2. Academic Validation
  3. Identification of FAH domain-containing protein 1 (FAHD1) as oxaloacetate decarboxylase

Identification of FAH domain-containing protein 1 (FAHD1) as oxaloacetate decarboxylase

  • J Biol Chem. 2015 Mar 13;290(11):6755-62. doi: 10.1074/jbc.M114.609305.
Haymo Pircher 1,  Susanne von Grafenstein 2,  Thomas Diener 1,  Christina Metzger 1,  Eva Albertini 1,  Andrea Taferner 1,  Hermann Unterluggauer 1,  Christian Kramer 2,  Klaus R Liedl 2,  Pidder Jansen-Dürr 3
Affiliations

Affiliations

  • 1 From the Institute for Biomedical Aging Research and Center for Molecular Biosciences Innsbruck (CMBI), Universität Innsbruck, Rennweg 10, 6020 Innsbruck and.
  • 2 the Institute for General, Inorganic and Theoretical Chemistry and Center for Molecular Biosciences Innsbruck, Universität Innsbruck, Innrain 80-82, 6020 Innsbruck, Austria.
  • 3 From the Institute for Biomedical Aging Research and Center for Molecular Biosciences Innsbruck (CMBI), Universität Innsbruck, Rennweg 10, 6020 Innsbruck and pidder.jansen-duerr@uibk.ac.at.
PMID: 25575590 DOI: 10.1074/jbc.M114.609305
Abstract

Fumarylacetoacetate hydrolase (FAH) domain-containing proteins occur in both prokaryotes and eukaryotes, where they carry out diverse enzymatic reactions, probably related to structural differences in their respective FAH domains; however, the precise relationship between structure of the FAH domain and the associated Enzyme function remains elusive. In mammals, three FAH domain-containing proteins, FAHD1, FAHD2A, and FAHD2B, are known; however, their enzymatic function, if any, remains to be demonstrated. In bacteria, oxaloacetate is subject to enzymatic decarboxylation; however, oxaloacetate decarboxylases (ODx) were so far not identified in eukaryotes. Based on molecular modeling and subsequent biochemical investigations, we identified FAHD1 as a eukaryotic ODx Enzyme. The results presented here indicate that dedicated oxaloacetate decarboxylases exist in eukaryotes.

Keywords

Computer Modeling; Decarboxylase; Energy Metabolism; FAH Domain; FAHD1; Mitochondria; Oxaloacetate Decarboxylase; Pyruvate.

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