In: Biology
Protein tyrosine phosphatases display exquisite specificity for their substrates, unlike most serine/threonine protein phosphatases, which have rather broad specificity.
The given statement is true.
Substrate phosphorylation and dephosphorylation plays a key role in switching on and off a signal during cell signalling. The phosphorylation is driven by protein kinases which generally triggers a downstrean signalling response. However, it is phosphatase at work which ensures that the signalling does not remain active constitutively. Phosphatases dephosphorylate the target molecule and stops the signalling cascade.
The reason behind absolute specificity of Protein tyrosine phosphatases is that they are actively involved in cell signalling response. In a cell there are so many interconnected signalling going on. If a Protein tyrosine phosphatases is not specific for it's substrate (phosphorylated tyrosine residue of a specific protein) then it can arrest a non target signalling and that can be deleterious for the cell, Whereas, serine/threonine protein phosphatases have wide specificity.