Human Phosphoserine phosphatase (hPSP) is an important enzyme in the phosphorylated pathway of serine biosynthesis, which contributes a major portion of the endogenous L-serine. Similar to known L-3-phosphoserine phosphatases, it catalyzed the Mg2+-dependent hydrolysis of L-phosphoserine and an exchange reaction between L-serine and L-phosphoserine. Recently, its complex structures reveal that the open-closed environmental change of the active site, generated -helical bundle domain, is important to substrate by local rearrangement of the recognition and hydrolysis.
Phosphoserine Phosphatase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids and having a molecular mass of 25 kDa.
PSP was overexpressed in E. coli and purified by conventional chromatography.
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