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.

3.1.1: Carboxylic
ester hydrolases

Exodeoxyribonuclease	RecBCD
Exoribonuclease	Oligonucleotidase

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme;see ((Restriction enzyme)) UvrABC endonuclease
Endoribonuclease	RNase III Drosha: Microprocessor complex Dicer: RNA-induced silencing complex RNase H 1 2A 2B 2C RNase P RNase A RNase Z RNase E 1 2 3 4/5 RNase T1
either deoxy- or ribo-	Nuclease S1 Mung bean nuclease Serratia marcescens nuclease Micrococcal nuclease

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)