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Literature summary for 3.1.3.48 extracted from

  • Chen, V.L.; Bishop, A.C.
    Chemical rescue of protein tyrosine phosphatase activity (2010), Chem. Commun. (Camb. ), 46, 637-639.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information inhibition of the WPD-loop can be used to potently and specifically turn on the activity of a biologically important tyrosine phosphatase, PTP-PEST Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information the catalytically critical loop of the PTP domain, the WPD loop, can be engineered to contain cysteine-rich elements that bind the inhibitory biarsenical reagent Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Synonyms

Synonyms Comment Organism
protein tyrosine phosphatase
-
Homo sapiens

General Information

General Information Comment Organism
malfunction improperly regulated PTP activity has been implicated in a range of human diseases including leukemia, solid-tumor cancers, diabetes, and several autoimmune disorders Homo sapiens
physiological function protein tyrosine phosphatases are a large and important class of signaling enzymes that catalyze the dephosphorylation of phosphotyrosine in protein substrates. A number of PTPs are tumor-suppressor proteins. PEST is a wide-ranging and ubiquitously expressed signaling molecule, which is involved in the regulation of osteoclast activation, cell motility and adhesion, the immune response, and apoptosis Homo sapiens