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@ARTICLE{Alvarez:872761,
      author       = {Alvarez, Clarisa E. and Bovdilova, Anastasiia and Höppner,
                      Astrid and Wolff, Christian-Claus and Saigo, Mariana and
                      Trajtenberg, Felipe and Zhang, Tao and Buschiazzo, Alejandro
                      and Nagel-Steger, Luitgard and Drincovich, Maria F. and
                      Lercher, Martin J. and Maurino, Veronica G.},
      title        = {{M}olecular adaptations of {NADP}-malic enzyme for its
                      function in {C}4 photosynthesis in grasses},
      journal      = {Nature plants},
      volume       = {5},
      number       = {7},
      issn         = {2055-0278},
      address      = {London},
      publisher    = {Nature Publ. Group},
      reportid     = {FZJ-2020-00239},
      pages        = {755 - 765},
      year         = {2019},
      abstract     = {In C4 grasses of agronomical interest, malate shuttled into
                      the bundle sheath cells is decarboxylated mainly by
                      nicotinamide adenine dinucleotide phosphate (NADP)-malic
                      enzyme (C4-NADP-ME). The activity of C4-NADP-ME was
                      optimized by natural selection to efficiently deliver CO2 to
                      Rubisco. During its evolution from a plastidic
                      non-photosynthetic NADP-ME, C4-NADP-ME acquired increased
                      catalytic efficiency, tetrameric structure and pH-dependent
                      inhibition by its substrate malate. Here, we identified
                      specific amino acids important for these C4 adaptions based
                      on strict differential conservation of amino acids, combined
                      with solving the crystal structures of maize and sorghum
                      C4-NADP-ME. Site-directed mutagenesis and struc-tural
                      analyses show that Q503, L544 and E339 are involved in
                      catalytic efficiency; E339 confers pH-dependent regulation
                      by malate, F140 is critical for the stabilization of the
                      oligomeric structure and the N-terminal region is involved
                      in tetramerization. Together, the identified molecular
                      adaptations form the basis for the efficient catalysis and
                      regulation of one of the central biochemical steps in C4
                      metabolism},
      cin          = {ICS-6},
      ddc          = {580},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31235877},
      UT           = {WOS:000474454600022},
      doi          = {10.1038/s41477-019-0451-7},
      url          = {https://juser.fz-juelich.de/record/872761},
}