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The Enamine Intermediate May Not Be Universal to Thiamine Catalysis
Author(s) -
Amara Patricia,
Fdez. Galván Ignacio,
FontecillaCamps Juan C.,
Field Martin J.
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200702993
Subject(s) - enamine , thiamine , chemistry , oxidoreductase , catalysis , transketolase , active site , stereochemistry , enzyme , biochemistry , photochemistry
Contrast and controversy : Molecular modeling of the degradation of pyruvate in the active site of pyruvate:ferredoxin oxidoreductase (PFOR) and comparison of the energy cost of enamine formation in PFOR and transketolase has shown that in this case enamine formation, generally postulated for such enzymes, is unlikely. Optimized structures of possible intermediates are shown overlayed with an X‐ray crystal structure of the active site of the radical PFOR.