FAHD1 is a 27 kDa mitochondrial protein conserved across mammals. It catalyzes two key reactions:
Oxaloacetate decarboxylation: Converts oxaloacetate (OAA) to pyruvate, modulating TCA cycle flux and mitochondrial membrane potential .
Acylpyruvate hydrolysis: Breaks down acetylpyruvate and fumarylpyruvate, preventing toxic metabolite accumulation .
Critical residues for catalysis include Asp-102 and Arg-106, with Mg²⁺ as a cofactor . Structural studies reveal species-specific epitopes, such as residues 174–224 in human FAHD1 and V77–I88 in mouse FAHD1, which influence antibody cross-reactivity .
FAHD1 antibodies enable precise detection and functional analysis of the protein in diverse experimental settings:
Rabbit monoclonal antibodies (e.g., RabMab 27-1) recognize mouse FAHD1 but not human, due to differences in residues V77–I88. Polyclonal antibodies (e.g., anti-hFAHD1) cross-react with both species . This specificity is critical for comparative studies.
The epitope LLGKRGEAI (mouse FAHD1) overlaps with a SIRT3 deacetylation site (K83), suggesting acetylation may mask epitope accessibility in certain tissues (e.g., pancreas) .
FAHD1 overexpression reduces reactive oxygen species (ROS) in osteosarcoma cells by modulating OAA levels and TCA cycle flux. Catalytically enhanced variants (e.g., T192S) correlate with longevity and cancer resistance in animal models .
Target Background: A probable acylpyruvase that exhibits copper-binding affinity in vitro.
KEGG: ath:AT4G15940
UniGene: At.19940