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Updated: Aug 13, 2026

Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase
Published on: December 19, 2011
Kinetic mechanism of active site non-equivalence in transketolase
M V Kovina1, V A Selivanov, N V Kochevova
1A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia.
Abstract:
The two-step mechanism of coenzyme (TDP) binding to apotransketolase has been examined by kinetic modeling, and the rate and equilibrium constants for each binding step for two active sites have been determined. The dissociation constants for the primary fast binding step and the forward rate constants for the secondary slow binding step have been shown to be similar for two active sites. The backward rate constants for the secondary binding step are different for two active sites, providing the kinetic mechanism of their non-equivalence in TDP binding.
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