Skip to main content

Table 1 Inhibition of PP1 and PP2A by some naturally occurring inhibitors

From: Protein phosphatases 1 and 2A and their naturally occurring inhibitors: current topics in smooth muscle physiology and chemical biology

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)

  1. 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)
  2. n.d. not determined
  3. aUnpublished K i data of A. Takai
  4. 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])
  5. c,dAlso called nodularin-R and nodularin-V, respectively