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Updated: Dec 28, 2025

Extraction and Purification of FAHD1 Protein from Swine Kidney and Mouse Liver
Published on: February 18, 2022
Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse
Alexander K H Weiss1,2, Andreas Naschberger3, Elia Cappuccio1,2
1University of Innsbruck, Research Institute for Biomedical Aging Research, Rennweg 10, Innsbruck A-6020, Austria.
Abstract:
FAH domain containing protein 1 (FAHD1) is a mammalian mitochondrial protein, displaying bifunctionality as acylpyruvate hydrolase (ApH) and oxaloacetate decarboxylase (ODx) activity. We report the crystal structure of mouse FAHD1 and structural mapping of the active site of mouse FAHD1. Despite high structural similarity with human FAHD1, a rabbit monoclonal antibody (RabMab) could be produced that is able to recognize mouse FAHD1, but not the human form, whereas a polyclonal antibody recognized both proteins. Epitope mapping in combination with our deposited crystal structures revealed that the epitope overlaps with a reported SIRT3 deacetylation site in mouse FAHD1.
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