EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.4.39 | expressed in COS-7 cells | Mus musculus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.4.39 | DELTAA30-G41 | deletion mutants are generated from plasmid pcDNA-mATX, encompasses furin site | Mus musculus |
3.1.4.39 | DELTAA30-I33 | deletion mutants are generated from plasmid pcDNA-mATX, between signal peptidase and furin site | Mus musculus |
3.1.4.39 | DELTAA36-E40 | deletion mutants are generated from plasmid pcDNA-mATX | Mus musculus |
3.1.4.39 | DELTAC25 | deletion mutants are generated from plasmid pcDNA-mATX, amino acid -3 referring to the potential signal peptidase cleavage site | Mus musculus |
3.1.4.39 | DELTAE40-P43 | deletion mutants are generated from plasmid pcDNA-mATX | Mus musculus |
3.1.4.39 | DELTAG27 | deletion mutants are generated from plasmid pcDNA-mATX, amino acid -1 referring to the potential signal peptidase cleavage site | Mus musculus |
3.1.4.39 | DELTAG27-A30 | deletion mutants are generated from plasmid pcDNA-mATX, contain potential signal peptidase clevage site | Mus musculus |
3.1.4.39 | DELTAG27-R35 | deletion mutants are generated from plasmid pcDNA-mATX, encompasses both furin and signal peptidase cleavage sites | Mus musculus |
3.1.4.39 | DELTAL46-S49 | deletion mutants are generated from plasmid pcDNA-mATX | Mus musculus |
3.1.4.39 | DELTAN23 | deletion mutants are generated from plasmid pcDNA-mATX, amino acid -5 referring to the potential signal peptidase cleavage site | Mus musculus |
3.1.4.39 | DELTAN23-G27 | deletion mutants are generated from plasmid pcDNA-mATX, encompasses -1 and -3 amino acids referring to the potential signal peptidase clevage site | Mus musculus |
3.1.4.39 | DELTAN410 | deletion mutants are generated from plasmid pcDNA-mATX, contains a N-glycosylation site, point deletion of the amino-acid N410 inhibits lysophospholipase D activity of ATX, does not modify the ATX secretion and strongly inhibits ATX activity | Mus musculus |
3.1.4.39 | DELTAN53 | deletion mutants are generated from plasmid pcDNA-mATX, contains a N-glycosylation site, does not modify the ATX secretion and slightly reduces (25%) ATX activity | Mus musculus |
3.1.4.39 | DELTAN53/DELTAN410 | deletion mutants are generated from plasmid pcDNA-mATX, two N-glycosylation sites, double point deletion of the amino-acids N53 and N410 inhibits secretion of ATX, without altering the ATX amount in cell homogenate | Mus musculus |
3.1.4.39 | DELTAP43-L46 | deletion mutants are generated from plasmid pcDNA-mATX | Mus musculus |
3.1.4.39 | DELTAR32-R35 | deletion mutants are generated from plasmid pcDNA-mATX, furine site | Mus musculus |
3.1.4.39 | DELTAS49-N53 | deletion mutants are generated from plasmid pcDNA-mATX, contains N-glycosylation site | Mus musculus |
3.1.4.39 | DELTAV12-G27 | deletion mutants are generated from plasmid pcDNA-mATX, hydrophobic domain of signal peptide and signal peptide cleavage site, ATX secretion is suppressed | Mus musculus |
3.1.4.39 | DELTAV12-V22 | deletion mutants are generated from plasmid pcDNA-mATX, hydrophobic domain of signal peptide, ATX secretion is suppressed | Mus musculus |
3.1.4.39 | additional information | deletions of the amino acids N53 and N410 lead to a reduction of the molecular weight of ATX | Mus musculus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.4.39 | brefeldin-A | inhibitor of trans-Golgi transport, inhibits secretion of ATX | Mus musculus | |
3.1.4.39 | Globomycin | Treatment with the signal peptidase inhibitor inhibits ATX secretion by adipocytes treated for 6 h | Mus musculus | |
3.1.4.39 | lactacystin | proteasome inhibitor, restores the detection of ATX in cell homogenate of the mutants DELTAV12-V22 and DELTAV12-G27, Synthesis and secretion of ATX are highly dependent on the hydrophobic core of the signal peptide, but not on the amino acid composition the putative signal peptidase cleavage site | Mus musculus | |
3.1.4.39 | additional information | possible involement of furin in secretion of ATX by adipocytes tested, furin inhibitor decanoyl-ArgValLysArgchloromethylketone does not modify secretion or lysophospholipase D activity of ATX | Mus musculus | |
3.1.4.39 | N-glycosidase | treatment with N-glycosidase inhibits lysophospholipase D activity of ATX. N-glycosylation of ATX strongly influences its secretion and its lysoPLD activity | Mus musculus | |
3.1.4.39 | tunicamycin | inhibits secretion of ATX | Mus musculus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.1.4.39 | extracellular | results suggest that cell ATX behaves mainly as a soluble protein | Mus musculus | - |
- |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.1.4.39 | 120000 | - |
analyzed by Western blot, ATX is undetectable in conditioned media from undifferentiated 3T3F442A preadipocytes. Conditioned media treated with N-glycosidase and O-glycosidase, N-glycosidase leads to a reduction of 9.6 kDa apparent molecular weight of ATX, O-glycosidase is without influence | Mus musculus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.4.39 | lysophosphatidylcholine + H2O | Mus musculus | - |
lysophosphatidic acid + choline | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.4.39 | Mus musculus | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.1.4.39 | glycoprotein | - |
Mus musculus |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.4.39 | Western blot in cell homogenates requires a pre-purification with concanavalin A-sepharose | Mus musculus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.1.4.39 | adipocyte | Immunocyto-fluorescence microscopy reveals that ATX is detected in 3T3F442A adipocytes and is almost undetectable in 3T3F442A preadipocytes. 3T3F442A mouse preadipose cell line | Mus musculus | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.1.4.39 | additional information | - |
lysophospholipase D activity is measured by conversion of radiolabeled lysophosphatidylcholine into radiolabeled lysophosphatidic acid | Mus musculus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.4.39 | lysophosphatidylcholine + H2O | - |
Mus musculus | lysophosphatidic acid + choline | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.4.39 | ATX | - |
Mus musculus |
3.1.4.39 | autotaxin | - |
Mus musculus |
3.1.4.39 | ectonucleotide pyrophosphatase phosphodiesterase-2 | - |
Mus musculus |
3.1.4.39 | ENPP2 | - |
Mus musculus |
3.1.4.39 | lysophospholipase D | - |
Mus musculus |