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Crystal structure of transketolase in complex with thiamine thiazolone diphosphate, an analogue of the reaction intermediate, at 2.3 Å resolution
Author(s) -
Nilsson Ulrika,
Lindqvist Ylva,
Kluger Ronald,
Schneider Gunter
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81779-y
Subject(s) - transketolase , thiamine , chemistry , resolution (logic) , crystal structure , crystal (programming language) , crystallography , stereochemistry , biochemistry , enzyme , computer science , programming language , artificial intelligence
The crystal structure of the complex of transketolase and thiamine thiazolone diphosphate has been determined at 2.3 Å resolution. The complex has a structure which closely resembles that of this enzyme with the cofactor ThDP. This is consistent with the observation that the binding of the analogue to transketolase involves ground state rather than transition state interactions. Since thiamine thiazolone diphosphate resembles an expected intermediate in the catalytic pathway, the structure of the intermediate was modelled from the crystal structure. Based on this model, enzymic groups responsible for binding of the intermediate and proton transfer during catalysis are suggested.