EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.1.4.39 | 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 | Rattus norvegicus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.4.39 | additional information | five potential N-glycosylation sites of NPP2, Asn-53, Asn-398, Asn-410, Asn-524, and Asn-806. Mutagenesis and deglycosylation experiments reveal that only the glycosylation of Asn-524 is essential for the expression of the catalytic and motility-stimulating activities of NPP2 | Rattus norvegicus |
3.1.4.39 | N398A | NPP2 site-directed mutagenesis | Rattus norvegicus |
3.1.4.39 | N398A/N410A/N524A/N806A | NPP2 mutant | Rattus norvegicus |
3.1.4.39 | 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 | Rattus norvegicus |
3.1.4.39 | 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 | Rattus norvegicus |
3.1.4.39 | 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 | Rattus norvegicus |
3.1.4.39 | N53A/N398A/N410A/N524A | NPP2 mutant | Rattus norvegicus |
3.1.4.39 | N53A/N398A/N410A/N524A/N806A | NPP2 with sites 15 mutated, does not measurably stimulate cell motility | Rattus norvegicus |
3.1.4.39 | N53A/N398A/N410A/N806A | NPP2 with sites 1, 2, 3 and 5 mutated,only glycosylated on Asn-524 | Rattus norvegicus |
3.1.4.39 | N53A/N398A/N524A/N806A | NPP2 mutant | Rattus norvegicus |
3.1.4.39 | N53A/N410A/N524A/N806A | NPP2 mutant | Rattus norvegicus |
3.1.4.39 | N806A | NPP2, site-directed mutagenesis not appendant on catalytic domain | Rattus norvegicus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.1.4.39 | extracellular | secreted by various cell types in vertebrates | Rattus norvegicus | - |
- |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.1.4.39 | 125000 | - |
SDS-PAGE immunoblot, deglycosylation of Myc-tagged rat NPP2 with N-glycosidase F increase their mobility during SDS-PAGE | Rattus norvegicus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.4.39 | lysophosphatidylcholine + H2O | Rattus norvegicus | - |
lysophosphatidic acid + choline | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.4.39 | Rattus norvegicus | Q64610 | - |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.1.4.39 | glycoprotein | N-glycosylation of NPP2 is essential for the expression of its catalytic activity. Lysophospholipase-D activity and the nucleotide phosphodiesterase activity of rat are abolished by deglycosylation. Examination of the structure of the essential glycan side chain of Asn524. 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 | Rattus norvegicus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.4.39 | lysophosphatidylcholine + H2O | - |
Rattus norvegicus | lysophosphatidic acid + choline | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.4.39 | autotaxin | - |
Rattus norvegicus |
3.1.4.39 | ectonucleotide pyrophosphatase/phosphodiesterase 2 | - |
Rattus norvegicus |
3.1.4.39 | lysophospholipase D | - |
Rattus norvegicus |
3.1.4.39 | NPP2 | - |
Rattus norvegicus |