Dual Activity of Quinolinate Synthase: Triose Phosphate
Isomerase and Dehydration Activities Play Together To Form Quinolinate
Debora Reichmann
Yohann CouteĢ
Sandrine Ollagnier de Choudens
10.1021/acs.biochem.5b00991.s001
https://acs.figshare.com/articles/journal_contribution/Dual_Activity_of_Quinolinate_Synthase_Triose_Phosphate_Isomerase_and_Dehydration_Activities_Play_Together_To_Form_Quinolinate/2117341
Quinolinate
synthase (NadA) is an Fe<sub>4</sub>S<sub>4</sub> 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.
2015-10-27 00:00:00
Form QuinolinateQuinolinate synthase
NadA
Triose Phosphate Isomerase
IA
Dehydration Activities Play
condense
form QA
triose phosphate isomerase activity
4S
coenzyme nicotinamide adenine dinucleotide
DHAP