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The inhibition of isocitrate lyase fromEscherichia coli by glyoxylate
Authors:Young-Hee Ko  Dr Bruce A McFadden
Institution:(1) Department of Biochemistry and Biophysics, Washington State University, Pullman, Washington, USA
Abstract:Inhibition patterns have been studied to shed light on the current controversy involving the kinetic mechanism for isocitrate lyase fromEscherichia coli. A new coupled enzymatic assay for the product succinate has been developed, enabling the determination that glyoxylate, the other product, is a linear competitive inhibitor of isocitrate cleavage. This and other evidence suggest that the kinetic mechanism is steady-state, ordered uni-bi, and that succinate and glyoxylate are sequentially released from the enzyme after cleavage of isocitrate.
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