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@ARTICLE{Sonani:602498,
      author       = {Sonani, Ravi R. and Blat, Artur and Dubin, Grzegorz},
      title        = {{C}rystal structures of apo- and {FAD}-bound human
                      peroxisomal acyl-{C}o{A} oxidase provide mechanistic basis
                      explaining clinical observations},
      journal      = {International journal of biological macromolecules},
      volume       = {205},
      issn         = {0141-8130},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PUBDB-2024-00618},
      pages        = {203 - 210},
      year         = {2022},
      abstract     = {Peroxisomal acyl-CoA oxidase 1a (ACOX1a) catalyzes the
                      first and rate-limiting step of fatty acid oxidation, the
                      conversion of acyl-CoAs to 2-trans-enoyl-CoAs. The
                      dysfunction of human ACOX1a (hACOX1a) leads to deterioration
                      of the nervous system manifesting in myeloneuropathy,
                      hypotonia and convulsions. Crystal structures of hACOX1a in
                      apo- and cofactor (FAD)-bound forms were solved at 2.00 and
                      2.09 Å resolution, respectively. hACOX1a exists as a
                      homo-dimer with solvation free energy gain (ΔGo) of −44.7
                      kcal mol−1. Two FAD molecules bind at the interface of
                      protein monomers completing the active sites. The substrate
                      binding cleft of hACOX1a is wider compared to human
                      mitochondrial very-long chain specific acyl-CoA
                      dehydrogenase. Mutations (p.G178C, p.M278V and p.N237S)
                      reported to cause dysfunctionality of hACOX1a are analyzed
                      on its 3D-structure to understand structure-function related
                      perturbations and explain the associated phenotypes.},
      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},
      pubmed       = {pmid:35149097},
      UT           = {WOS:000784246800004},
      doi          = {10.1016/j.ijbiomac.2022.02.008},
      url          = {https://bib-pubdb1.desy.de/record/602498},
}