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- W2788114927 endingPage "309" @default.
- W2788114927 startingPage "295" @default.
- W2788114927 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." @default.
- W2788114927 created "2018-03-06" @default.
- W2788114927 creator A5000379524 @default.
- W2788114927 creator A5024671557 @default.
- W2788114927 creator A5028405436 @default.
- W2788114927 creator A5037775787 @default.
- W2788114927 creator A5076215352 @default.
- W2788114927 date "2018-02-27" @default.
- W2788114927 modified "2023-10-18" @default.
- W2788114927 title "The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes: multifunctional enzymes from microbes to mitochondria" @default.
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