phosphatidylinositol diacylglycerol-lyase
monophosphatidylinositol phosphodiesterase
1-phosphatidylinositol phosphodiesterase
1-phosphatidyl-D-myo-inositol inositolphosphohydrolase(cyclic-phosphate-forming)
1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase(1,2-cyclic-phosphate-forming)
Phospholipids chiral at phosphorus. Stereochemical mechanism of reactions catalyzed by phosphatidylinositide-specific phospholipase C from Bacillus cereus and guinea pig uterus.
Divalent cation regulation of phosphoinositide metabolism. Naturally occurring B lymphoblasts contain a Mg2(+)-regulated phosphatidylinositol-specific phospholipase C.
A chromogenic substrate for phosphatidylinositol-specific phospholipase C: 4-nitrophenyl myo-inositol-1-phosphate.
Phospholipase stereospecificity at phosphorus.
Phospholipids chiral at phosphorus. Stereochemical mechanism for the formation of inositol 1-phosphate catalyzed by phosphatidylinositol-specific phospholipase C.
Substrate requirements of bacterial phosphatidylinositol-specific phospholipase C.
Crystallization of phosphatidylinositol-specific phospholipase C from Bacillus cereus.
Phosphatidylinositol-specific phospholipase C from Bacillus cereus at the lipid-water interface: interfacial binding, catalysis, and activation.
src-homology 2 (SH2) domain ligation as an allosteric regulator: modulation of phosphoinositide-specific phospholipase C gamma 1 structure and activity.
Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol.
Mechanism and structure based inhibitors of phospholipase C enzymes.
Crystal structure of phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with glucosaminyl(alpha 1-->6)-D-myo-inositol, an essential fragment of GPI anchors.
Synthesis, structure-activity relationships, and the effect of polyethylene glycol on inhibitors of phosphatidylinositol-specific phospholipase C from Bacillus cereus.
Inhibition of phosphatidylinositol-specific phospholipase C: studies on synthetic substrates, inhibitors and a synthetic enzyme.
Phospholipid signalling. Taking stock of PI-PLC.
Structural views of phosphoinositide-specific phospholipase C: signalling the way ahead.
Probing the roles of active site residues in phosphatidylinositol-specific phospholipase C from Bacillus cereus by site-directed mutagenesis.
Phosphatidylinositol-specific phospholipase C: kinetic and stereochemical evidence for an interaction between arginine-69 and the phosphate group of phosphatidylinositol.
Short-chain phosphatidylinositol conformation and its relevance to phosphatidylinositol-specific phospholipase C.
Allosteric activation of phosphatidylinositol-specific phospholipase C: specific phospholipid binding anchors the enzyme to the interface.
Activation of phosphatidylinositol-specific phospholipase C toward inositol 1,2-(cyclic)-phosphate.
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 43-317.
Crystal structure of the phosphatidylinositol-specific phospholipase C from the human pathogen Listeria monocytogenes.
Determination of pKa values of the histidine side chains of phosphatidylinositol-specific phospholipase C from Bacillus cereus by NMR spectroscopy and site-directed mutagenesis.
Mechanism of phosphatidylinositol-specific phospholipase C: a unified view of the mechanism of catalysis.
Structural and mechanistic comparison of prokaryotic and eukaryotic phosphoinositide-specific phospholipases C.
Bacterial phosphatidylinositol-specific phospholipase C: structure, function, and interaction with lipids.
Mutagenesis of active-site histidines of Listeria monocytogenes phosphatidylinositol-specific phospholipase C: effects on enzyme activity and biological function.
Involvement of the Arg-Asp-His catalytic triad in enzymatic cleavage of the phosphodiester bond.
A catalytic diad involved in substrate-assisted catalysis: NMR study of hydrogen bonding and dynamics at the active site of phosphatidylinositol-specific phospholipase C.
N-terminal EF-hand-like domain is required for phosphoinositide-specific phospholipase C activity in Arabidopsis thaliana.
Role of tryptophan residues in interfacial binding of phosphatidylinositol-specific phospholipase C.
Engineering a catalytic metal binding site into a calcium-independent phosphatidylinositol-specific phospholipase C leads to enhanced stereoselectivity.
Water-miscible organic cosolvents enhance phosphatidylinositol-specific phospholipase C phosphotransferase as well as phosphodiesterase activity.
Application of Bronsted-type LFER in the study of the phospholipase C mechanism.
X-ray structure of the R69D phosphatidylinositol-specific phospholipase C enzyme: insight into the role of calcium and surrounding amino acids in active site geometry and catalysis.
Dimer structure of an interfacially impaired phosphatidylinositol-specific phospholipase C.
This enzyme was transferred from E.C. 3.1.4.10 to 4.6.1.13. This enzyme catalyzes the following reactions: (A) Intramolecular phosphotransfer reaction: (B) Hydrolysis: However, the activity of hydrolysis reaction is very low, according to the literature [25], [26]. The first reaction of this enzyme proceeds as follows: (1) Asp274 modulates the activity of a general base, His32. (2) His32 acts as a general base to deprotonate and activate 2-OH group of 1-Phosphatidyl-D-myo-inositol. (3) The activated hydroxyl group makes a nucleophilic attack on the phosphate group of the substrate, forming a pentacovalent transition state. (4) The negatively charged transition-state is stabilized by Arg69, which is modulated and oriented by Asp33. (5) Asp33 also modulates the activity of the general acid, His82. (6) His32 acts as a general acid to protonate the leaving group, completing the reaction.