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Information on EC 3.1.3.106 - 2-lysophosphatidate phosphatase and Organism(s) Homo sapiens and UniProt Accession Q9NPH0
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3.1.3.106 2-lysophosphatidate phosphataseIUBMB Comments
The enzyme has been studied from the plants Arachis hypogaea (peanut) and Arabidopsis thaliana (thale cress) and from the yeast Saccharomyces cerevisiae. The enzyme from yeast, but not from the plants, requires Mg2+.
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Word Map
- 3.1.3.106
- phosphatases
- monoacylglycerol
- phospholipid
- acyltransferases
-
circadian
- glycerophospholipid
-
littermates
- diacylglycerol
-
rhythms
-
lplats
-
oscillate
- lysophospholipid
- phosphatidylcholine
-
kennedy
- propranolol
- n-ethylmaleimide
- choline
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
lpa phosphatase, phosphatidate phosphohydrolase 1, at3g03520, lysophosphatidic acid phosphatase type 6, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-acyl-sn-glycerol 3-phosphatase
-
-
-
-
CPC3
-
-
-
-
Phm8
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
1-acyl-sn-glycerol 3-phosphate phosphohydrolase
The enzyme has been studied from the plants Arachis hypogaea (peanut) and Arabidopsis thaliana (thale cress) and from the yeast Saccharomyces cerevisiae. The enzyme from yeast, but not from the plants, requires Mg2+.
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
1-oleoyl-sn-glycerol 3-phosphate + H2O
1-oleoyl-sn-glycerol + phosphate
-
-
-
?
myristoyl-sn-glycerol3-phosphate + H2O
myristoyl-sn-glycerol + phosphate
best substrate
-
-
?
oleoyl-sn-glycerol 3-phosphate + H2O
oleoyl-sn-glycerol + phosphate
about 2fold the activity of stearoyl-sn-glycerol 3-phosphate
-
-
?
palmitoyl-sn-glycerol 3-phosphate + H2O
palmitoyl-sn-glycerol + phosphate
-
-
-
?
stearoyl-sn-glycerol-3-phosphate + H2O
stearoyl-sn-glycerol + phosphate
-
-
-
?
1-arachidonoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-arachidonoyl-sn-glycerol + phosphate
1-hexanoyl-2-[6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl]-sn-glycero-3-phosphate + H2O
1-hexanoyl-2-[6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl]-sn-glycerol + phosphate
-
-
-
-
?
1-myristoyl-sn-glycerol 3-phosphate + H2O
1-myristoylglycerol + phosphate
-
-
-
?
1-palmitoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-palmitoyl-sn-glycerol + phosphate
-
-
-
-
?
1-stearoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-stearoyl-sn-glycerol + phosphate
-
-
-
-
?
1-stearoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-stearoylglycerol + phosphate
-
-
-
?
1-arachidonoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-arachidonoyl-sn-glycerol + phosphate
-
-
-
-
?
1-arachidonoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-arachidonoyl-sn-glycerol + phosphate
-
-
-
?
1-oleoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-oleoyl-sn-glycerol + phosphate
-
-
-
-
?
1-oleoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-oleoyl-sn-glycerol + phosphate
-
-
-
?
additional information
?
-
no substrate: glycerol 3-phosphate. Activity increases with the length of acyl chain to a peak value on 14:0-lysophosphatidic acid. Activity gradually decreases, when the substrate length is increased above the optimal 14:0-lysophosphatidic acid
-
-
?
additional information
?
-
-
no substrate: glycerol 3-phosphate. Activity increases with the length of acyl chain to a peak value on 14:0-lysophosphatidic acid. Activity gradually decreases, when the substrate length is increased above the optimal 14:0-lysophosphatidic acid
-
-
?
additional information
?
-
no substrate: phosphatidylglycerol phosphate
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, overview, LPP-1 regulates the lysophosphatidic acid-induced calcium release, NF-kappaB activation and interleukin-8 secretion in human bronchial epithelial cells
-
-
?
additional information
?
-
-
no substrates: dipalmitoyl phosphatidic acid, distearoyl phosphatidic acid
-
-
?
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
myristoyl-sn-glycerol3-phosphate + H2O
myristoyl-sn-glycerol + phosphate
best substrate
-
-
?
oleoyl-sn-glycerol 3-phosphate + H2O
oleoyl-sn-glycerol + phosphate
about 2fold the activity of stearoyl-sn-glycerol 3-phosphate
-
-
?
palmitoyl-sn-glycerol 3-phosphate + H2O
palmitoyl-sn-glycerol + phosphate
-
-
-
?
stearoyl-sn-glycerol-3-phosphate + H2O
stearoyl-sn-glycerol + phosphate
-
-
-
?
additional information
?
-
no substrate: glycerol 3-phosphate. Activity increases with the length of acyl chain to a peak value on 14:0-lysophosphatidic acid. Activity gradually decreases, when the substrate length is increased above the optimal 14:0-lysophosphatidic acid
-
-
?
additional information
?
-
-
no substrate: glycerol 3-phosphate. Activity increases with the length of acyl chain to a peak value on 14:0-lysophosphatidic acid. Activity gradually decreases, when the substrate length is increased above the optimal 14:0-lysophosphatidic acid
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, overview, LPP-1 regulates the lysophosphatidic acid-induced calcium release, NF-kappaB activation and interleukin-8 secretion in human bronchial epithelial cells
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
in absence of Mg2+ activity towards 1-stearoyl-2-lyso-sn-glycerol 3-phosphate acid is significantly decreased
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibitory: 1-palmitoyl-sn-glycerol, 1-hexadecanol
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Insulin
-
insulin therapy increases both PAP1 activity and lipin mRNA expression in diabetic patients
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
recombinant activity of wild-type and mutant enzymes in transformed cells
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
gain-of-function mutations in TP53 downregulate the lysophosphatidic acid phosphatase type 6 (ACP6), leading to upregulation of focal adhesion signaling in an lysophosphatidic acid-dependent manner. Highly expressed in normal fallopian tube epithelium, ACP6 expression is significantly reduced in ovarian cancer tumors and early in situ lesions
malfunction
-
suppression of cardiac PAP1 activity/lipin expression may contribute to metabolic dysfunction of the diabetic heart
physiological function
physiological function
-
atrial tissue displays PAP1 activity that is 33% lower in those having type 2 diabetes mellitus than in non-diabetic controls
physiological function
bifunctional enzyme displaying C-terminal epoxide hydrolase and N-terminal phosphatase activity. The phosphatase activity represents a 20-60% of lysophosphatidic acid cellular hydrolysis, especially in the cytosol
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). PPA6_HUMAN
428
0
48886
Swiss-Prot
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L289W
about 50% of wild-type activity with substrate myristoyl-sn-glycerol 3-phosphate
S285W
about 50% of wild-type activity with substrate myristoyl-sn-glycerol 3-phosphate
additional information
additional information
a mutant with deletion of the putative signal peptide has no catalytic activity
additional information
-
a mutant with deletion of the putative signal peptide has no catalytic activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of myc-tagged wild-type human and mouse LPP-1 isozyme or Myc-tagged human and mouse LPP-1 mutant R217K in primary bronchial epithelial cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
atrial lipin-1 and lipin-3 mRNA expression in diabetic patients is 50% and 59% lower as in non-diabetic patients, respectively
-
insulin therapy increases both PAP1 activity and lipin mRNA expression in diabetic patients
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
highly expressed in normal fallopian tube epithelium, ACP6 expression is significantly reduced in ovarian cancer tumors and early in situ lesions. Downregulation of ACP6 in ovarian cancer cells is necessary and sufficient to support high-grade serous ovarian cancer proliferation, adhesion, migration, and invasion
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhao, Y.; Usatyuk, P.V.; Cummings, R.; Saatian, B.; He, D.; Watkins, T.; Morris, A.; Spannhake, E.W.; Brindley, D.; Natarajan, V.
Lipid phosphate phosphatase-1 regulates the lysophosphatidic acid-induced calcium release, NF-kappaB activation and interleukin-8 secretion in human bronchial epithelial cells
Biochem. J.
385
493-502
2005
Homo sapiens, Mus musculus
Burgdorf, C.; Haensel, L.; Heidbreder, M.; Joehren, O.; Schuette, F.; Schunkert, H.; Kurz, T.
Suppression of cardiac phosphatidate phosphohydrolase 1 activity and lipin mRNA expression in Zucker diabetic fatty rats and humans with type 2 diabetes mellitus
Biochem. Biophys. Res. Commun.
390
165-170
2009
Homo sapiens, Rattus norvegicus
Morisseau, C.; Schebb, N.H.; Dong, H.; Ulu, A.; Aronov, P.A.; Hammock, B.D.
Role of soluble epoxide hydrolase phosphatase activity in the metabolism of lysophosphatidic acids
Biochem. Biophys. Res. Commun.
419
796-800
2012
Homo sapiens (P34913)
Oguro, A.; Imaoka, S.
Lysophosphatidic acids are new substrates for the phosphatase domain of soluble epoxide hydrolase
J. Lipid Res.
53
505-512
2012
Homo sapiens
Hiroyama, M.; Takenawa, T.
Isolation of a cDNA encoding human lysophosphatidic acid phosphatase that is involved in the regulation of mitochondrial lipid biosynthesis
J. Biol. Chem.
274
29172-29180
1999
Homo sapiens (Q9NPH0), Homo sapiens
Li, J.; Dong, Y.; Lue, X.; Wang, L.; Peng, W.; Zhang, X.C.; Rao, Z.
Crystal structures and biochemical studies of human lysophosphatidic acid phosphatase type 6
Protein Cell
4
548-561
2013
Homo sapiens (Q9NPH0), Homo sapiens
EXTERNAL LINKS (specific for EC-Number 3.1.3.106)
Transporter Classification Database (TCDB): 9.B.105.3.2
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