Prokaryotic and eukaryotic fumarylacetoacetate hydrolase (FAH) superfamily members, sharing conserved regions that form the so-called FAH-domain, catalyze a remarkable variety of reactions. These enzymes are essential in the metabolic pathways to degrade aromatic compounds in prokaryotes and eukaryotes. It appears that prokaryotic FAH superfamily members evolved mainly to allow microbes to generate energy and useful metabolites from complex carbon sources. We review recent findings, indicating that both prokaryotic and eukaryotic members of the FAH superfamily also display oxaloacetate decarboxylase (ODx) activity. The identification of human FAH domain-containing protein 1 as mitochondrial ODx regulating mitochondrial function supports the new concept that, during evolution, eukaryotic FAH superfamily members have acquired important regulatory functions beyond catabolism of complex carbon sources. Molecular studies on the evolution and function of FAH superfamily members are expected to provide new mechanistic insights in their physiological roles.
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April 2018
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A 3D rendering of a Ubiquitin protein molecule. In this issue of Biochemical Society Transactions, Ovaa and Vertegaal discuss the role of ubiquitination and SUMO proteins in conjugation and deconjugation machineries; for details, see pages 423–436.
Review Article|
February 27 2018
The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes: multifunctional enzymes from microbes to mitochondria
Alexander K.H. Weiss;
1Research Institute for Biomedical Aging Research, University of Innsbruck, Rennweg 10, Innsbruck A-6020, Austria
2Center for Molecular Biosciences Innsbruck (CMBI), Innsbruck, Austria
Correspondence: Alexander K.H. Weiss (alexander.weiss@uibk.ac.at)
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Johannes R. Loeffler;
Johannes R. Loeffler
2Center for Molecular Biosciences Innsbruck (CMBI), Innsbruck, Austria
3Institute of General, Inorganic and Theoretical Chemistry, University of Innsbruck, Innrain 82, Innsbruck 6020, Austria
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Klaus R. Liedl;
Klaus R. Liedl
2Center for Molecular Biosciences Innsbruck (CMBI), Innsbruck, Austria
3Institute of General, Inorganic and Theoretical Chemistry, University of Innsbruck, Innrain 82, Innsbruck 6020, Austria
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Hubert Gstach;
Hubert Gstach
4University of Vienna, Austria; Faculty of Chemistry; Department of Organic Chemistry; Währinger Straße 38, A-1090 Vienna
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Pidder Jansen-Dürr
Pidder Jansen-Dürr
1Research Institute for Biomedical Aging Research, University of Innsbruck, Rennweg 10, Innsbruck A-6020, Austria
2Center for Molecular Biosciences Innsbruck (CMBI), Innsbruck, Austria
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Publisher: Portland Press Ltd
Received:
October 31 2017
Revision Received:
December 23 2017
Accepted:
January 02 2018
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2018 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2018
Biochem Soc Trans (2018) 46 (2): 295–309.
Article history
Received:
October 31 2017
Revision Received:
December 23 2017
Accepted:
January 02 2018
Citation
Alexander K.H. Weiss, Johannes R. Loeffler, Klaus R. Liedl, Hubert Gstach, Pidder Jansen-Dürr; The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes: multifunctional enzymes from microbes to mitochondria. Biochem Soc Trans 17 April 2018; 46 (2): 295–309. doi: https://doi.org/10.1042/BST20170518
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