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FEBS Lett. 2003 Mar 13;538(1-3):60-4.

The hydrolysis of lysophospholipids and nucleotides by autotaxin (NPP2) involves a single catalytic site.

Author information

1
Afdeling Biochemie, Faculteit Geneeskunde, University of Leuven, Herestraat 49, B-3000 Leuven, Belgium.

Abstract

Autotaxin (NPP2) is a tumor cell motility-stimulating factor that displays both a nucleotide pyrophosphatase/phosphodiesterase activity and a recently described lysophospholipase D activity. The hydrolysis of nucleotides is a metal-assisted reaction that occurs via a nucleotidylated threonine in the catalytic site. We show here that the catalytic site threonine and the metal-coordinating residues are also essential for the hydrolysis of lysophospholipids. In comparing the substrate specificity of NPP2 and the closely related NPP1 and NPP3, we found that only NPP2 displayed a lysophospholipase D activity, whereas NPP1 and NPP3 had a much higher nucleotide pyrophosphatase activity.

PMID:
12633853
DOI:
10.1016/s0014-5793(03)00133-9
[Indexed for MEDLINE]
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