Inhibitors |
K
i (nM) | References |
---|
PP1 | PP2A |
---|
Okadaic acid | 150 | 0.032 |
80–82
|
Calyculin A | 1 | 0.13 |
82, (83, 84) |
Tautomycin | 0.5 | 30 |
82, (85) |
Microcystin-LR | 0.22 | 0.008 |
82, (86, 87) |
Nodularinc
| 0.11a
| 0.022a
| (88) |
Motuporind
| <1b
| n.d. | (89) |
Cantharidin | 470b
| 40b
| (90, 91) |
Fostriecin | 130 μMb
| 3b
| (92) |
Rubratoxin A | >200 μMb
| 30b
| (93) |
- The dissociation constants (K
i) for the interaction of PP1 and PP2A with the naturally occurring inhibitors referred to in this review are listed. The values are in nM, unless otherwise stated. The difference between K
i and ID50 is usually negligible for inhibitors with relatively low affinity (say, K
i > 100 nM)
-
n.d. not determined
-
aUnpublished K
i data of A. Takai
-
bID50 instead of unavailable K
i data. The references in parentheses present ID50, which is generally dependent on the concentration of phosphatase in the assay (see Takai and Mieskes [80])
-
c,dAlso called nodularin-R and nodularin-V, respectively