Structural highlights
Function
[FAHD1_MOUSE] Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro (By similarity). Also has oxaloacetate decarboxylase activity (PubMed:25575590).[UniProtKB:Q6P587][1]
Publication Abstract from PubMed
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 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.
Structural and Functional Comparison of Fumarylacetoacetate Domain Containing Protein 1 (FAHD1) in Human and Mouse.,Weiss AKH, Naschberger A, Cappuccio E, Metzger C, Mottes L, Holzknecht M, von Velsen J, Bowler MW, Rupp B, Jansen-Durr P Biosci Rep. 2020 Feb 18. pii: 222164. doi: 10.1042/BSR20194431. PMID:32068790[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pircher H, von Grafenstein S, Diener T, Metzger C, Albertini E, Taferner A, Unterluggauer H, Kramer C, Liedl KR, Jansen-Durr P. Identification of FAH domain-containing protein 1 (FAHD1) as oxaloacetate decarboxylase. J Biol Chem. 2015 Mar 13;290(11):6755-62. doi: 10.1074/jbc.M114.609305. Epub 2015, Jan 9. PMID:25575590 doi:http://dx.doi.org/10.1074/jbc.M114.609305
- ↑ Weiss AKH, Naschberger A, Cappuccio E, Metzger C, Mottes L, Holzknecht M, von Velsen J, Bowler MW, Rupp B, Jansen-Durr P. Structural and Functional Comparison of Fumarylacetoacetate Domain Containing Protein 1 (FAHD1) in Human and Mouse. Biosci Rep. 2020 Feb 18. pii: 222164. doi: 10.1042/BSR20194431. PMID:32068790 doi:http://dx.doi.org/10.1042/BSR20194431
