Cooperativity and flexibility of active sites in homodimeric transketolase

FEBS Letters

Kochetov, German A¹  Kovina, Marina V¹ 

[1] A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119899 Moscow, Russia

关键词: Transketolase;    Flip-flop mechanism;    Alternative site reactivity;    Half-of-the-sites reactivity;    Active site flexibility;    TK;    transketolase;    ThDP;    thiamine diphosphate;    F6P;    fructose 6-phosphate;    HP;    hydroxypyruvate;   

DOI  :  10.1016/S0014-5793(98)01423-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Here we summarize evidence for non-equivalence of two structurally similar active sites in transketolase and other thiamine-dependent enzymes. This non-equivalence takes place when the enzymes interact with various ligands (inhibitors, cations, coenzyme and substrates). Data on different strains in the structure of the holotransketolase subunits are also given. The above results are discussed within the framework of a concept of permanent alternative site oscillation of the transketolase molecule in the presence and in the absence of substrate as a manifestation of a ‘flip-flop' mechanism.

【 授权许可】

Unknown