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- W3090877436 endingPage "1303" @default.
- W3090877436 startingPage "1303" @default.
- W3090877436 abstract "Although the nitrate assimilation into amino acids in photosynthetic leaf tissues is active under the light, the studies during 1950s and 1970s in the dark nitrate assimilation provided fragmental and variable activities, and the mechanism of reductant supply to nitrate assimilation in darkness remained unclear. 15N tracing experiments unraveled the assimilatory mechanism of nitrogen from nitrate into amino acids in the light and in darkness by the reactions of nitrate and nitrite reductases, glutamine synthetase, glutamate synthase, aspartate aminotransferase, and asparagine synthetase. Nitrogen assimilation in illuminated leaves and non-photosynthetic roots occurs either in the redundant way or in the specific manner regarding the isoforms of nitrogen assimilatory enzymes in their cellular compartments. The electron supplying systems necessary to the enzymatic reactions share in part a similar electron donor system at the expense of carbohydrates in both leaves and roots, but also distinct reducing systems regarding the reactions of Fd-nitrite reductase and Fd-glutamate synthase in the photosynthetic and non-photosynthetic organs." @default.
- W3090877436 created "2020-10-08" @default.
- W3090877436 creator A5015651263 @default.
- W3090877436 creator A5080302805 @default.
- W3090877436 date "2020-10-02" @default.
- W3090877436 modified "2023-09-30" @default.
- W3090877436 title "Light-Independent Nitrogen Assimilation in Plant Leaves: Nitrate Incorporation into Glutamine, Glutamate, Aspartate, and Asparagine Traced by 15N" @default.
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- W3090877436 doi "https://doi.org/10.3390/plants9101303" @default.
- W3090877436 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7600499" @default.
- W3090877436 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33023108" @default.
- W3090877436 hasPublicationYear "2020" @default.