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@ARTICLE{Myllykoski:633005,
      author       = {Myllykoski, Matti and Lundekvam, Malin and Osberg, Camilla
                      and Nilsen, Solveig Siqveland and Arnesen, Thomas},
      title        = {{T}he molecular basis for acetylhistidine synthesis by
                      {H}is{AT}/{NAT}16},
      journal      = {Nature Communications},
      volume       = {16},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {PUBDB-2025-02331},
      pages        = {5960},
      year         = {2025},
      abstract     = {Acetylhistidine has been detected in human blood, but its
                      origin and function are not known. It is formed when the
                      acetyl group of acetyl-CoA is transferred to the α-amino
                      group of histidine. Here we identify the intracellular NAT16
                      as the human histidine acetyltransferase (HisAT) responsible
                      for histidine acetylation in vitro and in vivo. A NAT16
                      variant (p.Phe63Ser) present in over $5\%$ of the population
                      was previously found to correlate with reduced plasma levels
                      of acetylhistidine and increased risk of kidney disease. Our
                      biochemical analysis of HisAT/NAT16 Phe63Ser shows reduced
                      affinity for Histidine supporting a model where this variant
                      has less acetylhistidine catalysis leading to lower blood
                      level of acetylhistidine. We find that HisAT adopts a
                      double-GNAT (Gcn5-related N-Acetyltransferase) fold where
                      the N-terminal domain binds acetyl-CoA and with distinct
                      active site conformation allowing the binding of histidine
                      in between the two domains. We detect similar structures
                      from across living organisms and find that the HisAT
                      structure is conserved in several archaeal and bacterial
                      species. In sum, NAT16 is the human histidine
                      acetyltransferase utilizing a rare double-GNAT structure to
                      steer plasma acetylhistidine levels with potential impact
                      for kidney function.},
      cin          = {EMBL-User},
      ddc          = {500},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / NterAct - Discovery and
                      functional significance of post-translational N-terminal
                      acetylation (772039) / Q-Room - Q-Room – Quintetto’s
                      Holographic Telepresence Room (673617) / FS-Proposal:
                      BAG-20190768 EC (BAG-20190768-EC) / FS-Proposal:
                      BAG-20211049 EC (BAG-20211049-EC)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(EU-Grant)772039 /
                      G:(EU-Grant)673617 / G:(DE-H253)BAG-20190768-EC /
                      G:(DE-H253)BAG-20211049-EC},
      experiment   = {EXP:(DE-H253)P-P11-20150101 / EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40595645},
      doi          = {10.1038/s41467-025-61145-x},
      url          = {https://bib-pubdb1.desy.de/record/633005},
}