A glycine to aspartic acid change in the MoCo domain of nitrate reductase reduces both activity and phosphorylation levels in Arabidopsis.

@article{Labrie1994AGT,
  title={A glycine to aspartic acid change in the MoCo domain of nitrate reductase reduces both activity and phosphorylation levels in Arabidopsis.},
  author={S T Labrie and Nigel M. Crawford},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 20},
  pages={14497-501}
}
Nitrate reductase (NR), the first enzyme in the nitrate assimilation pathway, is regulated post-transcriptionally in response to light and CO2. In spinach, it has been shown that phosphorylation is one mechanism that mediates this regulation. In this paper, the phosphorylation of NR in Arabidopsis is described in both wild-type and NR- mutant plants. A 110-kDa protein radiolabeled in vivo with 32PO4 was immunoprecipitated with anti-NR antibody from extracts of wild-type plants but not of mutant… CONTINUE READING

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NITRATE REDUCTASE STRUCTURE, FUNCTION AND REGULATION: Bridging the Gap between Biochemistry and Physiology.

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