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A “Radical Dance” in Thiamin Biosynthesis: Mechanistic Analysis of the Bacterial Hydroxymethylpyrimidine Phosphate Synthase
Author(s) -
Chatterjee Abhishek,
Hazra Amrita B.,
Abdelwahed Sameh,
Hilmey David G.,
Begley Tadhg P.
Publication year - 2010
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.201003419
Subject(s) - atp synthase , biosynthesis , chemistry , ribonucleotide , abstraction , biochemistry , active site , substrate (aquarium) , enzyme , stereochemistry , computational biology , combinatorial chemistry , biology , gene , philosophy , nucleotide , ecology , epistemology
Tricky things with ThiC : Hydroxymethylpyrimidine phosphate (HMP‐P) synthase (ThiC) catalyzes one of the most complex rearrangement reactions in primary metabolism. Deuteration experiments show that under reducing conditions, in the presence of aminoimidazole ribonucleotide, the 5′‐deoxyadenosyl radical generated at the active site of ThiC reacts directly with the substrate and performs two iterative hydrogen atom abstraction events to catalyze this rearrangement (see scheme; SAM= S ‐adenosylmethionine).