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Information on EC 3.1.4.50 - glycosylphosphatidylinositol phospholipase D and Organism(s) Bos taurus and UniProt Accession P80109
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3.1.4.50 glycosylphosphatidylinositol phospholipase DIUBMB Comments
This enzyme is also active when O-4 of the glucosamine is substituted by carrying the oligosaccharide that can link a protein to the structure. It therefore cleaves proteins from the lipid part of the glycosylphosphatidylinositol (GPI) anchors, but does so by hydrolysis, whereas glycosylphosphatidylinositol diacylglycerol-lyase (EC 4.6.1.14) does so by elimination. It acts on plasma membranes only after solubilization of the substrate with detergents or solvents, but it may act on intracellular membranes.
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Word Map
- 3.1.4.50
-
gpi-anchored
- medicine
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gpi-phospholipase
- gpi-plc
-
glycosyl-phosphatidylinositol
-
3hmyristate-labeled
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3hethanolamine
- diagnostics
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
gpi-pld, glycosylphosphatidylinositol-specific phospholipase d, gpld1, gpi-specific phospholipase d, glycosylphosphatidylinositol phospholipase d, pi-g pld, phosphatidylinositol-specific phospholipase d, glycosylphosphatidylinositol-phospholipase d, glycoprotein phospholipase d, phosphatidylinositol phospholipase d, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glycoprotein phospholipase D
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-
-
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GPI-PLD
-
-
-
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phosphatidylinositol phospholipase D
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-
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phosphatidylinositol-specific phospholipase D
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-
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phospholipase D, phosphatidylinositol
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-
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PI-G PLD
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric diester
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-
-
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
glycoprotein-phosphatidylinositol phosphatidohydrolase
This enzyme is also active when O-4 of the glucosamine is substituted by carrying the oligosaccharide that can link a protein to the structure. It therefore cleaves proteins from the lipid part of the glycosylphosphatidylinositol (GPI) anchors, but does so by hydrolysis, whereas glycosylphosphatidylinositol diacylglycerol-lyase (EC 4.6.1.14) does so by elimination. It acts on plasma membranes only after solubilization of the substrate with detergents or solvents, but it may act on intracellular membranes.
CAS REGISTRY NUMBER
COMMENTARY
113756-14-2
-
127737-50-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
membrane form of variant-surface-glycoprotein + H2O
phosphatidic acid + variant-surface-glycoprotein inositol
Zn2+-glycerophosphocholine cholinephosphodiesterase, amphiphilic form + H2O
Zn2+-glycerophosphocholine cholinephosphodiesterase, hydrophilic form
membrane form of variant-surface-glycoprotein + H2O
phosphatidic acid + variant-surface-glycoprotein inositol
-
-
-
?
membrane form of variant-surface-glycoprotein + H2O
phosphatidic acid + variant-surface-glycoprotein inositol
-
phospholipase D-type hydrolysis
-
?
Zn2+-glycerophosphocholine cholinephosphodiesterase, amphiphilic form + H2O
Zn2+-glycerophosphocholine cholinephosphodiesterase, hydrophilic form
-
-
-
?
Zn2+-glycerophosphocholine cholinephosphodiesterase, amphiphilic form + H2O
Zn2+-glycerophosphocholine cholinephosphodiesterase, hydrophilic form
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-
-
?
additional information
?
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glycosylphosphatidyl-inositol-anchor cleavage of cell adhesion molecule (csA)
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-
?
additional information
?
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no substrate: phosphatidylethanolamine, phosphatidylcholine, phosphatidylinositol derived from HNO2-cleaved mfVSG, overview on substrate specificity
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-
?
additional information
?
-
-
overexpression of enzyme is lethal to wild-type cells, possibly by catalysing the overproduction of enzyme-derived toxic substances
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-
?
additional information
?
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the cleavage of chiro-inositol-containing glycerophosphatidylinositols results in both L-chiro- and D-chiro-inositol-containing inositol-phosphoglycans
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-
?
additional information
?
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cleavage of glycosylphosphatidylinositol-anchor of membrane proteins
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
membrane form of variant-surface-glycoprotein + H2O
phosphatidic acid + variant-surface-glycoprotein inositol
-
-
-
?
additional information
?
-
-
overexpression of enzyme is lethal to wild-type cells, possibly by catalysing the overproduction of enzyme-derived toxic substances
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
monoacylglycerol
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stimulates in a size-dependent manner, maximal enhancement with monodecanoylglycerol
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PHLD_BOVIN
839
0
92602
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
signal-peptide deficient form of enzyme is catalytically active and intracellularly localized, GPI-anchored form of enzyme is catalytically active and cells release endogenous GPI-anchored alkaline phosphatase
additional information
C-terminal deletion of 2-5 amino acids results in loss of about 70% of enzymic activity, deletion of more than 5 amino acids results in complete loss of activity, Y811 may be crucial for activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable over a range of 0.01-0.1% detergent, ionic detergents such as SDS are inhibitory, and bicarbonate buffer is inhibitory
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Low, M.G.; Prasad, A.R.S.
A phospholipase D specific for the phosphatidylinositol anchor of cell-surface proteins is abundant in plasma
Proc. Natl. Acad. Sci. USA
85
980-984
1988
Bos taurus, Canis lupus familiaris, Equus caballus, Gallus gallus, Homo sapiens, Oryctolagus cuniculus, Rattus norvegicus
Deeg, M.A.; Davitz, M.A.
Glycosylphosphatidylinositol-phospholipase D: a tool for glycosylphosphatidylinositol structural analysis
Methods Enzymol.
250
630-640
1995
Bos taurus, Homo sapiens
Du, X.; Cai, J.; Zhou, J.Z.; Stevens, V.L.; Low, M.G.
Tolerance of glycosylphosphatidylinositol (GPI)-specific phospholipase D overexpression by Chinese hamster ovary cell mutants with aberrant GPI biosynthesis
Biochem. J.
361
113-118
2002
Bos taurus
Hari, T.; Buetikofer, P.; N.Wiesmann, U.; Brodbeck, U.
Uptake and intracellular stability of glycosylphosphatidylinositol-specific phospholipase D in neuroblastoma cells
Biochim. Biophys. Acta
1355
293-302
1997
Bos taurus
Kueng, M.; Buetikofer, P.; Brodbeck, U.; Stadelmann, B.
Expression of intracellular and GPI-anchored forms of GPI-specific phospholipase D in COS-1 cells
Biochim. Biophys. Acta
1357
329-338
1997
Bos taurus (P80109)
Lee, J.Y.; Kim, M.R.; Sok, D.E.
Enzymatic release of Zn2+-glycerophosphocholine cholinephosphodiesterase from brain membranes by glycosylphosphatidylinositol-specific phospholipases and its regulation
Neurochem. Res.
23
899-905
1998
Bos taurus
Lee, J.Y.; Lee, H.J.; Kim, M.R.; Myung, P.K.; Sok, D.E.
Regulation of brain glycosylphosphatidylinositol-specific phospholipase D by natural amphiphiles
Neurochem. Res.
24
1577-1583
1999
Bos taurus
Li, J.Y.; Hollfelder, K.; Huang, K.S.; Low, M.G.
Structural features of GPI-specific phospholipase D revealed by proteolytic fragmentation and Ca2+ binding studies
J. Biol. Chem.
269
28963-28971
1994
Bos taurus
Stadelmann, B.; Butikofer, P.; Konig, A.; Brodbeck, U.
The C-terminus of glycosylphosphatidylinositol-specific phospholipase D is essential for biological activity
Biochim. Biophys. Acta
1355
107-113
1997
Bos taurus (P80109)
Bonilla, J.B.; Cid, M.B.; Contreras, F.X.; Goni, F.M.; Martin-Lomas, M.
Phospholipase cleavage of D- and L-chiro-glycosylphosphoinositides asymmetrically incorporated into liposomal membranes
Chem. Eur. J.
12
1513-1528
2006
Bos taurus
Yoshida, M.; Sakuragi, N.; Kondo, K.; Tanesaka, E.
Cleavage with phospholipase of the lipid anchor in the cell adhesion molecule, csA, from Dictyostelium discoideum
Comp. Biochem. Physiol. B
143B
138-144
2006
Bos taurus (P80109)
-
Elortza, F.; Mohammed, S.; Bunkenborg, J.; Foster, L.J.; Nuehse, T.S.; Brodbeck, U.; Peck, S.C.; Jensen, O.N.
Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment
J. Proteome Res.
5
935-943
2006
Bos taurus
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