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Dual activity of quinolinate synthase: triose phosphate isomerase and dehydration activities play together to form quinolinate.
- Source :
-
Biochemistry [Biochemistry] 2015 Oct 27; Vol. 54 (42), pp. 6443-6. Date of Electronic Publication: 2015 Oct 16. - Publication Year :
- 2015
-
Abstract
- 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.
- Subjects :
- Aspartic Acid analogs & derivatives
Aspartic Acid metabolism
Bacterial Proteins chemistry
Bacterial Proteins metabolism
Dihydroxyacetone Phosphate metabolism
Metabolic Networks and Pathways
Models, Chemical
NAD biosynthesis
Quinolinic Acid metabolism
Thermotoga maritima enzymology
Multienzyme Complexes chemistry
Multienzyme Complexes metabolism
Triose-Phosphate Isomerase chemistry
Triose-Phosphate Isomerase metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1520-4995
- Volume :
- 54
- Issue :
- 42
- Database :
- MEDLINE
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 26455817
- Full Text :
- https://doi.org/10.1021/acs.biochem.5b00991