The inhibition of isocitrate lyase fromEscherichia coli by glyoxylate |
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Authors: | Young-Hee Ko Dr. Bruce A. McFadden |
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Affiliation: | (1) Department of Biochemistry and Biophysics, Washington State University, Pullman, Washington, USA |
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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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