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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.

PTEN dephosphorylates PIP3

PI(3,4,5)P3 + H2O → PI(4,5)P2 + Pi

Reactome: R-HSA-199456
Compartment: cytosol · plasma membrane
Rhea: RHEA:25017

Inputs

PI(3,4,5)P3CHEBI:57836, C11H13O22P4R2, plasma membrane
H2OCHEBI:15377, H2O, cytosol

Outputs

PI(4,5)P2CHEBI:58456, C11H14O19P3R2, plasma membrane
PiCHEBI:43474, HO4P, cytosol

Catalysed by

phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity of PTEN [cytosol]EC 3.1.3.67; UniProt P60484

Literature

Membrane-binding and activation mechanism of PTEN Proc Natl Acad Sci U S A, 2003
The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate J Biol Chem, 1998
The lipid phosphatase activity of PTEN is critical for its tumor supressor function Proc Natl Acad Sci U S A, 1998
Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association Cell, 1999
Purification and characterization of the phosphatidylinositol-3,4,5-trisphosphate phosphatase in bovine thymus Eur. J. Biochem., 1996