Importance of the C28-C38 hydrophobic domain of okadaic acid for potent inhibition of protein serine-threonine phosphatases 1 and 2A

V A Frydrychowski; R A Urbanek; A B Dounay; C J Forsyth

doi:10.1016/s0960-894x(01)00026-9

Importance of the C28-C38 hydrophobic domain of okadaic acid for potent inhibition of protein serine-threonine phosphatases 1 and 2A

Bioorg Med Chem Lett. 2001 Mar 12;11(5):647-9. doi: 10.1016/s0960-894x(01)00026-9.

Authors

V A Frydrychowski¹, R A Urbanek, A B Dounay, C J Forsyth

Affiliation

¹ Department of Chemistry, University of Minnesota, Minneapolis 55455, USA.

PMID: 11266161
DOI: 10.1016/s0960-894x(01)00026-9

Abstract

Okadaic acid is a potent inhibitor of select serine/threonine protein phosphatases. The importance of the C28-C38 hydrophobic domain of okadaic acid for inhibition of PP1 and PP2A was investigated. The hydrophobic domain is required but not sufficient for potent inhibition, and it also contributes to differential inhibition between PP1 and PP2A.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Enzyme Inhibitors / chemistry*
Molecular Conformation
Molecular Structure
Okadaic Acid / analogs & derivatives
Okadaic Acid / chemistry*
Phosphoprotein Phosphatases / antagonists & inhibitors*
Phosphoprotein Phosphatases / metabolism

Substances

Enzyme Inhibitors
Okadaic Acid
Phosphoprotein Phosphatases

Grants and funding

CA62195/CA/NCI NIH HHS/United States