The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes: multifunctional enzymes from microbes to mitochondria

Biochemical Society Transactions
Alexander K H WeissPidder Jansen-Dürr

Abstract

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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Citations

Oct 24, 2018·The Biochemical Journal·Alexander K H WeissPidder Jansen-Dürr
Feb 2, 2019·Molecular Microbiology·Andreas ReinhardtPeter Schönheit
Feb 19, 2020·Bioscience Reports·Alexander K H WeissPidder Jansen-Dürr
Jul 19, 2020·International Journal of Molecular Sciences·Neha SarodayaSuresh Ramakrishna
Jun 24, 2020·Mechanisms of Ageing and Development·Alexander K H WeissPidder Jansen-Dürr
Apr 4, 2021·International Journal of Molecular Sciences·Davide GernaIlse Kranner
Apr 6, 2021·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Audrey-Ann DumontMannix Auger-Messier
Aug 28, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Alexander K H WeissHubert Gstach

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