Identification of domains involved in tetramerization and malate inhibition of maize C4-NADP-malic enzyme.

@article{Detarsio2007IdentificationOD,
  title={Identification of domains involved in tetramerization and malate inhibition of maize C4-NADP-malic enzyme.},
  author={Enrique Detarsio and Clarisa E. Alvarez and Mariana Saigo and Carlos Santiago Andreo and Mar{\'i}a F Drincovich},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 9},
  pages={
          6053-60
        }
}
C(4) photosynthetic NADP-malic enzyme (ME) has evolved from non-C(4) isoforms and gained unique kinetic and structural properties during this process. To identify the domains responsible for the structural and kinetic differences between maize C(4) and non-C(4)-NADP-ME several chimeras between these isoforms were constructed and analyzed. By using this approach, we found that the region flanked by amino acid residues 102 and 247 is critical for the tetrameric state of C(4)-NADP-ME. In this way… CONTINUE READING

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