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Literature summary for 3.1.3.48 extracted from

  • Chia, J.Y.; Gajewski, J.E.; Xiao, Y.; Zhu, H.J.; Cheng, H.C.
    Unique biochemical properties of the protein tyrosine phosphatase activity of PTEN-demonstration of different active site structural requirements for phosphopeptide and phospholipid phosphatase activities of PTEN (2010), Biochim. Biophys. Acta, 1804, 1785-1795.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant PTEN in Spodoptera fruiperda Sf9 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
C124S site-directed mutagenesis, inactive mutant Homo sapiens
D92A site-directed mutagenesis, the D92A mutation causes a 250 to 700fold reduction in phospholipid phosphatase activity of PTEN, the mutation perturbs the structure and function of the active site imposing significantly different impacts on the two activities of PTEN Homo sapiens
G129E naturally occuring mutation, the Cowden syndrome-associated G129E mutation abrogates the phospholipid phosphatase activity but not the phosphoprotein phosphatase activity of PTEN, the mutation perturbs the structure and function of the active site imposing significantly different impacts on the two activities of PTEN, complete loss of phospholipid phosphatase activity of the G129E PTEN mutant Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic analyses of the effects of D92A and G129E mutations on the phospholipid and phosphoprotein phosphatase activities of PTEN Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens PTEN phosphoprotein phosphatase catalysis of phosphoprotein dephosphorylation follows a two-step mechanism with Cys124 transiently phosphorylated to form the phosphoenzyme intermediate ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation, possibly at Ser380, Thr382 and Thr383 at the C-terminal tail suppresses the activity of PTEN and D92A PTEN, dephosphorylation of recombinant wild-type PTEN and D92A PTEN leaads to a 2-5 fold increase in phosphatase activity. PTEN reacts with pY-SOP to form a phospho-PTEN protein. The phosphoPTEN protein is not the cysteinyl phosphoenzyme intermediate formed by transient phosphorylation of Cys124 in the course of phosphopeptide dephosphorylation reaction Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant PTEN from Spodoptera fruiperda Sf9 cells by anion exchange chromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PTEN phosphoprotein phosphatase catalysis of phosphoprotein dephosphorylation follows a two-step mechanism with Cys124 transiently phosphorylated to form the phosphoenzyme intermediate Homo sapiens ?
-
?
additional information Ser380, Thr382 and Thr383 C-terminal tail residues do not affect the recruitment of the WPD-loop into the active site to participate in the phosphoprotein dephosphorylation reaction, catalytic mechanism of PTEN phosphoprotein phosphatase activity, overview. The phosphoPTEN protein is not the cysteinyl phosphoenzyme intermediate formed by transient phosphorylation of Cys124 in the course of phosphopeptide dephosphorylation reaction. PTEN can adopt the closed conformation to allow Asp92 to participate in catalysis when it dephosphorylates the physiological protein substrates such as FAK and Shc in cells Homo sapiens ?
-
?
protein FAK + H2O
-
Homo sapiens ?
-
?
protein Shc + H2O
-
Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
protein tyrosine phosphatase
-
Homo sapiens
PTEN phosphoprotein phosphatase
-
Homo sapiens

General Information

General Information Comment Organism
malfunction the Cowden syndrome-associated G129E mutation abrogates the phospholipid phosphatase activity but not the phosphoprotein phosphatase activity of PTEN Homo sapiens