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Information on EC 3.1.4.11 - phosphoinositide phospholipase C and Organism(s) Gallus gallus

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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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Word Map
The taxonomic range for the selected organisms is: Gallus gallus
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
1-phosphatidyl-D-myo-inositol 4,5-bisphosphate inositoltrisphosphohydrolase
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1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase
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No receptor potential A protein
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phosphatidylinositol -phospholipase C
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phosphatidylinositol 4,5-bisphosphate phosphodiesterase
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phosphatidylinositol-4,5-bisphosphate phosphodiesterase
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phosphatidylinositol-4,5-bisphosphate phospholipase C
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phosphodiesterase, triphosphoinositide
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phosphoinositidase C
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phospholipase C
phosphotidylinositol 4,5-bisphosphate-specific phospholipase C
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PIC
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-
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PIP2 PDE
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PIP2 phosphodiesterase
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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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PtdIns(4,5)P2-directed phospholipase C
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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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-
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -
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
additional information
?
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-
phosphatidylinositol-phospholipase C plays a critical role, most likely through activation of protein kinase C pathway, in TLR4 mediated immune responses of avian macrophage cells to lipopolysaccharides
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?
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
additional information
?
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-
phosphatidylinositol-phospholipase C plays a critical role, most likely through activation of protein kinase C pathway, in TLR4 mediated immune responses of avian macrophage cells to lipopolysaccharides
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1 -[6-[[17-beta-3-methoxyestra-1,3,5(10)-trien-17-yl]amino] hexyl]-1H-pyrrole-2,5-dione)
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edelfosin
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U-73122
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PLCZ1_CHICK
637
0
72533
Swiss-Prot
other Location (Reliability: 1)
GDPD5_CHICK
599
6
69101
Swiss-Prot
other Location (Reliability: 5)
A0A1D5P143_CHICK
1033
0
117465
TrEMBL
other Location (Reliability: 5)
A0A3Q2U5R0_CHICK
1575
0
175907
TrEMBL
other Location (Reliability: 3)
A0A1D5PHP4_CHICK
1265
0
148107
TrEMBL
other Location (Reliability: 1)
A0A1D5PER6_CHICK
1223
0
142680
TrEMBL
other Location (Reliability: 2)
R4GLW0_CHICK
735
0
83875
TrEMBL
other Location (Reliability: 3)
A0A3Q2U0G2_CHICK
1210
0
137579
TrEMBL
other Location (Reliability: 2)
A0A3Q2U9P4_CHICK
1303
0
151186
TrEMBL
other Location (Reliability: 2)
F1NN68_CHICK
1277
0
147212
TrEMBL
other Location (Reliability: 2)
F1NDD2_CHICK
1038
0
117114
TrEMBL
Secretory Pathway (Reliability: 4)
E1C3D8_CHICK
781
0
89956
TrEMBL
Mitochondrion (Reliability: 4)
F1NLL3_CHICK
1155
0
132059
TrEMBL
other Location (Reliability: 2)
A0A3Q3AX15_CHICK
1206
0
137109
TrEMBL
other Location (Reliability: 2)
F1NUW4_CHICK
1022
0
113375
TrEMBL
other Location (Reliability: 5)
A0A1D5P5N5_CHICK
1139
0
126101
TrEMBL
Secretory Pathway (Reliability: 4)
A0A1D5NZL7_CHICK
1219
0
139213
TrEMBL
other Location (Reliability: 2)
A0A1D5PQ57_CHICK
2255
0
252614
TrEMBL
other Location (Reliability: 3)
A0A3Q2TWU3_CHICK
759
0
87251
TrEMBL
other Location (Reliability: 1)
A0A1L1RQE7_CHICK
789
0
89500
TrEMBL
other Location (Reliability: 5)
A0A3Q2U5C7_CHICK
1623
0
181589
TrEMBL
other Location (Reliability: 2)
E1C7E3_CHICK
1001
0
113220
TrEMBL
other Location (Reliability: 3)
A0A1D5PM11_CHICK
1071
0
118764
TrEMBL
Secretory Pathway (Reliability: 4)
A0A3Q2UM09_CHICK
1629
0
182013
TrEMBL
other Location (Reliability: 3)
A0A3Q2UNN2_CHICK
893
0
100235
TrEMBL
other Location (Reliability: 3)
A0A1D5PDS9_CHICK
1211
0
138636
TrEMBL
other Location (Reliability: 1)
F1P354_CHICK
1121
0
125598
TrEMBL
other Location (Reliability: 1)
A0A3Q2UAI3_CHICK
1587
0
177457
TrEMBL
other Location (Reliability: 2)
A0A3Q2TX28_CHICK
1155
0
133269
TrEMBL
other Location (Reliability: 5)
F1P0V6_CHICK
1585
0
177654
TrEMBL
other Location (Reliability: 2)
R4GFB3_CHICK
1194
0
135737
TrEMBL
other Location (Reliability: 2)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
He, H.; Genovese, K.J.; Nisbet, D.J.; Kogut, M.H.
Involvement of phosphatidylinositol-phospholipase C in immune response to Salmonella lipopolysacharide in chicken macrophage cells (HD11)
Int. Immunopharmacol.
6
1780-1787
2006
Gallus gallus
Manually annotated by BRENDA team
He, H.; Genovese, K.J.; Nisbet, D.J.; Kogut, M.H.
Phospholipase C, phosphatidylinositol 3-kinase, and intracellular [Ca(2+)] mediate the activation of chicken HD11 macrophage cells by CpG oligodeoxynucleotide
Dev. Comp. Immunol.
32
1111-1118
2008
Gallus gallus
Manually annotated by BRENDA team