Nonequivalence of transketolase active centers with respect to acceptor substrate binding

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 transketol...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2007-10, Vol.361 (4), p.1044-1047
Main Authors: Yurshev, Vladimir A., Sevostyanova, Irina A., Solovjeva, Olga N., Zabrodskaya, Svetlana V., Kochetov, German A.
Format: Article
Language:English
Subjects:
Binding Sites
Negative cooperativity
Nonequivalence of active centers
Ribosemonophosphates - metabolism
Transketolase
Transketolase - chemistry
Transketolase - metabolism
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2007.07.132