Cooperativity and flexibility of active sites in homodimeric transketolase.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kovina MV,Kochetov GA

doi

10.1016/s0014-5793(98)01423-9

subject

Has Abstract

pub_date

1998-11-27 00:00:00

pages

81-4

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(98)01423-9

journal_volume

440

pub_type

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