Literature summary for 3.1.4.39 extracted from

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 (2007), J. Biol. Chem., 282, 11084-11091.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Protein Variants

Protein Variants	Comment	Organism
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
N398A	NPP2 site-directed mutagenesis	Rattus norvegicus
N398A/N410A/N524A/N806A	NPP2 mutant	Rattus norvegicus
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
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
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
N53A/N398A/N410A/N524A	NPP2 mutant	Rattus norvegicus
N53A/N398A/N410A/N524A/N806A	NPP2 with sites 15 mutated, does not measurably stimulate cell motility	Rattus norvegicus
N53A/N398A/N410A/N806A	NPP2 with sites 1, 2, 3 and 5 mutated,only glycosylated on Asn-524	Rattus norvegicus
N53A/N398A/N524A/N806A	NPP2 mutant	Rattus norvegicus
N53A/N410A/N524A/N806A	NPP2 mutant	Rattus norvegicus
N806A	NPP2, site-directed mutagenesis not appendant on catalytic domain	Rattus norvegicus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	secreted by various cell types in vertebrates	Rattus norvegicus	-	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
125000	-	SDS-PAGE immunoblot, deglycosylation of Myc-tagged rat NPP2 with N-glycosidase F increase their mobility during SDS-PAGE	Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
lysophosphatidylcholine + H2O	Rattus norvegicus	-	lysophosphatidic acid + choline	-	?

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	Q64610	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
lysophosphatidylcholine + H2O	-	Rattus norvegicus	lysophosphatidic acid + choline	-	?

Synonyms

Synonyms	Comment	Organism
autotaxin	-	Rattus norvegicus
ectonucleotide pyrophosphatase/phosphodiesterase 2	-	Rattus norvegicus
lysophospholipase D	-	Rattus norvegicus
NPP2	-	Rattus norvegicus