Glycosylphosphatidylinositol (GPI) is used as a membrane anchor by many eukaryotic cell surface proteins. The first step in GPI biosynthesis involves the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to phosphatidylinositol (PI) . The second step is de-N-acetylation of GlcNAc-PI.
PIGL encodes a deduced 252-amino acid protein that shares 77% identity with the rat protein. Using transfection into mammalian PIGL-deficient cells, Watanabe et al. (1999) demonstrated that S. cerevisiae Gpi12 is the ortholog of human and rat PIGL. Disruption of Gpi12 in yeast resulted in a lethal phenotype. Using purified, recombinant rat PIGL, Watanabe et al. (1999) demonstrated that PIGL has GlcNAc-PI de-N-acetylase activity in vitro, which is enhanced by metal ions.
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