Biology:Glycosylphosphatidylinositol diacylglycerol-lyase
| glycosylphosphatidylinositol diacylglycerol-lyase | |||||||||
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| Identifiers | |||||||||
| EC number | 4.6.1.14 | ||||||||
| CAS number | 129070-68-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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The enzyme glycosylphosphatidylinositol diacylglycerol-lyase (EC 4.6.1.14) catalyzes the reaction
- 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol = 6-(α-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
This enzyme belongs to the family of lyases, specifically the class of phosphorus-oxygen lyases. The systematic name of this enzyme class is 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol 1,2-diacyl-sn-glycerol-lyase [6-(α-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate-forming]. Other names in common use include (glycosyl)phosphatidylinositol-specific phospholipase C, GPI-PLC, GPI-specific phospholipase C, VSG-lipase, glycosyl inositol phospholipid anchor-hydrolyzing enzyme, glycosylphosphatidylinositol-phospholipase C, glycosylphosphatidylinositol-specific phospholipase C, variant-surface-glycoprotein phospholipase C, 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol, and diacylglycerol-lyase (1,2-cyclic-phosphate-forming).
References
- "A phospholipase C from Trypanosoma brucei which selectively cleaves the glycolipid on the variant surface glycoprotein". J. Biol. Chem. 261 (29): 13813–9. 1986. doi:10.1016/S0021-9258(18)67092-9. PMID 3759991.
- "Mutagenesis study of the glycosylphosphatidylinositol phospholipase C of Trypanosoma brucei". Mol. Biochem. Parasitol. 90 (2): 423–32. 1997. doi:10.1016/S0166-6851(97)00177-1. PMID 9476790.
- "Tetramerization of glycosylphosphatidylinositol-specific phospholipase C from Trypanosoma brucei". J. Biol. Chem. 275 (25): 19334–42. 2000. doi:10.1074/jbc.M001798200. PMID 10764777.
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