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4.6.1.13: phosphatidylinositol diacylglycerol-lyase

This is an abbreviated version!
For detailed information about phosphatidylinositol diacylglycerol-lyase, go to the full flat file.

Word Map on EC 4.6.1.13

Reaction

1-phosphatidyl-1D-myo-inositol
=
1D-myo-inositol 1,2-cyclic phosphate
+
1,2-diacyl-sn-glycerol

Synonyms

1-phosphatidyl-D-myo-inositol inositolphosphohydrolase (cyclic-phosphate-forming), 1-phosphatidylinositol phosphodiesterase, EC 3.1.4.10, monophosphatidylinositol phosphodiesterase, More, Phosphatidylinositol diacylglycerol-lyase, phosphatidylinositol phosphodiesterase, phosphatidylinositol phospholipase C, phosphatidylinositol-specific phospholipase C, phosphatidylinositol-specific PLC, phosphatidylinositolphospholipase C, PI-phospholipase C, PI-PLC, PLC, PLC1, PLC2, PLC3, PLC4, PLC5, PLC6

ECTree

     4 Lyases
         4.6 Phosphorus-oxygen lyases
             4.6.1 Phosphorus-oxygen lyases (only sub-subclass identified to date)
                4.6.1.13 phosphatidylinositol diacylglycerol-lyase

Activating Compound

Activating Compound on EC 4.6.1.13 - phosphatidylinositol diacylglycerol-lyase

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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
butyl-fluorescein myo-inositol phosphate
-
two molecules bind to enzyme, one at the active site and one at a subsite, causing an increase in activity, kinetics
deoxycholate
diacylglycerol
diethyl ether
-
strongly activates
diheptanoyl phosphatidylcholine
-
activates
dihexanoyl phosphatidylcholine
-
activates, 4-5fold increase in catalytic efficiency, binds to a lipid-binding subsite, not to the active site, maximal activation at 0.4 mM
dihexanoylphosphatidylcholine
-
non-substrate activator lipid, maximum PI-PLC activity at 0.7-1 mM
dimethylformamide
-
water-miscible, enhances phosphotransferase activity
Dimethylsulfoxide
-
water-miscible, enhances phosphotransferase activity
ethanol
-
all PLC1-6 are activated in salt/ethanol extractions
heme
-
heme receptor mediates the stimulatory effect of heme on the (Na+ + K+)ATPase activity through a PIPLC/PKC signaling pathway
Isopropanol
KCl
-
ionic strength, and not the salt identity, is important for PI-PLC activation towards phosphatidylinositol in micelles. Added salt has a synergistic effect with zwitterionic phospholipids, leading to high specific activities for phosphatidylinositol cleavage with only moderate dilution of the anionic substrate in the interface. This kinetic activation correlates with weakening of strong PI-PLC hydrophobic interactions with the interface. PI-PLC cleavage of phosphatidylinositol presented in small unilamellar vesicles is activated by salt
phosphatidic acid
-
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
phosphatidylcholine
phosphatidylglycerol
-
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
phosphatidylmethanol
-
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
phosphatidylserine
-
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
Salt
-
all PLC1-6 are activated in salt/ethanol extractions
SDS
-
strongly activates
Triton X-100
Tween 20
-
slight stimulation
additional information
-