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@ARTICLE{Sorci:642756,
      author       = {Sorci, Leonardo and Cianci, Michele and Fortunato, Carlo
                      and Gasparrini, Massimiliano and Raffaelli, Nadia},
      title        = {{A}rabidopsis thaliana nicotinate mononucleotide
                      adenylyltransferase: unveiling the molecular determinants
                      and evolutionary origin of nicotinic acid mononucleotide
                      recognition},
      journal      = {International journal of biological macromolecules},
      volume       = {331},
      issn         = {0141-8130},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PUBDB-2025-05605},
      pages        = {148370},
      year         = {2025},
      abstract     = {The pyridine nucleotide adenylyltransferase (PNAT) enzyme
                      family is crucial for the synthesis of NAD, a pivotal
                      cofactor in cellular metabolism. PNATs catalyze the transfer
                      of an AMP moiety from ATP to either nicotinate
                      mononucleotide (NaMN), forming nicotinate adenine
                      dinucleotide, the immediate precursor to NAD, or to
                      nicotinamide mononucleotide (NMN), directly yielding NAD.
                      This enzyme family exhibits modular substrate specificity,
                      comprising strictly NaMN-selective (bacterial NadD),
                      NMN-selective (bacterial NadR and NadM), or bifunctional
                      (mammalian PNAT and archaeal NadM). While Arabidopsis
                      thaliana PNAT has been ambiguously annotated as
                      bifunctional, our detailed kinetic analysis definitively
                      establishes its strict NaMN preference, analogous to
                      bacterial NadD. By integrating bioinformatics and X-ray
                      crystallography of the enzyme in its apo and NaMN-bound
                      forms, we elucidate the structural basis for NaMN
                      selectivity, which differs from bacterial NadD. In plants, a
                      positively charged residue (Arg106 in A. thaliana NaMN
                      adenylyltransferase, NaMNAT) ensures NaMN specificity by
                      counteracting the negative charge of the nicotinate moiety.
                      Site-directed mutagenesis confirms the essential role of
                      Arg106 in NaMN recognition and catalysis. Our findings
                      support the extension of this functional assignment across
                      Archaeoplastida. Furthermore, phylogenetic analysis reveals
                      the complex and intertwined evolution of bacterial and plant
                      NaMNATs, shaped by ancient gene transfers from
                      cyanobacteria.},
      cin          = {EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1016/j.ijbiomac.2025.148370},
      url          = {https://bib-pubdb1.desy.de/record/642756},
}