Abstract
A fluorescence polarization study reveals that 1 N6-ethenoadenosine triphosphate (ɛATP) binds to native aspartate transcarbamylase (ATCase) from E. coli. However, unlike adenosine triphosphate (ATP) ɛATP inhibits the enzyme, which strongly suggests that the N-1 atom in the purine ring is crucial for ATP activation. Study of the binding curve for ɛATP shows multiple binding sites with overlapping affinities, but a simple system of six equivalent binding sites with a dissociation constant K = 7.5 × 10−5M gives a reasonable approximation to the experimental data.
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