Kinetic mechanism of active site non-equivalence in transketolase

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 consta...

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Bibliographic Details
Published inFEBS letters Vol. 418; no. 1; pp. 11 - 14
Main Authors Kovina, Marina V, Selivanov, Vitaliy A, Kochevova, Natalia V, Kochetov, German A
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 24.11.1997
Subjects
Binding Sites
Kinetic modeling
Kinetics
Models, Chemical
Saccharomyces cerevisiae - enzymology
TDP
Thiamine diphosphate
Thiamine Pyrophosphate - metabolism
Transketolase
Transketolase - chemistry
Transketolase - metabolism
TDP
Kinetic modeling
Thiamine diphosphate
Transketolase
TK
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)01331-8