Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse | Zendy

Alexander K. H. Weiss | Zendy; Andreas Naschberger | Zendy; Elia Cappuccio | Zendy; Christina Metzger | Zendy; Lorenza Mottes | Zendy; Max Holzknecht | Zendy; Jill von Velsen | Zendy; Matthew W. Bowler | Zendy; Bernhard Rupp | Zendy; Pidder JansenDürr | Zendy

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Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse

Author(s) -

Alexander K. H. Weiss,

Andreas Naschberger,

Elia Cappuccio,

Christina Metzger,

Lorenza Mottes,

Max Holzknecht,

Jill von Velsen,

Matthew W. Bowler,

Bernhard Rupp,

Pidder JansenDürr

Publication year - 2020

Publication title -

bioscience reports

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.938

H-Index - 77

eISSN - 1573-4935

pISSN - 0144-8463

DOI - 10.1042/bsr20194431

Subject(s) - epitope , hydrolase , biochemistry , polyclonal antibodies , epitope mapping , chemistry , monoclonal antibody , microbiology and biotechnology , acetylation , structural similarity , sirt3 , biology , antibody , enzyme , genetics , gene , sirtuin

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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