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. 1989 Dec 8;993(2-3):224-7.
doi: 10.1016/0304-4165(89)90168-2.

Amiloride activation of hepatic microsomal glucose-6-phosphatase; activation of T1?

J Pears  1 , R T Jung, A Burchell
Affiliations

Amiloride activation of hepatic microsomal glucose-6-phosphatase; activation of T1?

J Pears et al. Biochim Biophys Acta. .

Abstract

The mechanism of activation of hepatic microsomal glucose-6-phosphatase (EC 3.1.3.9) in vitro by amiloride has been investigated in both intact and fully disrupted microsomes. The major effect of amiloride is a 4.5-fold reduction in the Km of glucose-6-phosphatase activity in intact diabetic rat liver microsomes. Amiloride also decreased the Km of glucose-6-phosphatase activity in intact liver microsomes isolated from starved rats 2.5-fold. Kinetic calculations, direct enzyme assays and direct transport assays all demonstrated that the site of amiloride action was T1, the hepatic microsomal glucose 6-phosphate transport protein. This is, to our knowledge, the first report of an activation of any of the proteins of the multimeric hepatic microsomal glucose-6-phosphatase complex.

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