protein tyrosine/threonine phosphatase activity

Definition

Target type: molecularfunction

Catalysis of the reactions: protein threonine phosphate + H2O = protein threonine + phosphate; and protein tyrosine phosphate + H2O = protein tyrosine + phosphate. [GOC:mah]

Protein tyrosine/threonine phosphatases (PTPs) are a diverse group of enzymes that catalyze the removal of phosphate groups from tyrosine and threonine residues of proteins. This dephosphorylation process plays a critical role in regulating a wide range of cellular processes, including signal transduction, cell cycle control, growth, differentiation, and apoptosis. PTPs are highly specific for their substrates, often targeting specific motifs or sequences within proteins. The active site of PTPs typically contains a conserved catalytic cysteine residue that acts as a nucleophile in the dephosphorylation reaction. This cysteine residue attacks the phosphate group of the substrate, forming a transient phosphotyrosine-cysteine intermediate. This intermediate is then hydrolyzed, releasing inorganic phosphate and regenerating the active enzyme. The activity of PTPs is tightly regulated by a variety of mechanisms, including substrate binding, allosteric regulation, and post-translational modifications. For example, some PTPs are activated by binding to specific adaptor proteins or by phosphorylation of their own regulatory domains. Others are inhibited by the binding of small molecules or by oxidation of their active site cysteine. Dysregulation of PTP activity has been implicated in a number of human diseases, including cancer, diabetes, and neurodegenerative disorders. The development of specific PTP inhibitors is therefore a promising therapeutic strategy for the treatment of these conditions.'
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Proteins (2)

Compounds (3)