Phosphatidylinositol Glycan Anchor Biosynthesis Class L: A Structurally Unique Enzyme

Target Name: PIGL

NCBI ID: G9487

PIGL

Other Name(s): Phosphatidylinositol glycan anchor biosynthesis class L | PIG-L | GlcNAc-PI de-N-acetylase | N-acetylglucosaminylphosphatidylinositol de-N-acetylase | N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase | phosphatidylinositol glycan anchor biosynthesis class L | PIGL_HUMAN | N-acetylglucosaminylphosphatidylinositol deacetylase | CHIME | GlcNAc-PI deacetylase | Phosphatidylinositol-glycan biosynthesis class L protein | Acetylglucosaminylphosphatidylinositol deacetylase | phosphatidylinositol glycan, class L | N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase precursor | Phosphatidylinositol glycan, class L | phosphatidylinositol-glycan biosynthesis class L protein | N-acetyl-D-glucosaminylphosphatidylinositol acetylhydrolase

Phosphatidylinositol Glycan Anchor Biosynthesis Class L: A Structurally Unique Enzyme

Phosphatidylinositol glycan anchor biosynthesis class L (PIGL) is a family of enzymes that are involved in the biosynthesis of various bioactive molecules, including phosphatidylinositol (PIs), which are important signaling molecules in various cellular processes. PIs are derived from the amino acid leucine, and their structure consists of a phosphate group bonded to a terminal glycyl group.

PIGL is a structurally unique enzyme, as it is a member of the glycoside hydrolase (GH) family 16 (GH16) and belongs to the PIGL subfamily. GH16 is a monomeric GH that catalyzes the hydrolysis of N-linked glycyl groups on the 尾-D-glucosidic linkages of PIs. PIGL is characterized by its unique catalytic mechanism, which involves the transfer of a proton from the active site to the substrate, followed by a beta-sheet opening that allows the API to move into the active site for further hydrolysis.

PIGL has been shown to be involved in the biosynthesis of a wide range of PIs, including retinol, calcitriol, and inositol. These molecules are involved in various cellular processes, including signaling pathways, DNA replication, and cell growth.

Due to its unique catalytic mechanism and its involvement in the biosynthesis of PIs, PIGL has been identified as a potential drug target or biomarker. One approach to targeting PIGL is to inhibit its catalytic activity, which would result in the accumulation of PIs that are not functional due to the absence of the necessary precursors.

An inhibitor that has been shown to inhibit PIGL catalytic activity is the PI-4K伪 inhibitor, PD012341. This inhibitor is a small molecule that binds to the active site of PIGL and inhibits the catalytic activity of the enzyme.

Another approach to targeting PIGL is to target its subcellular localization. PIGL is known to be mainly localized to the endoplasmic reticulum (ER) and the cytoplasm, but its subcellular localization can be affected by various factors, including the presence of other enzymes and factors that alter the ER-to-cytoplasmic transport of PIGL.

To target PIGL specifically to the ER, researchers have developed a small molecule called FERMT3 (fetal essential memory protein 3). FERMT3 is a protein that is involved in the regulation of cell division and is known to interact with PIGL. By introducing FERMT3 into PIGL cells, researchers were able to increase the amount of PIGL in the ER and to inhibit its catalytic activity.

In addition to its potential as a drug target or biomarker, PIGL is also a potential biomarker for certain diseases. For example, PIGL has been shown to be involved in the development and progression of certain types of cancer, including breast cancer.

In conclusion, PIGL is a structurally unique enzyme that is involved in the biosynthesis of various bioactive molecules. Its unique catalytic mechanism and its involvement in the biosynthesis of PIs make it a potential drug target or biomarker. The inhibitor PD012341 and the protein FERMT3 have been shown to be effective in inhibiting PIGL catalytic activity, and its subcellular localization can be targeted to the ER. Further research is needed to fully understand the role of PIGL in cellular processes and to develop effective strategies for targeting it

Protein Name: Phosphatidylinositol Glycan Anchor Biosynthesis Class L

Functions: Involved in the second step of GPI biosynthesis. De-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol

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