Kinetic mechanism of active site non-equivalence in transketolase
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(97)01331-8/fullpdf
Reference20 articles.
1. Kinetics of reconstruction of holo-transketolase
2. The binding of thiamine pyrophosphate with transketolase in equilibrium conditions
3. The number of active sites in a molecule of transketolase
4. The functional identity of the active centres of transketolase
5. Transketolase kinetics. The slow reconstitution of the holoenzyme is due to rate-limiting dimerization of the subunits.
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1. Novel insights into transketolase activation by cofactor binding identifies two native species subpopulations;Scientific Reports;2019-11-06
2. Stages of the formation of nonequivalence of active centers of transketolase from baker’s yeast;Molecular Catalysis;2019-04
3. Structure and functioning mechanism of transketolase;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2014-09
4. Functional nonequivalence of transketolase active centers;IUBMB Life;2010-11
5. Crystal structure ofBifidobacterium Longumphosphoketolase; key enzyme for glucose metabolism inBifidobacterium;FEBS Letters;2010-07-30
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