The cellular functions of the yeast lipin homolog PAH1p are dependent on its phosphatidate phosphatase activity.

@article{Han2007TheCF,
  title={The cellular functions of the yeast lipin homolog PAH1p are dependent on its phosphatidate phosphatase activity.},
  author={Gil-Soo Han and Symeon Siniossoglou and George M Carman},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 51},
  pages={37026-35}
}
The Saccharomyces cerevisiae PAH1-encoded Mg2+-dependent phosphatidate phosphatase (PAP1, 3-sn-phosphatidate phosphohydrolase, EC 3.1.3.4) catalyzes the dephosphorylation of phosphatidate to yield diacylglycerol and Pi. This enzyme plays a major role in the synthesis of triacylglycerols and phospholipids in S. cerevisiae. PAP1 contains the DXDX(T/V) catalytic motif (DIDGT at residues 398-402) that is shared by the mammalian fat-regulating protein lipin 1 and the superfamily of haloacid… CONTINUE READING