Binding of the coenzyme and formation of the transketolase active center.

Abstract:

:Transketolase (TK) is a homodimer, the simplest representative of thiamine diphosphate (ThDP)-dependent enzymes. It was first ThDP-dependent enzymes the crystal structure of which has been solved and revealed the general fold for this class of enzymes and the interactions of the non-covalently bound coenzyme ThDP with the protein component. Transketolase is a convenient model to study the structure(s) of the active center and the mechanism of action of ThDP-dependent enzymes. This review summarizes the results of studies on the kinetics of the interaction of ThDP with TK from Saccharomyces cerevisiae as well as the generation of the catalytically active form of the coenzyme within the holoenzyme and formation of the enzyme's active center.

journal_name

IUBMB Life

journal_title

IUBMB life

authors

Kochetov G,Sevostyanova IA

doi

10.1080/15216540500167203

keywords:

subject

Has Abstract

pub_date

2005-07-01 00:00:00

pages

491-7

issue

7

eissn

1521-6543

issn

1521-6551

pii

NJ30260W273036XQ

journal_volume

57

pub_type

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