Interaction of tetraiodofluorescein with a modified form of aspartate transcarbamylase.
Academic Article
Overview
abstract
Low concentrations of the dye tetraiodofluorescein activate native aspartate transcarbamylase (aspartate carbomoyltransferase, carbomoylphosphate:L-aspartate carbomoyltransferase, EC 2.1.3.2), while high concentrations inhibit the enzyme's activity [Jacobsberg, L. B., Kantrowitz, E. R. & Lipscomb, W. N. (1975) J. Biol. Chem. 250, 9238-9249]. This dye is now shown to produce similar effects upon a modified form of aspartate transcarbamylase produced by Escherichia coli grown in a culture medium supplemented with thiouracil. Significantly, the ATP-induced activation is reduced in the modified form of the enzyme to the same extent as is the tetraiodofluorescein-induced activation. Thus, a relationship is demonstrated between the internal mechanisms by which ATP and tetraiodofluorescein activate aspartate transcarbamylase.
