Inhibition of an archaeal protein phosphatase activity by okadaic acid, microcystin‐LR, or calyculin A

FEBS Letters

Thorsteinsson, Marc V.¹  Kennelly, Peter J.¹  Rasche, Madeline E.¹  Oxenrider, Keith A.¹ 

[1] Department of Biochemistry and Anaerobic Microbiology, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061-0308, USA

关键词: Protein phosphatase;    Okadaic acid;    Microcystin-LR;    Calyculin A;    Archaea;   

DOI  :  10.1016/0014-5793(93)80355-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Soluble extracts of the methanogenic archaeon, Methanosarcina thermophila TM-1, contained a divalent metal ion-stimulated protein-serine phosphatase activity. This activity was sensitive to micromolar concentrations of okadaic acid, microcystin-LR, or calyculin A, three compounds thought to be highly specific inhibitors of the type 1/2A/2B genetic superfamily of eukaryotic protein-serine/threonine phosphatases. The observation that each of these three chemically unrelated compounds inhibited this archaeal protein phosphatase activity suggests the existence of structural homology, and perhaps even common genetic ancestry, with the type 1/2A/2B superfamily of protein-serine/threonine phosphatases found in eukaryotic organisms.

【 授权许可】

Unknown