Identification of FAH Domain-containing Protein 1 (FAHD1) as Oxaloacetate Decarboxylase |
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| Authors: | Haymo Pircher Susanne von Grafenstein Thomas Diener Christina Metzger Eva Albertini Andrea Taferner Hermann Unterluggauer Christian Kramer Klaus R Liedl Pidder Jansen-Dürr |
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| Institution: | From the ‡Institute for Biomedical Aging Research and Center for Molecular Biosciences Innsbruck (CMBI), Universität Innsbruck, Rennweg 10, 6020 Innsbruck and ;the §Institute for General, Inorganic and Theoretical Chemistry and Center for Molecular Biosciences Innsbruck, Universität Innsbruck, Innrain 80-82, 6020 Innsbruck, Austria |
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| 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. |
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| Keywords: | Computer Modeling Decarboxylase Energy Metabolism Mitochondria Pyruvate FAH Domain FAHD1 Oxaloacetate Decarboxylase |
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