Survey of calcineurin activity towards nonprotein compounds and identification of XXXX as a substrate.

@entity14855 @entity7954 @entity3281 @entity10393 @entity3411 @entity7480
@entity14855 , originally identified as a calmodulin-dependent phosphoprotein phosphatase (Stewart, A.A. et al. (1982) FEBS Lett. 137, 80-84) also uses @entity7480 and @entity10393 as substrates (Pallen, C.J. and Wang, J.H. (1983) J. Biol. Chem. 258, 8550-8553). We have surveyed a wide range of nonprotein phosphocompounds and found that several synthetic aryl phosphocompounds serve as calcineurin substrates. Among more than 20 naturally occurring phosphocompounds tested, only @entity7954 possesses significant @entity14855 substrate activity. The @entity7954 phosphatase activity is dependent on @entity3411 and @entity3281 , is stimulated by calmodulin, and is inhibited by a monoclonal antibody to calcineurin, thus indicating that it is an intrinsic property of calcineurin. The results suggest that functional roles of calcineurin may include actions of the enzyme toward nonprotein phosphocompounds.
