title: Identification of FAH domain-containing protein 1 (FAHD1) as oxaloacetate decarboxylase.
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.
authors.affiliation: From the Institute for Biomedical Aging Research and Center for Molecular Biosciences Innsbruck (CMBI), Universität Innsbruck, Rennweg 10, 6020 Innsbruck and.
authors.forename: Haymo
authors.initials: H
authors.lastname: Pircher
authors.affiliation: the Institute for General, Inorganic and Theoretical Chemistry and Center for Molecular Biosciences Innsbruck, Universität Innsbruck, Innrain 80-82, 6020 Innsbruck, Austria.
authors.forename: Susanne
authors.initials: S
authors.lastname: von Grafenstein
authors.affiliation: From the Institute for Biomedical Aging Research and Center for Molecular Biosciences Innsbruck (CMBI), Universität Innsbruck, Rennweg 10, 6020 Innsbruck and.
authors.forename: Thomas
authors.initials: T
authors.lastname: Diener
authors.affiliation: From the Institute for Biomedical Aging Research and Center for Molecular Biosciences Innsbruck (CMBI), Universität Innsbruck, Rennweg 10, 6020 Innsbruck and.
authors.forename: Christina
authors.initials: C
authors.lastname: Metzger
authors.affiliation: From the Institute for Biomedical Aging Research and Center for Molecular Biosciences Innsbruck (CMBI), Universität Innsbruck, Rennweg 10, 6020 Innsbruck and.
authors.forename: Eva
authors.initials: E
authors.lastname: Albertini
authors.affiliation: From the Institute for Biomedical Aging Research and Center for Molecular Biosciences Innsbruck (CMBI), Universität Innsbruck, Rennweg 10, 6020 Innsbruck and.
authors.forename: Andrea
authors.initials: A
authors.lastname: Taferner
authors.affiliation: From the Institute for Biomedical Aging Research and Center for Molecular Biosciences Innsbruck (CMBI), Universität Innsbruck, Rennweg 10, 6020 Innsbruck and.
authors.forename: Hermann
authors.initials: H
authors.lastname: Unterluggauer
authors.affiliation: the Institute for General, Inorganic and Theoretical Chemistry and Center for Molecular Biosciences Innsbruck, Universität Innsbruck, Innrain 80-82, 6020 Innsbruck, Austria.
authors.forename: Christian
authors.initials: C
authors.lastname: Kramer
authors.affiliation: the Institute for General, Inorganic and Theoretical Chemistry and Center for Molecular Biosciences Innsbruck, Universität Innsbruck, Innrain 80-82, 6020 Innsbruck, Austria.
authors.forename: Klaus R
authors.initials: KR
authors.lastname: Liedl
authors.affiliation: 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.
authors.forename: Pidder
authors.initials: P
authors.lastname: Jansen-Dürr
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002262:Carboxy-Lyases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D018360:Crystallography, X-Ray; D004734:Energy Metabolism; D005260:Female; D005786:Gene Expression Regulation; D006801:Humans; D006867:Hydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D008810:Mice, Inbred C57BL; D018345:Mice, Knockout; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D019289:Pyruvic Acid / Q000378:metabolism; D016415:Sequence Alignment
chemical_list: D019289:Pyruvic Acid; D006867:Hydrolases; C020156:fumarylacetoacetase; D002262:Carboxy-Lyases; C021916:oxaloacetate decarboxylase
keywords: Computer Modeling; Decarboxylase; Energy Metabolism; FAH Domain; FAHD1; Mitochondria; Oxaloacetate Decarboxylase; Pyruvate