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Information on EC 4.6.1.14 - glycosylphosphatidylinositol diacylglycerol-lyase
for references in articles please use BRENDA:EC4.6.1.14
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EC Tree 4 Lyases
4.6 Phosphorus-oxygen lyases
4.6.1 Phosphorus-oxygen lyases (only sub-subclass identified to date)
4.6.1.14 glycosylphosphatidylinositol diacylglycerol-lyase
IUBMB 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 glycosylphostphatidylinositol (GPI) anchors. In some cases, the long-chain acyl group at the sn-1 position of glycerol is replaced by an alkyl or alk-1-enyl group. In other cases, the diacylglycerol is replaced by ceramide (see Lip-1.4 and Lip-1.5 for definition). The only characterized enzyme with this specificity is from Trypanosoma brucei, where the acyl groups are myristoyl, but the function of the trypanosome enzyme is unknown. Substitution on O-2 of the inositol blocks action of this enzyme. It is not identical with EC 3.1.4.50, glycosylphosphatidylinositol phospholipase D.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 4.6.1.14
- trypanosoma
- brucei
- glycosylphosphatidylinositols
-
gpi-anchored
-
procyclic
-
glycosylphosphatidylinositol-anchored
-
tsetse
-
gpi-deficient
- medicine
-
anti-crd
-
stumpy
-
gpi-specific
Reaction Schemes
showSynonyms
glycosylphosphatidylinositol-specific phospholipase c, gpi-plcp, vsg lipase, gpi-phospholipase c, glycosylphosphatidylinositol-phospholipase c, glycan-phosphatidylinositol-specific phospholipase c, gpi-phospholipase c polypeptide, vsg-lipase, gpi-plc enzyme, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(glycosyl)phosphatidylinositol-specific phospholipase C
-
-
-
-
EC 3.1.4.47
-
-
formerly
-
glycan-phosphatidylinositol-specific phospholipase C
glycosyl inositol phospholipid anchor-hydrolyzing enzyme
-
-
-
-
glycosylphosphatidylinositol phospholipase C
glycosylphosphatidylinositol-phospholipase C
-
-
-
-
glycosylphosphatidylinositol-specific phospholipase C
GPI-PC
GPI-PLC
GPI-specific phospholipase C
-
-
-
-
phospholipase C, glycosylphosphatidylinositol
-
-
-
-
variant-surface-glycoprotein phospholipase C
-
-
-
-
variant-surface-glycoprotein-1,2-didecanoyl-sn-phosphatidylinositol inositolphosphohydrolase
-
-
-
-
VSG-lipase
-
-
-
-
glycosylphosphatidylinositol-specific phospholipase C
-
-
-
-
glycosylphosphatidylinositol-specific phospholipase C
-
-
glycosylphosphatidylinositol-specific phospholipase C
-
regulates transferrin endocytosis in the African trypanosome, surmise that GPI-PLC regulates transferrin endocytosis in Trypanosoma brucei
GPI-PLC
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol = 6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P-O bond cleavage
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol 1,2-diacyl-sn-glycerol-lyase [6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate-forming]
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 glycosylphostphatidylinositol (GPI) anchors. In some cases, the long-chain acyl group at the sn-1 position of glycerol is replaced by an alkyl or alk-1-enyl group. In other cases, the diacylglycerol is replaced by ceramide (see Lip-1.4 and Lip-1.5 for definition). The only characterized enzyme with this specificity is from Trypanosoma brucei, where the acyl groups are myristoyl, but the function of the trypanosome enzyme is unknown. Substitution on O-2 of the inositol blocks action of this enzyme. It is not identical with EC 3.1.4.50, glycosylphosphatidylinositol phospholipase D.
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CAS REGISTRY NUMBER
COMMENTARY
129070-68-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-dimyristoyl-sn-phosphatidylinositol + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
lipid A
?
-
Substrates: biological precursor of variant-surface-glycoprotein glycolipid
Products: -
Products: -
?
membrane form variant surface glycoprotein + H2O
soluble variant surface glycoprotein + sn-1,2-dimyristoylglycerol
-
Substrates: mfVSG, enzyme catalyzes the conversion of membrane form variant surface glycoproteins to soluble variant surface glycoproteins, with the release of sn-1,2-dimyristylglycerol
Products: -
Products: -
?
myristate-labeled variant-surface-glycoprotein
?
-
Substrates: -
Products: -
Products: -
?
pronase fragment + H2O
?
-
Substrates: aspartylethanolamine-glycolipid moiety of mfVSG
Products: -
Products: -
?
pronase fragment of mfVSG + H2O
?
-
Substrates: contains only the terminal amino acid and the glycolipid anchor
Products: -
Products: -
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
-
Substrates: -
Products: -
Products: -
?
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
-
Substrates: -
Products: -
Products: -
?
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
-
Substrates: the assay contains acetylcholinesterase
Products: -
Products: -
?
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
-
Substrates: -
Products: -
Products: -
?
acetylcholinesterase
soluble acetylcholinesterase + 1,2-diacylglycerol
-
Substrates: isolated from bovine erythrocytes, does not act on membrane-bound forms but hydrolyzes the membrane-anchor from solubilized substrate
Products: -
Products: -
?
acetylcholinesterase
soluble acetylcholinesterase + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
glycolipid A
?
-
Substrates: is cleaved when Trypanosoma brucei encounters a mildly alkaline or hypotonic extracellular environment
Products: -
Products: -
?
glycolipid A
?
-
Substrates: is cleaved when Trypanosoma brucei encounters a mildly alkaline or hypotonic extracellular environment
Products: -
Products: -
?
phosphatidylinositol
inositol 1,2-cyclic phosphate + inositol phosphate
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol
inositol 1,2-cyclic phosphate + inositol phosphate
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol
inositol 1,2-cyclic phosphate + inositol phosphate
-
Substrates: very poor substrate
Products: -
Products: -
?
phosphatidylinositol
inositol 1,2-cyclic phosphate + inositol phosphate
-
Substrates: at 0.005 mM phosphatidylinositol, hydrolysis is maximal at 0.005% Triton X-100, at 1 mM phosphatidylinositol hydrolysis is maximal at 0.05% Triton X-100
Products: -
Products: -
?
variant surface glycoprotein
?
-
Substrates: on exposure to mild alkali
Products: -
Products: -
?
variant surface glycoprotein
?
-
Substrates: on exposure to mild alkali
Products: -
Products: -
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
Substrates: -
Products: -
Products: -
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
Substrates: peanut enzyme does not act on membrane-bound forms but hydrolyzes the membrane-anchor from solubilized substrate
Products: -
Products: -
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
Substrates: isolated from Trypanosoma brucei
Products: -
Products: -
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
Substrates: highly specific
Products: -
Products: -
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
Substrates: isolated from Trypanosoma equiperdum BoTat-1
Products: -
Products: -
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
Substrates: -
Products: -
Products: -
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
Substrates: -
Products: -
Products: -
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
Substrates: -
Products: -
Products: -
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
Substrates: -
Products: i.e. 1,2-dimyristoylglycerol
Products: i.e. 1,2-dimyristoylglycerol
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
Substrates: highly specific
Products: i.e. 1,2-dimyristoylglycerol
Products: i.e. 1,2-dimyristoylglycerol
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
Substrates: substrate is tethered to cell membrane by glycolipid moiety containing 1,2-dimyristoyl-sn-phosphatidylinositol
Products: i.e. 1,2-dimyristoylglycerol
Products: i.e. 1,2-dimyristoylglycerol
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
Substrates: enzyme activity is stimulated by acid-treatment of the cells
Products: -
Products: -
?
variant-surface-glycoprotein
1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
Substrates: phospholipase C-type hydrolysis
Products: i.e. 1,2-dimyristoylglycerol
Products: i.e. 1,2-dimyristoylglycerol
?
additional information
?
-
-
Substrates: no substrates are phosphatidylcholine, phosphatidylserine, phosphatidylinositol 4-monophosphate, phosphatidylinositol 4,5-bisphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: glucosaminyl(alpha1-, 6)inositol is the crucial glycan moiety for substrate recognition
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate is 1-stearoyl-2-arachidonoyl-sn-phosphatidylinositol
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not digest glycolipid Z and glycolipid C
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme exhibits substantial specificity for molecules containing glycosylated phosphatidylinositol
Products: -
Products: -
?
additional information
?
-
-
Substrates: GPI-PLC is a signalling enzyme, and DAG is a second messenger for GPI-PLC. Its enzyme activity is important for stimulating uptake of transferrin
Products: -
Products: -
?
additional information
?
-
-
Substrates: [32P]phosphatidylinositol-4-phosphate, [32P]phosphatidylinositol 4,5-bisphosphate or [3H]phosphatidylcholine are not significantly hydrolyzed by the GPI-PLC
Products: -
Products: -
?
additional information
?
-
-
Substrates: hippocampal detergent-resistant membranes: alpha2beta subunits of voltage-gated calcium channels, alpha2delta-1, alpha2delt-2, and alpha2delt-3, show all properties expected of GPI-anchored proteins, which are substrates for GPI-PLC
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme exhibits substantial specificity for molecules containing glycosylated phosphatidylinositol
Products: -
Products: -
?
additional information
?
-
-
Substrates: [32P]phosphatidylinositol-4-phosphate, [32P]phosphatidylinositol 4,5-bisphosphate or [3H]phosphatidylcholine are not significantly hydrolyzed by the GPI-PLC
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not digest glycolipid Z and glycolipid C
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
-
Substrates: -
Products: -
Products: -
?
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
-
Substrates: -
Products: -
Products: -
?
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme exhibits substantial specificity for molecules containing glycosylated phosphatidylinositol
Products: -
Products: -
?
additional information
?
-
-
Substrates: GPI-PLC is a signalling enzyme, and DAG is a second messenger for GPI-PLC. Its enzyme activity is important for stimulating uptake of transferrin
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme exhibits substantial specificity for molecules containing glycosylated phosphatidylinositol
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Glucosaminyl-alpha-1,6-2-deoxy-D-myo-inositol
-
i.e. compound VP-615L, more effective than VP-606L
Glucosaminyl-alpha-1,6-D-myo-inositol
-
i.e. compound VP-606L or 6-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol
Glucosaminyl-alpha-1,6-D-myo-inositol 1,2-cyclic phosphate
-
i.e. compound VP-601L, product inhibition
Glucosaminyl-alpha-1,6-D-myo-inositol 1-dodecylphosphonate
-
i.e. compound VP-604L
Glucosaminyl-alpha-1,6-D-myo-inositol 1-hexylphosphonate
-
i.e. compound VFT-2
Mannosyl-alpha-1,4-glucosaminyl-alpha-1,6-D-myo-inositol
-
i.e. O-alpha-D-mannopyranosyl-1,4-O-2-amino-2-deoxy-alpha-D-glucopyranosyl-1,6-D-myo-inositol
N-(N,N-Dimethylcarbamyl)-glucosaminyl-alpha-1,6-D-myo-inositol
-
i.e. compound VC-109B, less effective than VP-606L
N-Acetylglucosaminyl-alpha-1,6-D-myo-inositol
-
i.e. compound VC-105B, weak
Ca2+
-
activity of GPI-PLC exhibited small but significant inhibition in the presence of calcium ions, 70% activity left
additional information
-
low inhibition by 2-deoxy-2-fluoro-scyllo-inositol-1-O-dodecyl-phosphonic acid (GPI-1793) and very low inhibition by myo-inositol-1-O-dodecylphosphonic acid methylester (GPI-2349)
-
additional information
-
no inhibition by palmitate, myristate, phosphatidylethanolamine, inositol 1-phosphate, N-acetylglucosamine, ethanolamine, inositol, glucosamine, mannose, glucosaminyl-alpha-1,6-2-deoxy-D-myo-inositol 1-phosphate (i.e. VP-612L), glucosaminyl-alpha-1,6-2-deoxy-L-myo-inositol (i.e. VP-614L)
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
deoxycholate
-
activation, 0.5-1 mg/ml, neutral enzyme form, not acidic enzyme form, inhibits above 1 mg/ml
dithiothreitol
-
enzyme activity shows marked stimulation in the presence of the thiol-reducing agent, DTT
Triton X-100
-
activation, above critical micelle concentration, inhibition from 0.05% to 0.5%
additional information
-
2 enzyme forms differing in pH-optima and response to stimulation by butanol and deoxycholate
-
additional information
-
reactive oxygen species (ROS) mediates GPI-PLC activation
-
additional information
-
no activation by aminoglycoside antibiotic geneticin (G418)
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Role of urokinase plasminogen activator receptor in thrombospondin 1-mediated tumor cell invasion.
Malaria
Plasmodium falciparum and Plasmodium chabaudi: characterization of glycosylphosphatidylinositol-degrading activities.
Neoplasms
Role of urokinase plasminogen activator receptor in thrombospondin 1-mediated tumor cell invasion.
Parasitemia
The GPI-phospholipase C of Trypanosoma brucei is nonessential but influences parasitemia in mice.
Trypanosomiasis, African
Regulated cleavage of intracellular glycosylphosphatidylinositol in a trypanosome. Peroxisome-to-endoplasmic reticulum translocation of a phospholipase C.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0003
myristate-labeled variant-surface-glycoprotein
-
37Ā°C, pH 8, 50 mM sodium phosphate, Q81N
-
0.0005
myristate-labeled variant-surface-glycoprotein
-
37Ā°C, pH 8, 50 mM sodium phosphate, wild-type
-
0.0011
myristate-labeled variant-surface-glycoprotein
-
37Ā°C, pH 8, wild-type
-
0.0018
myristate-labeled variant-surface-glycoprotein
-
37Ā°C, pH 8, C80A
-
0.0021
myristate-labeled variant-surface-glycoprotein
-
37Ā°C, pH 8, C80T
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
in high cholesterol-containing detergent-soluble glycolipid-enriched membrane microdomains: 488% of the activity measured in plasma membranes, in low cholesterol-containing detergent-soluble glycolipid-enriched membrane microdomains: 141% of the activity measured in plasma membranes, in non-detergent-soluble glycolipid-enriched membrane microdomains: 29% of the activity measured in plasma membranes
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
-
two maxima, one at pH 7.0 and the other at pH 10.0, that shows the highest enzyme activity
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.5
-
about half-maximal activity at pH 6.5 and 9.5, little or no activity below pH 6
7 - 10
-
pH dependence of GPI-PLC activity. Two maxima, one at pH 7.0 and the other at pH 10.0, that shows the highest enzyme activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
bloodstream-form Trypanosoma brucei RUMP528 (GPI-PLC-/-)
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
in case of mutations on the endosome targeting motif, glycosomal GPI-PLC from Trypanosoma brucei fails to produce the glycosylphosphatidylinositol deficiency in Leishmania major
brenda
additional information
-
Cys347 is part of a peptide motif required for post-translational targeting of GPI-PLC to the endoplasmic reticulum
brenda
-
Cys347 is part of a peptide motif required for post-translational targeting of GPI-PLC to the endoplasmic reticulum
-
brenda
-
enzyme is translocated from glycosomes to the endoplasmic reticulum when cells are treated with mild alkaline or hypo-osmotic conditions
brenda
-
enzyme is translocated from glycosomes to the endoplasmic reticulum when cells are treated with mild alkaline or hypo-osmotic conditions
-
brenda