Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1936649 | Biochemical and Biophysical Research Communications | 2007 | 4 Pages |
Abstract
The interaction of transketolase with its acceptor substrate, ribose 5-phosphate, has been studied. The active centers of the enzyme were shown to be functionally nonequivalent with respect to ribose 5-phosphate binding. Under the conditions where only one out of the two active centers of transketolase is functional, their affinities for ribose 5-phosphate are identical. The phenomenon of nonequivalence becomes apparent when the substrate interacts with one of the two active centers. As a consequence of such interaction, the affinity of the second active center for ribose 5-phosphate decreases.
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Authors
Vladimir A. Yurshev, Irina A. Sevostyanova, Olga N. Solovjeva, Svetlana V. Zabrodskaya, German A. Kochetov,