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Title: Galactose- and maltose-stimulated lipoamide dehydrogenase activities related to the binding-protein-dependent transport of galactose and maltose in toluenized cells of Escherichia coli. Author: Richarme G, Heine HG. Journal: Eur J Biochem; 1986 Apr 15; 156(2):399-405. PubMed ID: 3084252. Abstract: The binding protein-dependent transport of galactose and maltose occurs at a reduced but significant rate in Escherichia coli cells which have undergone a mild toluenization. Dihydrolipoate and 3-acetyl-NAD produce a severalfold stimulation of these transports in the toluenized cells. In parallel to the stimulation of galactose and maltose transport by dihydrolipoate and 3-acetyl-NAD, there is a stimulation by galactose and maltose of lipoamide dehydrogenase activities which seem to be related to the binding-protein-dependent transport of these sugars. The lipoamide dehydrogenase component of the pyruvate and 2-oxoglutarate dehydrogenase complexes (the lpd gene product) is not involved in this stimulation. These results are discussed in relation to our recent studies showing a possible involvement of lipoic acid and of the 2-oxoacid dehydrogenases in the binding-protein-dependent transports.[Abstract] [Full Text] [Related] [New Search]