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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1d5r

E.C. namephosphoprotein phosphatase
SpeciesHomo sapiens (Human)
E.C. Number (IntEnz) 3.1.3.16
CSA Homologues of 1d5rThere are 79 Homologs
CSA Entries With UniProtID P60484
CSA Entries With EC Number 3.1.3.16
PDBe Entry 1d5r
PDBSum Entry 1d5r
MACiE Entry 1d5r

Literature Report

IntroductionPTEN is a phosphatase and a tumour suppressor. It can act on both polypeptide and phosphoinositide substrates in vitro. PTEN can dephosphorylate tyrosine-, serine-, and threonine-phosphorylated peptides, and this activity requires highly acidic substrates. PTEN can also dephosphorylate phosphatidylinositol (3,4,5)-trisphosphate in vitro, with specificity for the phosphate group at the D3 position of the inositol ring.
MechansimThe mechanism of PTEN is similar to that of Protein Tyrosine Phosphatase 1B. Cys124 functions as a nucleophile, accepting the phosphate moiety from the phosphorylated amino acid and generating a phosphocysteine intermediate. Asp92 serves as an acid to protonate the hydroxyl oxygen atom of the leaving group. Next, the phosphate moiety is transferred to a water molecule, restoring the enzyme. Arg130 stabilises the transition state.
Reaction

Catalytic Sites for 1d5r

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspA9292macie:sideChainIt serves as an acid to protonate the hydroxyl oxygen atom of the leaving group.
ArgA130130macie:sideChainIt stabilises the transition state.
CysA124124macie:sideChainIt acts as a nucleophile, accepting the phosphate moiety from the phosphorylated amino acid and generating a phosphocysteine intermediate.

Literature References

Notes:
Maehama T
The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate.
J Biol Chem 1998 273 13375-13378
PubMed: 9593664
Lee JO
Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association.
Cell 1999 99 323-334
PubMed: 10555148
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