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Literature summary for 3.1.3.48 extracted from

  • Peti, W.; Page, R.
    Strategies to make protein serine/threonine (PP1, calcineurin) and tyrosine phosphatases (PTP1B) druggable Achieving specificity by targeting substrate and regulatory protein interaction sites (2015), Bioorg. Med. Chem., 23, 2781-2785 .
    View publication on PubMedView publication on EuropePMC
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Inhibitors

Inhibitors Comment Organism Structure
additional information the active sites of PTPs are exceptionally conserved and charged, making it nearly impossible to develop PTP inhibitors that are selective. But targeting PTP protein (substrate/regulatory) interaction sites, which are distal from the active sites, are highly viable and suitable drug targets. Domains outside PTP catalytic domains have also been demonstrated to directly alter PTP activity. Development of drugs that bind to intrinsically disordered regions of the enzyme, overview Homo sapiens
MSI-1436 small molecule inhibitor MSI-1436 binds to the disordered C-terminal domain of PTP1B, C-terminal to the catalytic domain, MSI-1436 functions using an allosteric mechanism to direct the enzymatic activity of PTP1B Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[a protein]-tyrosine phosphate + H2O Homo sapiens
-
 [a protein]-tyrosine + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P18031
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[a protein]-tyrosine phosphate + H2O
-
 Homo sapiens [a protein]-tyrosine + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
protein tyrosine phosphatase
-
 Homo sapiens
PTP1B
-
 Homo sapiens