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  • Title: The binding of glycerol kinase to the outer membrane of rat liver mitochondria: its importance in metabolic regulation.
    Author: Ostlund AK, Göhring U, Krause J, Brdiczka D.
    Journal: Biochem Med; 1983 Oct; 30(2):231-45. PubMed ID: 6316940.
    Abstract:
    Glycerol kinase was found to associate with the hexokinase binding protein. The binding of glycerol kinase has a high specificity as illustrated by the fact that the magnitude of binding was reduced by glycerophosphate and antibodies against the hexokinase binding protein. A possible function of glycerol kinase binding to the mitochondria with respect to metabolic regulation is proposed for the following reasons: (i) Glycerol kinase seems to bind to the same binding protein as hexokinase. (ii) Both kinases were observed to be reversibly bound to the mitochondria in different metabolic situations, i.e., 10% of total cellular activity from both kinases is bound in starved rats whereas no activity of glycerol kinase and 30% of hexokinase become bound in fed rats. (iii) The kinetic properties of the associated glycerol kinase change in an analogous manner to those known for structure-bound hexokinase. (iv) With the binding of glycerol kinase to the mitochondria, it is possible to propose a metabolic pathway for glycerol oxidation to dihydroxyacetone phosphate by a combined action involving the enzyme, glycerol phosphate oxidase, and oxidative phosphorylation.
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