S. Mitsuhashi et al., Tautomycetin is a novel and specific inhibitor of serine/threonine proteinphosphatase type 1, PP1, BIOC BIOP R, 287(2), 2001, pp. 328-331
Citations number
27
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Here we isolated tautomycetin, TC, and examined its phosphatase inhibitory
activity. Recently we have reported that the left-hand moiety of tautomycin
, TM, and the right one containing the spiroketal are essentially required
for inhibition of protein phosphatase, PP, and induction of apoptosis, resp
ectively. TC is structurally almost identical to TM except that TC is lacki
ng the spiroketal, which has the potential apoptosis-inducing activity. TC
specifically inhibited PP1 activity, IC50 values for purified PP1 and PP2A
enzymes being 1.6 and 62 nM, respectively, whereas the IC50 values of TM we
re 0.21 and 0.94 nM, respectively. These results demonstrate that TC is the
most specific PPI inhibitor out of over 40 species of natural phosphatase
inhibitors reported, strongly suggesting that TC is a novel powerful tool t
o elucidate the physiological roles of PP1 in various biological events. (C
) 2001 Academic Press.