Classification of protein-serine/threonine phosphatases: identification and quantitation in cell extracts.
作者： Philip Cohen
DOI: 10.1016/0076-6879(91)01035-Z
关键词: Turn (biochemistry) 、 Phosphorylase kinase 、 Serine 、 Molecular biology 、 Biochemistry 、 Phosphatase 、 Divalent 、 Biology 、 Threonine 、 Α subunit 、 Enzyme
摘要: Publisher Summary This chapter discusses the classification of protein-serine/threonine phosphatases. These enzymes are divided into two groups—type 1 and type 2, depending on whether they dephosphorylate β subunit phosphorylase kinase specifically inhibited by nanomolar concentrations, or α preferentially insensitive to inhibitors 2. The 2 phosphatases can, in turn, be subdivided three distinct enzymes—PP2A, PP2B, PP2C their dependence divalent cations.
sci-hub.se 参考文章(37)
C MacKintosh, J Coggins, P Cohen, Plant protein phosphatases. Subcellular distribution, detection of protein phosphatase 2C and identification of protein phosphatase 2A as the major quinate dehydrogenase phosphatase Biochemical Journal. ,vol. 273, pp. 733- 738 ,(1991) , 10.1042/BJ2730733
J Goris, W Merlevede, Isolation of an active form of the ATP+Mg2+-dependent protein phosphatase stimulated by the deinhibitor protein and by p-nitrophenyl phosphate Biochemical Journal. ,vol. 254, pp. 501- 507 ,(1988) , 10.1042/BJ2540501
S. Klumpp, P. Cohen, J.E. Schultz, Okadaic acid, an inhibitor of protein phosphatase 1 in Paramecium, causes sustained Ca2(+)-dependent backward swimming in response to depolarizing stimuli. The EMBO Journal. ,vol. 9, pp. 685- 689 ,(1990) , 10.1002/J.1460-2075.1990.TB08160.X
C MacKintosh, P Cohen, Identification of high levels of type 1 and type 2A protein phosphatases in higher plants Biochemical Journal. ,vol. 262, pp. 335- 339 ,(1989) , 10.1042/BJ2620335
P Cohen, P T W Cohen, Protein phosphatases come of age. Journal of Biological Chemistry. ,vol. 264, pp. 21435- 21438 ,(1989) , 10.1016/S0021-9258(20)88197-6
H Usui, M Imazu, K Maeta, H Tsukamoto, K Azuma, M Takeda, Three distinct forms of type 2A protein phosphatase in human erythrocyte cytosol. Journal of Biological Chemistry. ,vol. 263, pp. 3752- 3761 ,(1988) , 10.1016/S0021-9258(18)68988-4
M D Pato, E Kerc, Purification and characterization of a smooth muscle myosin phosphatase from turkey gizzards. Journal of Biological Chemistry. ,vol. 260, pp. 12359- 12366 ,(1985) , 10.1016/S0021-9258(17)39033-6
P Agostinis, J Goris, E Waelkens, L A Pinna, F Marchiori, W Merlevede, Dephosphorylation of phosphoproteins and synthetic phosphopeptides. Study of the specificity of the polycation-stimulated and MgATP-dependent phosphorylase phosphatases. Journal of Biological Chemistry. ,vol. 262, pp. 1060- 1064 ,(1987) , 10.1016/S0021-9258(19)75749-4
Philip Cohen, Susana Alemany, Brian A. Therese, J. Resink, Peter Stralfors, H.Y. Lim Tung, Protein phosphatase-1 and protein phosphatase-2A from rabbit skeletal muscle. Methods in Enzymology. ,vol. 159, pp. 390- 408 ,(1988) , 10.1016/0076-6879(88)59039-0
C Bialojan, A Takai, Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics Biochemical Journal. ,vol. 256, pp. 283- 290 ,(1988) , 10.1042/BJ2560283