| Literature DB >> 8397116 |
K A Oxenrider1, M E Rasche, M V Thorsteinsson, P J Kennelly.
Abstract
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.Entities:
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Year: 1993 PMID: 8397116 DOI: 10.1016/0014-5793(93)80355-x
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124