"A Radical dance in thiamin biosynthesis: Mechanistic analysis of the bacterial hydroxymethylpyrimidine phosphate synthase" by Abhishek Chatterjee

Article

A Radical dance in thiamin biosynthesis: Mechanistic analysis of the bacterial hydroxymethylpyrimidine phosphate synthase

Chemistry & Physics Faculty Publications

Abhishek Chatterjee, Texas A&M University
Amrita B. Hazra, Texas A&M University
Sameh Abdelwahed, Texas A&M University
David G. Hilmey, Texas A&M University
Tadhg P. Begley, Texas A&M University

Document Type

Article

Publication Date

11-8-2010

Abstract

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). © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Citation Information

Abhishek Chatterjee, Amrita B. Hazra, Sameh Abdelwahed, David G. Hilmey, et al.. "A Radical dance in thiamin biosynthesis: Mechanistic analysis of the bacterial hydroxymethylpyrimidine phosphate synthase" (2010)
Available at: http://works.bepress.com/Sameh-Abdelwahed/6/