Phosphoserine phosphatase

From Proteopedia

Revision as of 07:03, 3 July 2016 by Michal Harel (Talk | contribs)
Jump to: navigation, search

Phosphoserine phosphatase dimer complex with phosphoserine 1l8o

Drag the structure with the mouse to rotate


Contents

Function

Phosphoserine phosphatase (PSP) catalyzes the dephosphorylation of phosphoserine to produce serine and phosphate. This is the last reaction in serine biosynthesis. PSP is part of the glycine, serine and threonine metabolism[1]. Mg+2 ion is a cofactor of PSP.

Disease

Mutations of PSP were found in patients with Williams syndrome[2].

Structural highlights

</StructureSection>

3D structures of phosphoserine phosphatase

Updated on 03-July-2016

References

  1. NEUHAUS FC, BYRNE WL. Metabolism of phosphoserine. II. Purification and properties of O-phosphoserine phosphatase. J Biol Chem. 1959 Jan;234(1):113-21. PMID:13610904
  2. Jaeken J, Detheux M, Fryns JP, Collet JF, Alliet P, Van Schaftingen E. Phosphoserine phosphatase deficiency in a patient with Williams syndrome. J Med Genet. 1997 Jul;34(7):594-6. PMID:9222972

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

Personal tools