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

Rik Gijsbers, Junken Aoki, Hiroyuki Arai, Mathieu Bollen

Research output: Contribution to journalArticlepeer-review

96 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)60-64
Number of pages5
JournalFEBS Letters
Volume538
Issue number1-3
DOIs
Publication statusPublished - 2003 Mar 13
Externally publishedYes

Keywords

  • Autotaxin
  • Catalytic mechanism
  • Cell motility
  • Lysophospholipase D
  • NPP
  • Nucleotide pyrophosphatase/phosphodiesterase
  • PC-1

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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