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Information on EC 4.6.1.13 - phosphatidylinositol diacylglycerol-lyase and Organism(s) Staphylococcus aureus and UniProt Accession P45723

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IUBMB Comments
This enzyme is bacterial. Activity is also found in animals, but this activity is due to the presence of EC 3.1.4.11, phosphoinositide phospholipase C.
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Staphylococcus aureus
UNIPROT: P45723
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The taxonomic range for the selected organisms is: Staphylococcus aureus
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphatidylinositol-specific plc, pi-phospholipase c, 1-phosphatidylinositol phosphodiesterase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphatidylinositol-specific phospholipase C
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1-phosphatidyl-D-myo-inositol inositolphosphohydrolase (cyclic-phosphate-forming)
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1-phosphatidylinositol phosphodiesterase
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monophosphatidylinositol phosphodiesterase
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Phosphatidylinositol diacylglycerol-lyase
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phosphatidylinositol phosphodiesterase
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phosphatidylinositol phospholipase C
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phosphatidylinositol-specific phospholipase C
additional information
cf. EC 3.1.4.11
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P-O bond cleavage
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
1-phosphatidyl-1D-myo-inositol 1,2-diacyl-sn-glycerol-lyase (1D-myo-inositol-1,2-cyclic-phosphate-forming)
This enzyme is bacterial. Activity is also found in animals, but this activity is due to the presence of EC 3.1.4.11, phosphoinositide phospholipase C.
CAS REGISTRY NUMBER
COMMENTARY hide
37288-19-0
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63551-76-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
show the reaction diagram
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at first the enzyme catalyzes phosphate transfer within the molecule of phosphatidylinositol from glycerol OH to 2-OH of myo-inositol, resulting in diacylglycerol and myo-inositol 1,2-cyclic phosphate. Next myo-inositol 1,2-cyclic phosphate is hydrolyzed by the enzyme to inositol 1-phosphate. Since the reaction rate of the first step (phosphotransferase) is 1000 times as much as that of the second step (cyclic phosphodiesterase) myo-inositol 1,2-cyclic phosphate accumulates as one of the major products during enzyme action
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?
additional information
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formation of inositol 1,2-(cyclic)phosphate from L-alpha-phoshatidylinositol, NMR spectroscopy analysis
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
phospholipid binding kinetics of the recombinant enzyme, ooverview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the enzyme is secreted
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is a virulence factor in the pathogenicity of Staphylococcus aureus
additional information
the enzyme can form a dimer via helix B, a structural feature present in all secreted, bacterial phosphatidylinositol-specific phospholipases C that is important for membrane binding. The small interface is critical for optimal enzyme activity. The enzyme dimerization is enhanced in membranes containing phosphatidylcholine, the zwitterionic phospholipid acts not by specific binding to the protein, but rather by reducing anionic lipid interactions with a cationic pocket on the surface of the enzyme that stabilizes monomeric protein. Staphylococcus aureus phosphatidylinositol-specific phospholipase C appears to have a unique mechanism where enzyme activity is modulated by competition between binding of soluble anions or anionic lipids to the cationic sensor and transient dimerization on the membrane
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
the enzyme can form a dimer via helix B, a structural feature present in all secreted, bacterial phosphatidylinositol-specific phospholipases C that is important for membrane binding. The small interface is critical for optimal enzyme activity. The enzyme dimerization is enhanced in membranes containing phosphatidylcholine, fluorescence correlation spectroscopy binding analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type enzyme and mutant Y253S complexed with 1,2-dibutyroyl-sn-glycero-3-phosphocholine, hanging drop vapour diffusion method, mixing of 0.0015 ml of 10 mg/ml protein, 50 mM myo-inositol and 2.5 mM 1,2-dibutyroyl-sn-glycero-3-phosphocholine, with 0.0015 ml of reservoir solution containing 150 mM ammonium acetate, 100 mM sodium acetate, pH 4.6, with 1 mM Mg(NO3)2 (100 mM for the mutant enzymes), and 16-20% PEG 4000, 20°C, 2 weeks, X-ray diffraction structure determination and analysis at 2.16-2.3 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F249W
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
H86E
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
H86Y
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
V44C
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
V44W
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
Y253K
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
Y253S
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
Y253S/Y255S
site-directed mutagenesis, the mutant has the same secondary structure content but a 5°C lower thermal denaturation temperature than the wild-type and an altered enzyme activity
Y253W
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
Y290A
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21-Codonplus (DE3)-RIL
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Codonplus (DE3)-RIL
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
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enzyme is used as a tool in the studies of GPI-anchored proteins
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ikezawa, H.
Bacterial phosphatidylinositol-specific phospholipase C as membrane-attacking agents and tools for research on GPI-anchored proteins
J. Toxicol. Toxin Rev.
23
479-508
2004
Bacillus cereus, Bacillus thuringiensis, Listeria monocytogenes, Staphylococcus aureus
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Manually annotated by BRENDA team
Cheng, J.; Goldstein, R.; Stec, B.; Gershenson, A.; Roberts, M.F.
Competition between anion binding and dimerization modulates Staphylococcus aureus phosphatidylinositol-specific phospholipase C enzymatic activity
J. Biol. Chem.
287
40317-40327
2012
Staphylococcus aureus (P45723)
Manually annotated by BRENDA team