A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase (cf. EC 188.8.131.52 protein-tyrosine-phosphatase). The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 184.108.40.206, phosphoamidase).
Deutscher, J., Kessler, U. and Hengstenberg, W. Streptococcal phosphoenolpyruvate: sugar phosphotransferase system: purification and characterization of a phosphoprotein phosphatase which hydrolyzes the phosphoryl bond in seryl-phosphorylated histidine-containing protein. J. Bacteriol.163 (1985) 1203–1209. [PMID: 2993239]
Ingebritsen, T.S. and Cohen, P. The protein phosphatases involved in cellular regulation. 1. Classification and substrate specificities. Eur. J. Biochem.132 (1983) 255–261. [DOI] [PMID: 6301824]
Sundarajan, T.A. and Sarma, P.S. Substrate specificity of phosphoprotein phosphatase from spleen. Biochem. J.71 (1959) 537–544. [PMID: 13638262]
Tonks, N.K. and Cohen, P. The protein phosphatases involved in cellular regulation. Identification of the inhibitor-2 phosphatases in rabbit skeletal muscle. Eur. J. Biochem.145 (1984) 65–70. [DOI] [PMID: 6092084]
[EC 220.127.116.11 created 1961, modified 1989, modified 2013]