Biosynthesis of the thiamin pyrimidine: the reconstitution of a remarkable rearrangement reaction. Academic Article

abstract

• The conversion of 5-aminoimidazole ribonucleotide (AIR) into 4-amino-2-methyl-5-hydroxymethylpyrimidine (HMP) is a fascinating reaction on the thiamin biosynthetic pathway in bacteria and is probably the most complex unresolved rearrangement in primary metabolism. We have successfully reconstituted this reaction in a cell-free system. The E. coli thiC gene product and an additional unidentified E. coli protein are required for the reaction. In addition, SAM and nicotinamide cofactors are required for full activity. Labeling studies to determine the origin of most of the atoms in the pyrimidine are described. Based on these studies, a new mechanism for HMP formation is proposed.

authors

• Begley, Tadhg

published proceedings

• Org Biomol Chem

author list (cited authors)

• Lawhorn, B. G., Mehl, R. A., & Begley, T. P.

citation count

• 61

complete list of authors

• Lawhorn, Brian G||Mehl, Ryan A||Begley, Tadhg P

publication date

• September 2004

publisher

• Royal Society of Chemistry (RSC)  Publisher

published in

• Organic and Biomolecular Chemistry  Journal

keywords

• Cell-Free System
• Mass Spectrometry
• Molecular Conformation
• Pyrimidines
• Ribonucleotides
• Saccharomyces Cerevisiae
• Thiamine
• Time Factors

Digital Object Identifier (DOI)

• 10.1039/B405429F

start page

• 2538

end page

• 2546

volume

• 2

issue

• 17

URL

• http%3A%2F%2Fdx.doi.org%2F10.1039%2Fb405429f