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Early Steps in the Biosynthesis of NAD in Arabidopsis Start with Aspartate and Occur in the Plastid1

Tipo de material: TextoTextoSeries ; Plant Physiology, 141, p.851-857, 2006Trabajos contenidos:
  • Katoh, A
  • Uenohara, K
  • Akita, M
  • Hashimoto, T
Recursos en línea: Resumen: NADis a ubiquitous coenzyme involved in oxidation-reduction reactions and is synthesized by way of quinolinate. Animals and some bacteria synthesize quinolinate from tryptophan, whereas other bacteria synthesize quinolinate from aspartate (Asp)using L-Asp oxidase and quinolinate synthase. We show here that Arabidopsis (Arabidopsis thaliana)uses the Asp-to-quinolinate pathway. The Arabidopsis L-Asp oxidase or quinolinate synthase gene complemented the Escherichia coli mutant defective in the corresponding gene, and T-DNA-based disruption of either of these genes, as well as of the gene coding for the enzyme quinolinate phosphoribosyltransferase, was embryo lethal. An analysis of functional green fluorescent protein-fused constructs and in vitro assays of uptake into isolated chloroplasts demonstrated that these three enzymes are located in the plastid.
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NADis a ubiquitous coenzyme involved in oxidation-reduction reactions and is synthesized by way of quinolinate. Animals and some bacteria synthesize quinolinate from tryptophan, whereas other bacteria synthesize quinolinate from aspartate (Asp)using L-Asp oxidase and quinolinate synthase. We show here that Arabidopsis (Arabidopsis thaliana)uses the Asp-to-quinolinate pathway. The Arabidopsis L-Asp oxidase or quinolinate synthase gene complemented the Escherichia coli mutant defective in the corresponding gene, and T-DNA-based disruption of either of these genes, as well as of the gene coding for the enzyme quinolinate phosphoribosyltransferase, was embryo lethal. An analysis of functional green fluorescent protein-fused constructs and in vitro assays of uptake into isolated chloroplasts demonstrated that these three enzymes are located in the plastid.

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