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Phosphoserine phosphatase

From Wikipedia, the free encyclopedia

The enzyme phosphoserine phosphatase (EC 3.1.3.3) catalyzes the reaction

O-phospho-L(or D)-serine + H2O L(or D)-serine + phosphate

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is O-phosphoserine phosphohydrolase. This enzyme participates in glycine, serine and threonine metabolism.

Structural studies

As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1F5S, 1J97, 1L7M, 1L7N, 1L7O, 1L7P, 1L8L, 1L8O, 1NNL, 2J6Y, 2J6Z, and 2J70.

References

  • Borkenhagen LF, Kennedy EP (1959). "The enzymatic exchange of L-serine with 'O-phospho-L-serine catalyzed by a specific phosphatase". J. Biol. Chem. 234 (4): 849–53. PMID 13654276.
  • Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, p. 73-78.
  • Neuhaus FC, Byrne WL (1959). "Metabolism of phosphoserine. II. Purification and properties of O-phosphoserine phosphatase". J. Biol. Chem. 234 (1): 113–121. PMID 13610904.


This page was last edited on 26 August 2023, at 15:26
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