Protein tyrosine phosphatases (PTPs) are involved in a variety of cellular processes such as signal transduction, cell cycle regulation, and differentiation. This enzyme is a low molecular weight cytosolic protein that is 157 amino acid residues long. Biologically, tyrosine phosphatase acts on tyrosine phosphorylated proteins, low molecular weight aryl phosphates, and acyl phosphates (both natural and synthetic). Thus, it catalyzes the transfer of a phosphate group from a protein to water creating an orthophosphate. However, this enzyme is inhibited by sulfhydryl reagents.
Tyrosine phosphatase has a beta alpha beta structural motif. This enzyme consists of a four-stranded parallel beta sheet (gold), four alpha-helices (red), and a single 310 helix (purple).