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Literature summary extracted from

  • Hausmann, J.; Perrakis, A.; Moolenaar, W.H.
    Structure-function relationships of autotaxin, a secreted lysophospholipase D (2013), Adv. Biol. Regul., 53, 112-117.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.4.39 enzyme crystal structure analysis, PDB entry 2XR9., overview Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.4.39 extracellular the enzyme is secreted Rattus norvegicus
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Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.4.39 additional information Rattus norvegicus protein-protein interaction with proteins via the enzyme's SMB1 domain, which binds to the PDE domain. The enzyme binds to activated lymphocytes possibly involving an enzyme lymphocyte- and alpha4beta1-specific 458LDV460 motif. Autotaxin (ATX or ENPP2) is an ectonucleotide pyrophosphatase/phosphodiesterase that functions as a secreted lysophospholipase D to produce the multifunctional lipid mediator lysophosphatidic acid from more complex lysophospholipids ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.39 Rattus norvegicus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.39 1-alkyl-sn-glycero-3-phospho-L-serine + H2O
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 Rattus norvegicus 1-alkyl-sn-glycerol 3-phosphate + L-serine
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 ?
3.1.4.39 1-alkyl-sn-glycero-3-phosphocholine + H2O
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 Rattus norvegicus 1-alkyl-sn-glycerol 3-phosphate + choline
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 ?
3.1.4.39 1-alkyl-sn-glycero-3-phosphoethanolamine + H2O
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 Rattus norvegicus 1-alkyl-sn-glycerol 3-phosphate + ethanolamine
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 ?
3.1.4.39 additional information protein-protein interaction with proteins via the enzyme's SMB1 domain, which binds to the PDE domain. The enzyme binds to activated lymphocytes possibly involving an enzyme lymphocyte- and alpha4beta1-specific 458LDV460 motif. Autotaxin (ATX or ENPP2) is an ectonucleotide pyrophosphatase/phosphodiesterase that functions as a secreted lysophospholipase D to produce the multifunctional lipid mediator lysophosphatidic acid from more complex lysophospholipids Rattus norvegicus ?
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 ?
3.1.4.39 additional information the enzyme can produce bioactive lysophosphatidic acid from diverse lysophospholipid substrates, particularly lysophosphatidylcholine, the most abundant lysophospholipid in the circulation, but also from lysophosphatidylserine and lysophosphatidylethanolamine. It does not discriminate between phospholipid headgroups Rattus norvegicus ?
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 ?

Subunits

EC Number Subunits Comment Organism
3.1.4.39 More the enzyme structure is a tunnel that spans from the active site location to the opposite side of ATX. It is formed from the interaction between the SMB1 and the PDE domain Rattus norvegicus

Synonyms

EC Number Synonyms Comment Organism
3.1.4.39 ATX
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 Rattus norvegicus
3.1.4.39 autocrine motility factor
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 Rattus norvegicus
3.1.4.39 autotaxin
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 Rattus norvegicus
3.1.4.39 ectonucleotide pyrophosphatase/phosphodiesterase
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 Rattus norvegicus
3.1.4.39 ENPP
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 Rattus norvegicus
3.1.4.39 ENPP2
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 Rattus norvegicus
3.1.4.39 lysophospholipase D
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 Rattus norvegicus

General Information

EC Number General Information Comment Organism
3.1.4.39 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) Rattus norvegicus
3.1.4.39 additional information enzyme crystal structure analysis, phosphodiesterase domain and substrate binding pocket, overview, the enzyme structure is a tunnel that spans from the active site location to the opposite side of ATX. It is formed from the interaction between the SMB1 and the PDE domain. The tunnel may function as an lysophosphatidic acid binding site and, by inference, a product release site Rattus norvegicus
3.1.4.39 physiological function the enzyme is the major lysophosphatidic acid-producing enzyme being involved in a great diversity of (patho)physiological processes. Enzyme-produced lysophosphatidic acid acts on distinct G protein-coupled receptors thereby activating multiple signaling cascades and cellular responses. The ATX-LPA signaling axis is implicated in a remarkably wide variety of physiological and pathological processes, ranging from vascular and neural development to lymphocyte homing, fibrosis and cancer Rattus norvegicus