NAD biosynthesis: identification of the tryptophan to quinolinate pathway in bacteria. Academic Article

abstract

• Previous studies have demonstrated two different biosynthetic pathways to quinolinate, the universal de novo precursor to the pyridine ring of NAD. In prokaryotes, quinolinate is formed from aspartate and dihydroxyacetone phosphate; in eukaryotes, it is formed from tryptophan. It has been generally believed that the tryptophan to quinolinic acid biosynthetic pathway is unique to eukaryotes; however, this paper describes the use of comparative genome analysis to identify likely candidates for all five genes involved in the tryptophan to quinolinic acid pathway in several bacteria. Representative examples of each of these genes were overexpressed, and the predicted functions are confirmed in each case using unambiguous biochemical assays.

authors

• Begley, Tadhg

published proceedings

• Chem Biol

author list (cited authors)

• Kurnasov, O., Goral, V., Colabroy, K., Gerdes, S., Anantha, S., Osterman, A., & Begley, T. P.

citation count

• 163

complete list of authors

• Kurnasov, Oleg||Goral, Vasiliy||Colabroy, Keri||Gerdes, Svetlana||Anantha, Shubha||Osterman, Andrei||Begley, Tadhg P

publication date

• January 2003

publisher

• Elsevier  Publisher

published in

• Chemistry and Biology  Journal

keywords

• Arylformamidase
• Bacteria
• Chromosomes, Bacterial
• Gene Expression Regulation, Bacterial
• Genes, Bacterial
• Genetic Complementation Test
• Hydrolases
• Kinetics
• Molecular Sequence Data
• NAD
• Oxidoreductases
• Quinolinic Acid
• Tryptophan

PubMed Central ID

• 14700627

Digital Object Identifier (DOI)

• 10.1016/j.chembiol.2003.11.011

start page

• 1195

end page

• 1204

volume

• 10

issue

• 12

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2Fj.chembiol.2003.11.011