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DraconiticBiochemistryBiomolecules · Catabolism · Biosynthesis · MetabolismMap

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Human metabolism

Reactome's human metabolism drawn as one network. Each molecule has one home node; widely shared molecules also appear as dashed copies in other territories, linked from their details. .

Territories

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Metabolite; its structure appears as you zoom in
Reaction, arrow toward the product
Cofactors and co-substrates are written beside the reaction when you zoom in
Dashed ring: a copy of a widely shared molecule or cofactor in another territory or pathway
Compartment transfer of the molecule it is linked to
Binding, release or complex event; its proteins are named in its details
Outline: reactions mostly in the mitochondrion

Arrows follow Reactome's curated reaction direction.

PI(4,5)P2 is hydrolysed to I(1,4,5)P3 and DAG by tethered PLC[1] at the plasma membrane

PI(4,5)P2 + H2O → DAG + I(1,4,5)P3 + H+

Reactome: R-HSA-1855221
Compartment: plasma membrane · cytosol
Rhea: RHEA:33180, RHEA:33179

Inputs

PI(4,5)P2CHEBI:58456, C11H14O19P3R2, plasma membrane
H2OCHEBI:15377, H2O, cytosol

Outputs

DAGCHEBI:17815, C5H6O5R2, plasma membrane
I(1,4,5)P3CHEBI:203600, C6H9O15P3, cytosol
H+CHEBI:15378, H, cytosol

Catalysed by

phosphatidylinositol-4,5-bisphosphate phospholipase C activity of PLCdegh [plasma membrane]EC 3.1.4.11

Literature

Cloning and identification of amino acid residues of human phospholipase C delta 1 essential for catalysis J Biol Chem, 1995
A novel bifunctional phospholipase c that is regulated by Galpha 12 and stimulates the Ras/mitogen-activated protein kinase pathway J Biol Chem, 2001
Purification and characterization of membrane-bound phospholipase C specific for phosphoinositides from human platelets J Biol Chem, 1988
Expression, purification and kinetic properties of human recombinant phospholipase C delta 3 Acta Biochim Pol, 1997
Phosphorylation of Nephrin Triggers Ca2+ Signaling by Recruitment and Activation of Phospholipase C-{gamma}1 J Biol Chem, 2009
Molecular cloning and characterization of a novel phospholipase C, PLC-eta Biochem J, 2005