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Information on EC 3.1.4.11 - phosphoinositide phospholipase C and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32383

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.4 Phosphoric-diester hydrolases
                3.1.4.11 phosphoinositide phospholipase C
IUBMB Comments
These enzymes form some of the cyclic phosphate Ins(cyclic1,2)P(4,5)P2 as well as Ins(1,4,5)P3. They show activity towards phosphatidylinositol, i.e., the activity of EC 4.6.1.13, phosphatidylinositol diacylglycerol-lyase, in vitro at high [Ca2+]. Four beta-isoforms regulated by G-proteins, two gamma-forms regulated by tyrosine kinases, four delta-forms regulated at least in part by calcium and an epsilon-form, probably regulated by the oncogene ras, have been found.
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Saccharomyces cerevisiae
UNIPROT: P32383
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
pi-plc, phosphatidylinositol-specific phospholipase c, plc-gamma, plc-gamma1, plcgamma1, plc-beta, plcgamma, phosphoinositide-specific phospholipase c, plcgamma2, phospholipase c-gamma1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoinositide-specific phospholipase C
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1-phosphatidyl-D-myo-inositol 4,5-bisphosphate inositoltrisphosphohydrolase
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-
-
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1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase
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-
-
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No receptor potential A protein
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-
-
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phosphatidylinositol 4,5-bisphosphate phosphodiesterase
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-
-
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phosphatidylinositol-4,5-bisphosphate phosphodiesterase
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-
-
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phosphatidylinositol-4,5-bisphosphate phospholipase C
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-
-
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phosphodiesterase, triphosphoinositide
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-
-
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phosphoinositidase C
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-
-
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phospholipase C
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-
-
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phosphotidylinositol 4,5-bisphosphate-specific phospholipase C
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-
-
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PIC
-
-
-
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PIP2 PDE
-
-
-
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PIP2 phosphodiesterase
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-
-
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PIPLC
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-
-
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PLC
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-
-
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PLC-148
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-
-
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PLC-154
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-
-
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PLC-85
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-
-
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polyphosphoinositide phospholipase C
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-
-
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PtdIns(4,5)P2-directed phospholipase C
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-
-
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triphosphoinositide phosphodiesterase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase
These enzymes form some of the cyclic phosphate Ins(cyclic1,2)P(4,5)P2 as well as Ins(1,4,5)P3. They show activity towards phosphatidylinositol, i.e., the activity of EC 4.6.1.13, phosphatidylinositol diacylglycerol-lyase, in vitro at high [Ca2+]. Four beta-isoforms regulated by G-proteins, two gamma-forms regulated by tyrosine kinases, four delta-forms regulated at least in part by calcium and an epsilon-form, probably regulated by the oncogene ras, have been found.
CAS REGISTRY NUMBER
COMMENTARY hide
37213-51-7
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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
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
show the reaction diagram
-
preferred substrate
-
?
phosphatidylinositol + H2O
?
show the reaction diagram
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Ca2+ required. At 0.1 mM the enzyme hydrolyzes phosphatidylinositol 4,5-diphosphate at faster rate than phosphatidylinositol, at 0.005 mM Ca2+ it hydrolyzes phosphatidylinositol 4,5-diphosphate exclusively
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-
?
phosphatidylinositol 4,5-bisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphatidylinositol 4,5-bisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
show the reaction diagram
-
the enzyme generates two second messengers: D-myo-inositol 1,4,5-trisphosphate and diacylglycerol
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CEP A stre, YC17, and TS141, the strains are isogenic to W303
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100600
-
x * 100600, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 100600, calculation from nucleotide sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Flick, J.S.; Thorner, J.
Genetic and biochemical characterization of a phosphatidylinositol-specific phospholipase C in Saccharomyces cerevisiae
Mol. Cell. Biol.
13
5861-5876
1993
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Rebecchi, M.J.; Pentyala, S.N.
Structure, function, and control of phosphoinositide-specific phospholipase C
Physiol. Rev.
80
1291-1335
2000
Arabidopsis thaliana, Saccharomyces cerevisiae, Dictyostelium discoideum, Drosophila sp. (in: flies), Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae PLC1p
Manually annotated by BRENDA team
Demczuk, A.; Guha, N.; Nguyen, P.H.; Desai, P.; Chang, J.; Guzinska, K.; Rollins, J.; Ghosh, C.C.; Goodwin, L.; Vancura, A.
Saccharomyces cerevisiae phospholipase C regulates transcription of Msn2p-dependent stress-responsive genes
Eukaryot. Cell
7
967-979
2008
Saccharomyces cerevisiae (P32383), Saccharomyces cerevisiae
Manually annotated by BRENDA team