Enzyme

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     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.4 Phosphoric-diester hydrolases
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.

3D structure

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References

External Links

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
MSA:

3.1.4.50;

Phylogenetic Tree:

3.1.4.50;

Uniprot:
M-CSA:
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

References

TitleAuthorsDatePubMed ID
Structural features of GPI-specific phospholipase D revealed by proteolytic fragmentation and Ca2+ binding studies.Li JY, Hollfelder K, Huang KS, Low MG1994 Nov 187961859
A phospholipase D specific for the phosphatidylinositol anchor of cell-surface proteins is abundant in plasma.Low MG, Prasad AR1988 Feb3422494
GPI-specific phospholipase D associates with an apoA-I- and apoA-IV-containing complex.Deeg MA, Bierman EL, Cheung MC2001 Mar11254757