%0 Journal Article
%A Reichmann, Debora
%A CouteĢ, Yohann
%A Ollagnier de Choudens, Sandrine
%D 2015
%T Dual Activity of Quinolinate Synthase: Triose Phosphate
Isomerase and Dehydration Activities Play Together To Form Quinolinate
%U https://acs.figshare.com/articles/journal_contribution/Dual_Activity_of_Quinolinate_Synthase_Triose_Phosphate_Isomerase_and_Dehydration_Activities_Play_Together_To_Form_Quinolinate/2117341
%R 10.1021/acs.biochem.5b00991.s001
%2 https://acs.figshare.com/ndownloader/files/3751057
%K Form QuinolinateQuinolinate synthase
%K NadA
%K Triose Phosphate Isomerase
%K IA
%K Dehydration Activities Play
%K condense
%K form QA
%K triose phosphate isomerase activity
%K 4S
%K coenzyme nicotinamide adenine dinucleotide
%K DHAP
%X Quinolinate
synthase (NadA) is an Fe4S4 cluster-containing
dehydrating enzyme involved in the synthesis of quinolinic acid (QA),
the universal precursor of the essential coenzyme nicotinamide adenine
dinucleotide. The reaction catalyzed by NadA is not well understood,
and two mechanisms have been proposed in the literature that differ
in the nature of the molecule (DHAP or G-3P) that condenses with iminoaspartate
(IA) to form QA. In this article, using biochemical approaches, we
demonstrate that DHAP is the triose that condenses with IA to form
QA. The capacity of NadA to use G-3P is due to its previously unknown
triose phosphate isomerase activity.
%I ACS Publications