inhibition by chalcone oxide, 1-cyclohexyl-3-ethyl urea, 1-cyclohexyl-3-hexyl urea, 1-cyclohexyl-3-dodecyl urea, 1,3-dicyclohexyl urea, okadaic acid, tartaric acid, and sodium orthovanadate
-
additional information
-
no inhibition of the phosphatase activity by 1-cyclohexyl-3-dodecyl urea at 0.1 mM
-
additional information
-
inhibition mechanism of sulfates, sulfonates, and phosphonates
-
additional information
-
no inhibition of the phosphatase activity by dicyclohexylurea and 4-fluorochalcone oxide
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0036
2'-[2-benzothiazolyl]-6'-hydroxybenzothiazole phosphate
-
pH 7.0, 30°C, recombinant enzyme
0.02
threo-10-phosphonooxy-9-hydroxy-octadecanoic acid
-
pH 7.0, 30°C, recombinant enzyme
0.021
threo-9,10-phosphonooxyoctadecanoic acid
-
pH 7.0, 30°C, recombinant enzyme
0.021
threo-9-hydroxy-10-(phosphonooxy)octadecanoate
-
pH 7.8, 37°C, recombinant enzyme
1.1
4-nitrophenyl phosphate
-
pH 7.4, 37°C, recombinant wild-type allele MFA enzyme and mutant R103C
2.3
4-nitrophenyl phosphate
-
pH 7.8, 37°C, recombinant wild-type N-terminal domain
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.013
4-nitrophenyl phosphate
-
pH 7.8, 37°C, recombinant wild-type N-terminal domain
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.007
-
purified recombinant mutant R103C/R287Q, substrate 4-nitrophenyl phosphate
0.029
-
purified recombinant wild-type allele MFA enzyme and mutant E470G, substrate 4-nitrophenyl phosphate
0.03
additional information
-
optimization of activity assay conditions with the recombinant enzyme, maximal in 25 mM Tris buffer, pH 7.0, 30°C, 1 mM MgCl2
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the N-terminal lipid phosphatase may play a role in the development of hypoxia-induced pulmonary hypertension
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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). HYES_HUMAN
555
0
62616
Swiss-Prot
Secretory Pathway (Reliability: 3)
HYES_MOUSE
554
0
62515
Swiss-Prot
other Location (Reliability: 4)
HYES_PIG
555
0
62767
Swiss-Prot
other Location (Reliability: 5)
HYES_RAT
554
0
62340
Swiss-Prot
other Location (Reliability: 5)
A0A5B7AKX4_DAVIN
242
0
28180
TrEMBL
Mitochondrion (Reliability: 3)
A0A1Z5JN83_FISSO
342
0
37825
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2G9G099_9LAMI
571
3
63395
TrEMBL
Mitochondrion (Reliability: 3)
A0A369Q817_9SPHN
287
0
32672
TrEMBL
-
A0A5B6ZQW8_DAVIN
317
0
35862
TrEMBL
other Location (Reliability: 3)
A0A8J8W710_9EURO
336
0
38189
TrEMBL
other Location (Reliability: 2)
A0A0F8BL45_CERFI
340
0
37302
TrEMBL
other Location (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
-
the phosphatase activity of the enzyme is located at N-terminal part, the C-terminal part harbors the epoxide hydrolase activity of EC 3.3.2.10, Arg287 may be involved in formation of the quarternary enzyme structure
additional information
-
the phosphatase activity of the enzyme is located at the 35 kDa N-terminal part which has a alpha/beta-fold, the 25 kDa C-terminal part, with a different hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity of EC 3.3.2.10, quarternary structure analysis, structure-mechanism relationship
additional information
-
the phosphatase activity of the enzyme is located at the 35 kDa N-terminal part which has a alpha/beta-fold, the 25 kDa C-terminal part, with a different hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity of EC 3.3.2.10, structure analysis
additional information
-
the phosphatase activity of the enzyme is located at the 35 kDa N-terminal part which has a alpha/beta-fold, the 25 kDa C-terminal part, with a different hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity of EC 3.3.2.10, structure analysis
additional information
-
the phosphatase activity of the enzyme is located at the N-terminal part, the C-terminal part harbors the epoxide hydrolase activity of EC 3.3.2.10
additional information
-
the phosphatase activity of the enzyme is located at the N-terminal part, the C-terminal part harbors the epoxide hydrolase activity of EC 3.3.2.10
additional information
-
the phosphatase activity of the enzyme is located at the 35 kDa N-terminal part which has a alpha/beta-fold, the 25 kDa C-terminal part, with a different hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity of EC 3.3.2.10, structure analysis
additional information
-
the phosphatase activity of the enzyme is located at the 35 kDa N-terminal part which has a alpha/beta-fold, the 25 kDa C-terminal part, with a different hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity of EC 3.3.2.10, structure analysis
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, sitting drop vapour diffusion method, 0.005 ml of 12-16 mg/ml protein in 3 mM DTT, 0.1 M sodium phosphate, pH 7.4, is mixed with 0.005 ml precipitation solution containing 0.1 M Tris, pH 9.0, 30% w/v PEG 4000, and 0.2 M Li2SO4, versus 1 ml reservoir of precipitatin solution, 4°C, 10 days, X-ray diffraction structure determination and analysis at 2.6 A resolution, modeling
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C154Y
E470G
-
site-directed mutagenesis, the mutant shows a hydrolase/phosphatase ratio of 0.9, compared to the wild-type ratio of 1.0
K55R
-
site-directed mutagenesis, the mutant shows a hydrolase/phosphatase ratio of 1.9, compared to the wild-type ratio of 1.0
R103C
R103C/R287Q
R287Q
V422A
-
site-directed mutagenesis, the mutant shows a hydrolase/phosphatase ratio of 0.8, compared to the wild-type ratio of 1.0
Y465F
-
site-directed mutagenesis, mutant enzyme shows phosphatase, but no epoxide hydrolase activity
additional information
-
the isolated recombinant N-terminal domain is a fully active phosphatase
C154Y
-
site-directed mutagenesis, the mutant shows a hydrolase/phosphatase ratio of 2.2, compared to the wild-type ratio of 1.0
C154Y
-
the mutant shows similar activity for isoprenoid phosphate compared to the wild-type enzyme
R103C
-
site-directed mutagenesis, the mutant shows a hydrolase/phosphatase ratio of 1.3, compared to the wild-type ratio of 1.0
R103C
-
the mutant shows increased activity for isoprenoid phosphate compared to the wild-type enzyme
R103C/R287Q
-
site-directed mutagenesis, the mutant shows a hydrolase/phosphatase ratio of 1.2, compared to the wild-type ratio of 1.0
R103C/R287Q
-
the mutant shows similar activity for isoprenoid phosphate compared to the wild-type enzyme
R287Q
-
site-directed mutagenesis, the mutant shows the same hydrolase/phosphatase ratio of 1.0 as the wild-type, but reduced stability at 37°C
R287Q
-
the mutant shows increased activity for isoprenoid phosphate compared to the wild-type enzyme
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from liver to homogeneity by ultracentrifugation and affinity chromatography on a benzyl thio resin using 4-fluorochalcone oxide as eluent
-
recombinant enzyme by S-benzyl affinity chromatography with 4-fluorochalcone oxide as eluent
-
recombinant His-tagged wild-type and D9A mutant enzymes and N-terminal domains from Escherichia coli strain BL21-AI by nickel affinity chromatography, recombinant strep-tagged wild-type enzyme from Escherichia coli strain XL1-Blue by streptavidin affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from insect cells by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Sf21 insect cells by nickel affinity chromatography
-
recombinant wild-type and mutant enzymes from insect cells by affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
arabinose-inducible expression of His-tagged wild-type and D9A mutant enzymes and N-terminal domains from cDNA in Escherichia coli strain BL21-AI, expression of strep-tagged enzyme from full-length gene in Escherichia coli strain XL1-Blue
-
arabinose-inducible expression of the enzyme from full-length gene in Escherichia coli strain BL21-AI
-
expression of enzyme in insect cells using the baculovirus infection system
-
expression of His-tagged wild-type and mutant enzymes in insect cells using the baculovirus infection system
-
expression of wild-type and mutant enzymes in insect cells using the baculovirus infection system
-
gene EPHX2, expression of His-tagged wild-type and mutant enzymes in Spodoptera frugiperda Sf21 cells using the baculovirus infection system
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gomez, G.A.; Morisseau, C.; Hammock, B.D.; Christianson, D.W.
Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis
Biochemistry
43
4716-4723
2004
Homo sapiens
brenda
Newman, J.W.; Morisseau, C.; Harris, T.R.; Hammock, B.D.
The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity
Proc. Natl. Acad. Sci. USA
100
1558-1563
2003
Homo sapiens
brenda
Srivastava, P.K.; Sharma, V.K.; Kalonia, D.S.; Grant, D.F.
Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quarternary structure
Arch. Biochem. Biophys.
427
164-169
2004
Homo sapiens
brenda
Enayetallah, A.E.; Grant, D.F.
Effects of human soluble epoxide hydrolase polymorphisms on isoprenoid phosphate hydrolysis
Biochem. Biophys. Res. Commun.
341
254-260
2006
Homo sapiens, Rattus norvegicus
brenda
Tran, K.L.; Aronov, P.A.; Tanaka, H.; Newman, J.W.; Hammock, B.D.; Morisseau, C.
Lipid sulfates and sulfonates are allosteric competitive inhibitors of the N-terminal phosphatase activity of the mammalian soluble poxide hydrolase
Biochemistry
44
12179-12187
2005
Homo sapiens
brenda
Cronin, A.; Mowbray, S.; Duerk, H.; Homburg, S.; Fleming, I.; Fisslthaler, B.; Oesch, F.; Arand, M.
The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase
Proc. Natl. Acad. Sci. USA
100
1552-1557
2003
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Newman, J.W.; Morisseau, C.; Hammock, B.D.
Epoxide hydrolases: their roles and interactions with lipid metabolism
Prog. Lipid Res.
44
1-51
2005
Homo sapiens
brenda
Keserue, B.; Barbosa-Sicard, E.; Schermuly, R.T.; Tanaka, H.; Hammock, B.D.; Weissmann, N.; Fisslthaler, B.; Fleming, I.
Hypoxia-induced pulmonary hypertension: comparison of soluble epoxide hydrolase deletion vs. inhibition
Cardiovasc. Res.
85
232-240
2010
Mus musculus
brenda
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Release 2023.1 (January 2023)
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