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Gene Review:

LPP1 - phosphatidate phosphatase LPP1

Saccharomyces cerevisiae S288c

Synonyms: D9719.9, Lipid phosphate phosphatase 1, Phosphatidate phosphatase, YDR503C

Fernandez, F. et al., Toke, D.A. et al., Carman, G.M. et al., Furneisen, J.M. et al., Faulkner, A. et al., et al.

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High impact information on LPP1

Phosphatidate phosphatase (PAP) enzymes catalyze the dephosphorylation of phosphatidate, yielding diacylglycerol and inorganic phosphate [1].
Roles of phosphatidate phosphatase enzymes in lipid metabolism [1].
In eukaryotic cells, PAP activity has a central role in the synthesis of phospholipids and triacylglycerol through its product diacylglycerol, and it also generates and/or degrades lipid-signaling molecules that are related to phosphatidate [1].
Overexpression of Cwh8p in the yeast double mutant strain, lacking LPP1/DPP1, resulted in an impressive increase in Dol-P-P phosphatase activity, a relatively small increase in Dol-P phosphatase activity, but no change in phosphatidate (PA) phosphatase activity in microsomal fractions [2].
Disruption of either LPP1 or DPP1 caused respective decreases of about 25 and 75% in Mg2+-independent hydrolysis of several isoprenoid phosphates by particulate fractions isolated from these cells [3].

Biological context of LPP1

A multicopy plasmid containing the LPP1 gene directed a 12.9-fold overexpression of Mg2+-independent PA phosphatase activity in the S. cerevisiae lpp1Delta dpp1Delta double mutant [4].
The heterologous expression of the S. cerevisiae LPP1 gene in Sf-9 insect cells resulted in a 715-fold overexpression of Mg2+-independent PA phosphatase activity relative to control insect cells [4].
The LPP1-encoded enzyme exhibited saturation kinetics with respect to the surface concentrations of PA (K(m)=0.05 mol%), DGPP (K(m)=0.07 mol%), and LPA (K(m)=0.08 mol%) [5].

Associations of LPP1 with chemical compounds

The Dol-P-P phosphatase encoded by CWH8 is optimally active in the presence of 0.5% octyl glucoside and relatively unstable in Triton X-100, distinguishing this activity from the lipid phosphatases encoded by LPP1 and DPP1 [2].
Two genes in Saccharomyces cerevisiae, LPP1 and DPP1, with homology to a mammalian phosphatidic acid (PA) phosphatase were identified and disrupted [3].
The inhibitory effects of N-ethylmaleimide and phenylglyoxal on the LPP1-encoded enzyme were novel properties when compared with other Mg(2+)-independent lipid phosphate phosphatases from S. cerevisiae and mammalian cells [5].
A detailed kinetic analysis was performed to determine the mechanism of phosphatidate phosphatase inhibition by sphingoid bases [6].
Sphingosine, phytosphingosine, and sphinganine were parabolic competitive inhibitors of phosphatidate phosphatase activity [6].

Other interactions of LPP1

The LPP1 gene product also exhibited lyso-PA phosphatase and DGPP phosphatase activities [4].

References

Roles of phosphatidate phosphatase enzymes in lipid metabolism. Carman, G.M., Han, G.S. Trends Biochem. Sci. (2006) [Pubmed]
The CWH8 gene encodes a dolichyl pyrophosphate phosphatase with a luminally oriented active site in the endoplasmic reticulum of Saccharomyces cerevisiae. Fernandez, F., Rush, J.S., Toke, D.A., Han, G.S., Quinn, J.E., Carman, G.M., Choi, J.Y., Voelker, D.R., Aebi, M., Waechter, C.J. J. Biol. Chem. (2001) [Pubmed]
The LPP1 and DPP1 gene products account for most of the isoprenoid phosphate phosphatase activities in Saccharomyces cerevisiae. Faulkner, A., Chen, X., Rush, J., Horazdovsky, B., Waechter, C.J., Carman, G.M., Sternweis, P.C. J. Biol. Chem. (1999) [Pubmed]
Isolation and characterization of the Saccharomyces cerevisiae LPP1 gene encoding a Mg2+-independent phosphatidate phosphatase. Toke, D.A., Bennett, W.L., Oshiro, J., Wu, W.I., Voelker, D.R., Carman, G.M. J. Biol. Chem. (1998) [Pubmed]
Enzymological properties of the LPP1-encoded lipid phosphatase from Saccharomyces cerevisiae. Furneisen, J.M., Carman, G.M. Biochim. Biophys. Acta (2000) [Pubmed]
Regulation of phosphatidate phosphatase activity from the yeast Saccharomyces cerevisiae by sphingoid bases. Wu, W.I., Lin, Y.P., Wang, E., Merrill, A.H., Carman, G.M. J. Biol. Chem. (1993) [Pubmed]

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