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Literature summary for 3.1.4.39 extracted from
- Autotaxin: structure-function and signaling (2014), J. Lipid Res., 55, 1010-1018.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| heparin | enhances the lysoPLD activity of isozyme ATXalpha toward lysophosphatidylcholine up to 2fold, but it has no detectable effect on the activity of isozyme ATXbeta | Mus musculus |  |
| heparin | enhances the lysoPLD activity of isozyme ATXalpha toward lysophosphatidylcholine up to 2fold, but it has no detectable effect on the activity of isozyme ATXbeta | Homo sapiens | |
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | the enzyme is a good target for small molecule inhibitors | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| PF8380 | the inhibitor shows adequate oral bioavailability and potency in reducing lysophosphatidic acid levels in plasma and at sites of infl ammation | Homo sapiens | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | the enzyme is a secreted | Mus musculus | - |
- |
| extracellular | the enzyme is a secreted | Homo sapiens | - |
- |
| extracellular | the enzyme is a secreted | Streptomyces chromofuscus | - |
- |
| extracellular | the enzyme is a secreted | Loxosceles sp. | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the catalytic domain shows a characteristic bimetallic active site | Mus musculus | |
| additional information | the catalytic domain shows a characteristic bimetallic active site | Homo sapiens | |
| additional information | the catalytic domain shows a characteristic bimetallic active site | Streptomyces chromofuscus | |
| additional information | the catalytic domain shows a characteristic bimetallic active site | Loxosceles sp. |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1-alkyl-sn-glycero-3-phosphocholine + H2O | Mus musculus | - |
1-alkyl-sn-glycerol 3-phosphate + choline | - |
? | |
| 1-alkyl-sn-glycero-3-phosphocholine + H2O | Homo sapiens | - |
1-alkyl-sn-glycerol 3-phosphate + choline | - |
? | |
| additional information | Mus musculus | the enzyme hydrolyzes extracellular lysophospholipids into the lipid mediator lysophosphatidic acid, a ligand for specific G protein-coupled receptors | ? | - |
? | |
| additional information | Homo sapiens | the enzyme hydrolyzes extracellular lysophospholipids into the lipid mediator lysophosphatidic acid, a ligand for specific G protein-coupled receptors | ? | - |
? | |
| additional information | Streptomyces chromofuscus | the enzyme hydrolyzes extracellular lysophospholipids into the lipid mediator lysophosphatidic acid, a ligand for specific G protein-coupled receptors | ? | - |
? | |
| additional information | Loxosceles sp. | the enzyme hydrolyzes extracellular lysophospholipids into the lipid mediator lysophosphatidic acid, a ligand for specific G protein-coupled receptors | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
isozymes ATXalpa-ATXdelta | - |
| Loxosceles sp. | - |
- |
- |
| Mus musculus | - |
isozymes ATXalpa-ATXdelta | - |
| Streptomyces chromofuscus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| plasma | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1-alkyl-sn-glycero-3-phosphocholine + H2O | - |
Mus musculus | 1-alkyl-sn-glycerol 3-phosphate + choline | - |
? | |
| 1-alkyl-sn-glycero-3-phosphocholine + H2O | - |
Homo sapiens | 1-alkyl-sn-glycerol 3-phosphate + choline | - |
? | |
| additional information | the enzyme hydrolyzes extracellular lysophospholipids into the lipid mediator lysophosphatidic acid, a ligand for specific G protein-coupled receptors | Mus musculus | ? | - |
? | |
| additional information | the enzyme hydrolyzes extracellular lysophospholipids into the lipid mediator lysophosphatidic acid, a ligand for specific G protein-coupled receptors | Homo sapiens | ? | - |
? | |
| additional information | the enzyme hydrolyzes extracellular lysophospholipids into the lipid mediator lysophosphatidic acid, a ligand for specific G protein-coupled receptors | Streptomyces chromofuscus | ? | - |
? | |
| additional information | the enzyme hydrolyzes extracellular lysophospholipids into the lipid mediator lysophosphatidic acid, a ligand for specific G protein-coupled receptors | Loxosceles sp. | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | domain structure of the major ATX isoforms, overview | Mus musculus |
| More | domain structure of the major ATX isoforms, overview | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ATX | - |
Mus musculus |
| ATX | - |
Homo sapiens |
| ATX | - |
Streptomyces chromofuscus |
| ATX | - |
Loxosceles sp. |
| autotaxin | - |
Mus musculus |
| autotaxin | - |
Homo sapiens |
| autotaxin | - |
Streptomyces chromofuscus |
| autotaxin | - |
Loxosceles sp. |
| ecto-nucleotide pyrophosphatase/phosphodiesterase-2 | - |
Mus musculus |
| ecto-nucleotide pyrophosphatase/phosphodiesterase-2 | - |
Homo sapiens |
| ecto-nucleotide pyrophosphatase/phosphodiesterase-2 | - |
Streptomyces chromofuscus |
| ecto-nucleotide pyrophosphatase/phosphodiesterase-2 | - |
Loxosceles sp. |
| lysophospholipase D | - |
Mus musculus |
| lysophospholipase D | - |
Homo sapiens |
| lysophospholipase D | - |
Streptomyces chromofuscus |
| lysophospholipase D | - |
Loxosceles sp. |
| lysoPLD | - |
Mus musculus |
| lysoPLD | - |
Homo sapiens |
| lysoPLD | - |
Streptomyces chromofuscus |
| lysoPLD | - |
Loxosceles sp. |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the catalytic domain shows shallow groove and a deep hydrophobic pocket, and an open tunnel, which forms a sort of T-junction with the shallow groove, substrate binding structure, overview. The enzyme contains a SMB domain that mediates the binding to cell surface integrins | Mus musculus |
| additional information | the tripartite catalytic domain shows shallow groove and a deep hydrophobic pocket, and an open tunnel, which forms a sort of T-junction with the shallow groove, substrate binding structure, overview. The enzyme contains a SMB domain that mediates the binding to cell surface integrins | Homo sapiens |
| physiological function | the enzyme is the primary lysophosphatidic acid-producing phospholipase. Enzyme-lysophosphatidic acid signaling is essential for development and has been implicated in a great diversity of (patho)physiological processes, ranging from lymphocyte homing to tumor progression. Isozyme ATX alpha but not ATX beta binds abundantly to cultured mammalian cells in a manner strictly dependent on heparan sulfate. By mediating bindings to heparan sulfate proteoglycans, the isozyme ATXalpha insertion loop likely serves to target LPA production close to the lysophosphatidic acid receptors | Homo sapiens |
| physiological function | the enzyme is the primary lysophosphatidic acid-producing phospholipase. Enzyme-lysophosphatidic acid, ATX-LPA, signaling is essential for development and has been implicated in a great diversity of (patho)physiological processes, ranging from lymphocyte homing to tumor progression. Isozyme ATX alpha but not ATX beta binds abundantly to cultured mammalian cells in a manner strictly dependent on heparan sulfate. By mediating bindings to heparan sulfate proteoglycans, the isozyme ATXalpha insertion loop likely serves to target LPA production close to the lysophosphatidic acid receptors | Mus musculus |
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