FEBS Letters | |
The hydrolysis of lysophospholipids and nucleotides by autotaxin (NPP2) involves a single catalytic site | |
Arai, Hiroyuki1  Bollen, Mathieu2  Gijsbers, Rik2  Aoki, Junken1  | |
[1] Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan;Afdeling Biochemie, Faculteit Geneeskunde, University of Leuven, Herestraat 49, B-3000 Leuven, Belgium | |
关键词: NPP; Nucleotide pyrophosphatase/phosphodiesterase; Lysophospholipase D; Autotaxin; Cell motility; Catalytic mechanism; PC-1; NPP; nucleotide pyrophosphatase/phosphodiesterase; pNPP; p-nitrophenylphosphate; bis-pNPP; bis(p-nitrophenyl)phosphate; pNP-TMP; p-nitrophenyl thymidine 5′-monophosphate; lysoPC; lysophosphatidylcholine; lysoPA; lysophosphatidic acid; | |
DOI : 10.1016/S0014-5793(03)00133-9 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
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