Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.4.39 - alkylglycerophosphoethanolamine phosphodiesterase and Organism(s) Rattus norvegicus and UniProt Accession Q64610

for references in articles please use BRENDA:EC3.1.4.39
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Also acts on acyl and choline analogues.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
UNIPROT: Q64610
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
autotaxin (atx), lysophospholipase d, enpp2, ectonucleotide pyrophosphatase/phosphodiesterase, gdpd3, ectonucleotide pyrophosphatase/phosphodiesterase 2, heminecrolysin, pd-ialpha/atx, lyso-pld, atx/lysopld, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ectonucleotide pyrophosphatase/phosphodiesterase 2
-
lysophospholipase D
-
autocrine motility factor
-
-
ectonucleotide pyrophosphatase/phosphodiesterase
-
-
lyso-PLD
-
-
lysophospholipase D
lysophospholipase-D
-
-
lysoPLD
nucleotide pyrophosphatase/phosphodiesterase 2
-
-
phosphodiesterase, alkylglycerophosphorylethanolamine
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
1-alkyl-sn-glycero-3-phosphoethanolamine ethanolaminehydrolase
Also acts on acyl and choline analogues.
CAS REGISTRY NUMBER
COMMENTARY hide
62213-15-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
show the reaction diagram
-
-
-
?
1-alkyl-sn-glycero-3-phospho-L-serine + H2O
1-alkyl-sn-glycerol 3-phosphate + L-serine
show the reaction diagram
-
-
-
-
?
1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycero-3-phosphate + choline
show the reaction diagram
-
-
-
?
1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycerol 3-phosphate + choline
show the reaction diagram
-
-
-
-
?
1-alkyl-sn-glycero-3-phosphoethanolamine + H2O
1-alkyl-sn-glycero-3-phosphate + ethanolamine
show the reaction diagram
1-alkyl-sn-glycero-3-phosphoethanolamine + H2O
1-alkyl-sn-glycerol 3-phosphate + ethanolamine
show the reaction diagram
-
-
-
-
?
1-heptadecanoyl-sn-glycero-3-phosphocholine + H2O
1-heptadecanoyl-sn-glycerol 3-phosphate + choline
show the reaction diagram
-
-
-
-
?
1-linoleoyl-2-lyso-glycerophoshorylcholine + H2O
1-linoleoyl-sn-glycerol-3-phosphate + choline
show the reaction diagram
-
-
-
-
?
1-linoleoyl-sn-glycero-3-phosphocholine + H2O
1-linoleoyl-sn-glycerol 3-phosphate + choline
show the reaction diagram
-
-
-
-
?
1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-2-lyso-sn-glycero-3-phosphate + choline
show the reaction diagram
1-O-alkyl-2-lyso-sn-glycero-3-phosphoethanolamine + H2O
1-O-alkyl-2-lyso-sn-glycero-3-phosphate + ethanolamine
show the reaction diagram
-
the microsomal enzyme
the microsomal enzyme
?
1-O-hexadecyl-2-lyso-glycerophosphorylcholine + H2O
1-O-hexadecyl-sn-glycerol-3-phosphate + choline
show the reaction diagram
-
lysoPAF (alkyl-lysophosphatidylcholine), lysoPLD shows higher activity towards lysoPAF
-
-
?
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + choline
show the reaction diagram
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphoethanolamine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + ethanolamine
show the reaction diagram
1-O-octadecyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-octadecyl-2-lyso-sn-glycero-3-phosphate + choline
show the reaction diagram
-
-
-
?
1-palmitoyl-2-lyso-glycerophoshorylcholine + H2O
1-palmitoyl-sn-glycerol-3-phosphate + choline
show the reaction diagram
-
-
-
-
?
1-palmitoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-sn-glycerol 3-phosphate + choline
show the reaction diagram
-
-
-
-
?
1-stearoyl-2-lyso-glycerophoshorylcholine + H2O
1-stearoyl-sn-glycerol-3-phosphate + choline
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-TMP + H2O
4-nitrophenol + TMP
show the reaction diagram
-
-
-
-
?
lysophosphatidylcholine + H2O
lysophosphatic acid + choline
show the reaction diagram
-
LPC, purified enzyme hydrolyzes saturated forms of lysophosphatidylcholine more robustly than unsaturated forms
-
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
show the reaction diagram
-
-
-
-
?
platelet-activating factor + H2O
? + choline
show the reaction diagram
-
PAF, same extent as palmityl-lysophosphatidylcholine
-
-
?
sphingosylphosphorylcholine + H2O
sphingosine-1-phosphate + choline
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
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
show the reaction diagram
-
-
-
?
1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-2-lyso-sn-glycero-3-phosphate + choline
show the reaction diagram
-
may play a role in the metabolism of platelet-activating factor
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
required, active site bound
Ca2+
-
microsomal enzyme
KSCN
-
200 mM, 37% increase of activity
Na3VO4
-
enzyme activity requires Na3VO4, not necessary after purification
NaCl
-
200 mM, 37% increase of activity
Ni2+
-
extracellular enzyme
Zn2+
-
extracellular enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
HA155
the boron atom on one end of the inhibitor forms a reversible covalent bond with the nucleophile hydroxyl group of Thr209. One of the two boron hydroxyl groups is further stabilized between the two zinc ions, binding structure, overview
Cu2+
-
the inhibition of extracellular enzyme can be prevented by 2,6-di-tert-butyl-4-hydroxy-methylphenol
G protein
-
G protein exhibits lysoPLD activity, lysoPLD activity is highly associated with heterotrimeric G protein
-
iodoacetamide
-
-
N-ethylmaleimide
-
-
NaF
-
slight inhibition
p-hydroxymercuribenzoate
serine esterase inhibitors
-
inhibition of extracellular enzyme
-
sodium cholate
-
16 mM, 77% inhibition
sodium deoxycholate
-
6 mM, 100% inhibition
Triton X-100
-
0.3 mM, 64% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0083
1-linoleoyl-2-lyso-glycerophoshorylcholine
-
Vmax is 0.019 micromol/min/mg
0.0267
1-O-hexadecyl-2-lyso-glycerophosphorylcholine
-
Vmax is 0.29 micromol/min/mg, lysoPLD activity is more than twice that observed with 1-palmitoyl-glycerophoshorylcholine
0.0207
1-palmitoyl-2-lyso-glycerophoshorylcholine
-
Vmax is 0.059 micromol/min/mg
0.176
1-palmitoyl-glycerophoshorylcholine
-
Vmax is 0.3 micromol/min/mg, best substrate
0.101
1-stearoyl-2-lyso-glycerophoshorylcholine
-
Vmax is 0.035 micromol/min/mg
additional information
additional information
-
suggestion that lysoPLD predominantly utilizes saturated forms of lysophosphatidylcholine
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000005 - 0.000076
-
depending on presence of divalent cations
0.00009
-
lung
0.0002
-
testis
0.00022
-
liver
0.00034
-
kidney
0.00037
-
intestine
0.036
-
using isotopic assay
0.048
-
colorimetric assay, 6 h incubation, 37°C
0.14
-
purified enzyme, HiTrap DEAE FF
additional information
-
nuclear fraction has relatively high levels of lysoPLD activity. Both lysoPLD activity and highest band density found in microsomal fraction
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
7 - 7.5
-
highest enzyme activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
embryonic spinal cord
Manually annotated by BRENDA team
-
during embryonic development. In vivo expression of autotaxin in the brain during development and following neurotrauma
Manually annotated by BRENDA team
additional information
-
secreted cell motility-stimulating exo-phosphodiesterase with lysophospholipase D activity. Distribution of autotaxin in the developing and lesioned brain, function of autotaxin in oligodendrocyte precursor cells and brain injuries. Visual localization of NPP-2 in the brain. Developmental regulation of ATX. Cellular and subcellular distribution of ATX shown. These data indicate that ATX expression commences prior to the onset of myelin protein expression and myelination in the brain. Developmental regulation of autotaxin (ATX) mRNA expression in the brain. ATX is expressed in early and late oligodendrocyte precursor cells (OPCs). ATX is up-regulated and cell-type-specifically expressed following neurotrauma
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
expressed in the choroid plexus and secreted into the cerebrospinal fluid, not expressed on the cell surface
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
evolution
-
the enzyme belongs to the ENPP family, but ATX/ENPP2 is a unique lysoPLD with no functional redundancy within the ENPP family, overview. The enzyme and its ENPP family members can be divided into two main subgroups, namely ENPP1-3 and ENPP4-7. ATX/ENPP2 and its closest relatives, ENPP1 and ENPP3, have two N-terminal somatomedin B (SMB)-like domains, a central phosphodiesterase (PDE) domain and a C-terminal nuclease (NUC)-like domain. The second subgroup (ENPP4-7) has only the PDE domain in common. ATX/NPP2 is a secreted protein, while the other ENPPs are transmembrane proteins, either type-I (ENPP4-7) or type-II (ENPP1-3)
malfunction
-
fasting decreases enzyme activity. Nutritional deficiency of 18 : 2- and 18 : 1-containing phosphatidylcholines causes selective reduction of corresponding unsaturated lysophosphatidylcholines relative to other species in the blood circulation. Prolonged fasting of rats causes a greater decrease in the level of lysophosphatidylcholine in the liver than that of phosphatidylethanolamine
metabolism
-
in contrast to the decreased plasma enzyme activity in fasted rats, lysophosphatidic acid production from lysophosphatidylcholine by the enzyme activity progressively increases
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ENPP2_RAT
887
1
101576
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
125000
SDS-PAGE immunoblot, deglycosylation of Myc-tagged rat NPP2 with N-glycosidase F increase their mobility during SDS-PAGE
115000
-
immunoblotting, cell lysate
120000
125000
-
extracellular enzyme which is originally identified as an autocrine tumor cell motility stimulating factor overexpressed in a variety of human cancers including primary brain tumors
35000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 35000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain of NPP2 modeled on the known crystal structure of NPP from Xanthomonas axonopodis. Catalytic activity of NPP2 is critically dependent on the presence of a Man8/9GlcNAc2 moiety on Asn-524, a site that is phylogenetically conserved, not only in NPP2 but also in six of seven NPP isozymes. Suggestion that this glycan chain has a structural function and is involved in the interaction between the catalytic and nuclease-like domains of NPP2
purified recombinant ATX, hanging drop vapour diffusion method, usage of crystallization solution 0.1 M MIB buffer, pH 8, 25% w/v PEG 1500, or 0.1 M MIB buffer, pH 9, 25% w/v PEG 1500, or 0.2 M sodium citrate, 20% w/v PEG 3350, X-ray diffraction structure determination and analysis at 2.0-2.6 A resolution
purified recombinant enzyme, ATX alone and in complex with a small-molecule inhibitor HA155, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement and single-wavelength anomalous dispersion
enzyme crystal structure analysis, PDB entry 2XR9., overview
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A218V
site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type
A305E
site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type
F211A
site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type
F274E
site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type
F275Q
site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type
L214H
site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type
N398A
NPP2 site-directed mutagenesis
N398A/N410A/N524A/N806A
NPP2 mutant
N410A
increased mobility during SDS-PAGE is only noted following the mutation of sites N53A, N410A, and N524A, indicating that these are the only true glycosylation sites. Mutation of each of the corresponding asparagines into an alanine and examination of the effects of these mutations on the mobility of NPP2 during SDS-PAGE and on its enzymatic activities. Efficient chemoattractant for NIH-3T3 cells
N524A
mutation of N524A causes an accumulation of NPP2 in the cells, suggesting that the glycosylation of Asn-524 also contributes to the maturation and/or trafficking of NPP2. Only the mutation of N524A abolishes the nucleotide and lysophospholipid phosphodiesterase activities of NPP2, showing that the glycosylation of Asn-524 is required for the expression of catalytic activity. Increased mobility during SDS-PAGE is only noted following the mutation of sites N53A, N410A, and N524A, indicating that these are the only true glycosylation sites. Mutation of each of the corresponding asparagines into an alanine and examinations of the effects of these mutations on the mobility of NPP2 during SDS-PAGE and on its enzymatic activities. Does not measurably stimulate cell motility
N53A
increased mobility during SDS-PAGE is only noted following the mutation of sites N53A, N410A, and N524A, indicating that these are the only true glycosylation sites. Mutation of each of the corresponding asparagines into an alanine and examination of the effects of these mutations on the mobility of NPP2 during SDS-PAGE and on its enzymatic activities. Efficient chemoattractant for NIH-3T3 cells
N53A/N398A/N410A/N524A
NPP2 mutant
N53A/N398A/N410A/N524A/N806A
NPP2 with sites 1–5 mutated, does not measurably stimulate cell motility
N53A/N398A/N410A/N806A
NPP2 with sites 1, 2, 3 and 5 mutated,only glycosylated on Asn-524
N53A/N398A/N524A/N806A
NPP2 mutant
N53A/N410A/N524A/N806A
NPP2 mutant
N806A
NPP2, site-directed mutagenesis not appendant on catalytic domain
S170E
site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type
Y307Q
site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type
C194A
-
the mutant shows a specific activity similar to the wild type enzyme
C366A
-
the mutant shows a specific activity similar to the wild type enzyme
C413A
-
weakly active
C468A
-
the mutant shows a specific activity similar to the wild type enzyme
C513A
-
the mutant shows a specific activity similar to the wild type enzyme
C651A
-
the mutant shows a specific activity similar to the wild type enzyme
C666A
-
the mutant shows a specific activity similar to the wild type enzyme
C774A
-
the mutant shows a specific activity similar to the wild type enzyme
C784A
-
the mutant shows a specific activity similar to the wild type enzyme
C805A
-
weakly active
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57
-
5 min, 85% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant ATX from HEK-293 cell culture supernatant
includes a protease inhibitor at all steps to avoid isolation of the products of proteolysis. Purified to apparent homogeneity from rat brain nuclear fractions using 1-[14C]palmitoyl-glycerophosphorylcholine as a substrate
-
native enzyme from brain nuclear fractions by anion exchange chromatography, gel filtration, and again anion exchange chromatography
-
using GSH-Sepharose
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
stable expression of ATX in HEK-293 cells with secretion of the recombinnat enzyme
COS-7 cells (ATCC: CRL-1651) and HEK 293 cells. To gain further insight into the possible functional role of ATX in the brain, analysis of its cellular expression in the brain under physiological conditions and following trauma. Preparation and purification of oligodendrocyte precursor cells: Primary mixed glial cultures are prepared from the cerebral hemispheres of P0–P2 Sprague-Dawley rat pups from which the meninges has been stripped
-
expressed in HEK-293 cells
-
expressed in HEK-293T cells
-
expression in Escherichia coli DH5alpha
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
additional information
-
regulates cell growth, motility, and angiogenesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fernandez-Gallardo, S.; Gijon, M.A.; Gracia, M.D.C.; Cano, E.; Sanchez Crespo, M.
Biosynthesis of platelet-activating factor in glandular gastric mucosa. Evidence for the involvement of the de novo pathway and modulation by fatty acids
Biochem. J.
254
707-714
1988
Rattus norvegicus
Manually annotated by BRENDA team
Tokumura, A.; Harada, K.; Fukazawa, K.; Tsukatani, H.
Involvement of lysophospholipase D in the production of lysophosphatidic acid in rat plasma
Biochim. Biophys. Acta
875
31-38
1986
Rattus norvegicus
Manually annotated by BRENDA team
Wykle, R.L.; Kraemer, W.F.; Schremmer, J.M.
Specificity of lysophospholipase D
Biochim. Biophys. Acta
619
58-67
1980
Rattus norvegicus
Manually annotated by BRENDA team
Wykle, R.L.; Kraemer, W.F.; Schremmer, J.M.
Studies of lysophospholipase D of rat liver and other tissues
Arch. Biochem. Biophys.
184
149-155
1977
Rattus norvegicus
Manually annotated by BRENDA team
Wykle, R.L.; Schremmer, J.M.
A lysophospholipase D pathway in the metabolism of ether-linked lipids in brain microsomes
J. Biol. Chem.
249
1742-1746
1974
Rattus norvegicus
Manually annotated by BRENDA team
Tokumura, A.; Nishioka, Y.; Yoshimoto, O.; Shinomiya, J.; Fukazawa, K.
Substrate specificity of lysophospholipase D which produces bioactive lysophosphatidic acids in rat plasma
Biochim. Biophys. Acta
1437
235-245
1999
Rattus norvegicus
Manually annotated by BRENDA team
Furukawa, M.; Muguruma, k.; Frenkel, R.A.; Johnston, J.M.
Metabolic fate of platelet-activating factor in the rat enterocyte: the role of a specifiv lysophospholipase D
Arch. Biochem. Biophys.
319
274-280
1995
Rattus norvegicus
Manually annotated by BRENDA team
Wykle, L.; Strum, J.C.
Lysophospholipase D
Methods Enzymol.
197
583-590
1991
Rattus norvegicus
Manually annotated by BRENDA team
Xie, Y.; Meier, K.E.
Lysophospholipase D and its role in LPA production
Cell. Signal.
16
975-981
2004
Bos taurus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Koike, S.; Keino-Masu, K.; Ohto, T.; Masu, M.
The N-terminal hydrophobic sequence of autotaxin (ENPP2) functions as a signal peptide
Genes Cells
11
133-142
2006
Rattus norvegicus
Manually annotated by BRENDA team
Jansen, S.; Stefan, C.; Creemers, J.W.; Waelkens, E.; Van Eynde, A.; Stalmans, W.; Bollen, M.
Proteolytic maturation and activation of autotaxin (NPP2), a secreted metastasis-enhancing lysophospholipase D
J. Cell Sci.
118
3081-3089
2005
Rattus norvegicus
Manually annotated by BRENDA team
Sugimoto, S.; Sugimoto, H.; Aoyama, C.; Aso, C.; Mori, M.; Izumi, T.
Purification and characterization of lysophospholipase D from rat brain
Biochim. Biophys. Acta
1761
1410-1418
2006
Rattus norvegicus
Manually annotated by BRENDA team
Savaskan, N.E.; Rocha, L.; Kotter, M.R.; Baer, A.; Lubec, G.; van Meeteren, L.A.; Kishi, Y.; Aoki, J.; Moolenaar, W.H.; Nitsch, R.; Braeuer, A.U.
Autotaxin (NPP-2) in the brain: cell type-specific expression and regulation during development and after neurotrauma
Cell. Mol. Life Sci.
64
230-243
2007
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Jansen, S.; Callewaert, N.; Dewerte, I.; Andries, M.; Ceulemans, H.; Bollen, M.
An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D
J. Biol. Chem.
282
11084-11091
2007
Rattus norvegicus (Q64610)
Manually annotated by BRENDA team
Jansen, S.; Andries, M.; Vekemans, K.; Vanbilloen, H.; Verbruggen, A.; Bollen, M.
Rapid clearance of the circulating metastatic factor autotaxin by the scavenger receptors of liver sinusoidal endothelial cells
Cancer Lett.
284
216-221
2009
Rattus norvegicus
Manually annotated by BRENDA team
Jansen, S.; Andries, M.; Derua, R.; Waelkens, E.; Bollen, M.
Domain interplay mediated by an essential disulfide linkage is critical for the activity and secretion of the metastasis-promoting enzyme autotaxin
J. Biol. Chem.
284
14296-14302
2009
Rattus norvegicus
Manually annotated by BRENDA team
Hausmann, J.; Christodoulou, E.; Kasiem, M.; De Marco, V.; van Meeteren, L.A.; Moolenaar, W.H.; Axford, D.; Owen, R.L.; Evans, G.; Perrakis, A.
Mammalian cell expression, purification, crystallization and microcrystal data collection of autotaxin/ENPP2, a secreted mammalian glycoprotein
Acta Crystallogr. Sect. F
66
1130-1135
2010
Rattus norvegicus (Q64610)
Manually annotated by BRENDA team
Aoyama, C.; Sugimoto, H.; Ando, H.; Yamashita, S.; Horibata, Y.; Sugimoto, S.; Satou, M.
The heterotrimeric G protein subunits Galphaq and Gbeta1 have lysophospholipase D activity
Biochem. J.
440
241-250
2011
Rattus norvegicus
Manually annotated by BRENDA team
Hausmann, J.; Kamtekar, S.; Christodoulou, E.; Day, J.E.; Wu, T.; Fulkerson, Z.; Albers, H.M.; van Meeteren, L.A.; Houben, A.J.; van Zeijl, L.; Jansen, S.; Andries, M.; Hall, T.; Pegg, L.E.; Benson, T.E.; Kasiem, M.; Harlos, K.; Kooi, C.W.; Smyth, S.S.; Ovaa, H.; Bollen, M.; Morris, A.J.; Moolenaar, W.H.; Perrakis, A.
Structural basis of substrate discrimination and integrin binding by autotaxin
Nat. Struct. Mol. Biol.
18
198-204
2011
Rattus norvegicus (Q64610)
Manually annotated by BRENDA team
Hausmann, J.; Perrakis, A.; Moolenaar, W.H.
Structure-function relationships of autotaxin, a secreted lysophospholipase D
Adv. Biol. Regul.
53
112-117
2013
Rattus norvegicus
Manually annotated by BRENDA team
Ino, M.; Shimizu, Y.; Tanaka, T.; Tokumura, A.
Alterations of plasma levels of lysophosphatidic acid in response to fasting of rats
Biol. Pharm. Bull.
35
2059-2063
2012
Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team