Phosphoserine phosphatase

From Wikipedia, the free encyclopedia

In enzymology, a phosphoserine phosphatase (EC 3.1.3.3) is an enzyme that catalyzes the chemical reaction

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

The 3 substrates of this enzyme are O-phospho-L-serine, O-phospho-D-serine, and H₂O, whereas its 3 products are L-serine, D-serine, and phosphate.

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

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 3.1.3.3
BRENDA references for 3.1.3.3 (Recommended.)
PubMed references for 3.1.3.3
PubMed Central references for 3.1.3.3
Google Scholar references for 3.1.3.3
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: 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 and Byrne WL (1959). "Metabolism of phosphoserine. II. Purification and properties of O-phosphoserine phosphatase". J. Biol. Chem. 234: 113–121.