| ID: | 3.1.4.50 |
|---|---|
| Description: | Glycosylphosphatidylinositol phospholipase D. |
| Alternative Name: |
Phosphatidylinositol-specific phospholipase D. Phosphatidylinositol-glycan-specific phospholipase D. Phosphatidylinositol phospholipase D. GPI-PLD. Glycoprotein phospholipase D. |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 3.1.4.50 |
| BRENDA Enzyme Link: | BRENDA 3.1.4.50 |
| KEGG Enzyme Link: | KEGG3.1.4.50 |
| BioCyc Enzyme Link: | BioCyc 3.1.4.50 |
| ExPASy Enzyme Link: | ExPASy3.1.4.50 |
| EC2PDB Enzyme Link: | EC2PDB 3.1.4.50 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.1.4.50 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.1.4.50 |
| IntEnz Enzyme Link: | IntEnz 3.1.4.50 |
| MEDLINE Enzyme Link: | MEDLINE 3.1.4.50 |
| RHEA:10832 | a 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + a 1,2-diacyl-sn-glycero-3-phosphate + H(+) |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[OH;+0:3])-[CH;+0:4](-[*:5])-[O;H0;+0:6]-[*:7]-[O;H0;+0:8]-[CH;+0:9](-[*:10])-[*:11].[*:12]-[OH;+0:13].[H+;H0:14]>>[*:1]-[CH;+0:2](-[O;H0;+0:8]-[*:7]-[O;H0;+0:6]-[CH;+0:9](-[*:10])-[*:11])-[CH;+0:4](-[*:5])-[O;H0;+0:13]-[*:12].[OH2;+0:3] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structural features of GPI-specific phospholipase D revealed by proteolytic fragmentation and Ca2+ binding studies. | Li JY, Hollfelder K, Huang KS, Low MG | 1994 Nov 18 | 7961859 |
| A phospholipase D specific for the phosphatidylinositol anchor of cell-surface proteins is abundant in plasma. | Low MG, Prasad AR | 1988 Feb | 3422494 |
| GPI-specific phospholipase D associates with an apoA-I- and apoA-IV-containing complex. | Deeg MA, Bierman EL, Cheung MC | 2001 Mar | 11254757 |