INHIBITION OF AN ARCHAEAL PROTEIN PHOSPHATASE-ACTIVITY BY OKADAIC ACID, MICROCYSTIN-LR, OR CALYCULIN-A

被引：16

作者：

OXENRIDER, KA

RASCHE, ME

THORSTEINSSON, MV

KENNELLY, PJ

机构：

[1] Department of Biochemistry and Anaerobic Microbiology, Virginia Polytechnic Institute, State University, Blacksburg

来源：

FEBS LETTERS | 1993年 / 331卷 / 03期

关键词：

PROTEIN PHOSPHATASE; OKADAIC ACID; MICROCYSTIN-LR; CALYCULIN-A; ARCHAEA;

D O I：

10.1016/0014-5793(93)80355-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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.

引用

页码：291 / 295

页数：5

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