ArticleThe Biochemical journal2018
Structural basis for the bi-functionality of human oxaloacetate decarboxylase FAHD1.
Article in The Biochemical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Synergistic Roles of FAHD-1 and PYC-1 in Mitochondrial Function, Behavior, and Longevity in C. elegans.Advanced biology · 2026Article
- Catalytic activity of FAHD1 correlates with nuclear morphology and proteomic states in human osteosarcoma cells.Scientific reports · 2025Article
- FAHD1 and mitochondrial metabolism: a decade of pioneering discoveries.The FEBS journal · 2025Review
- FAHD1 prevents neuronal ferroptosis by modulating R-loop and the cGAS-STING pathway.Open medicine (Warsaw, Poland) · 2025Article
- Structural and Functional Characterization of a Novel Class A Flavin Monooxygenase fromBiochemistry · 2024Article
- Mitochondrial enzyme FAHD1 reduces ROS in osteosarcoma.Scientific reports · 2024Article
- A universal metabolite repair enzyme removes a strong inhibitor of the TCA cycle.Nature communications · 2024Article
- Inhibitors of Fumarylacetoacetate Hydrolase Domain Containing Protein 1 (FAHD1).Molecules (Basel, Switzerland) · 2021Article
- AtFAHD1a: A New Player Influencing Seed Longevity and Dormancy in Arabidopsis?International journal of molecular sciences · 2021Article
- Erythropoietin Regulates Transcription and YY1 Dynamics in a Pre-established Chromatin Architecture.iScience · 2020Article
- Regulation of cellular senescence by eukaryotic members of the FAH superfamily - A role in calcium homeostasis?Mechanisms of ageing and development · 2020Review
- Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse.Bioscience reports · 2020Article
- Decanoic Acid and Not Octanoic Acid Stimulates Fatty Acid Synthesis in U87MG Glioblastoma Cells: A Metabolomics Study.Frontiers in neuroscience · 2020Article
- Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins.Journal of visualized experiments : JoVE · 2019Article
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
Abstract
Whereas enzymes in the fumarylacetoacetate hydrolase (FAH) superfamily catalyze several distinct chemical reactions, the structural basis for their multi-functionality remains elusive. As a well-studied example, human FAH domain-containing protein 1 (FAHD1) is a mitochondrial protein displaying both acylpyruvate hydrolase (ApH) and oxaloacetate decarboxylase (ODx) activity. As mitochondrial ODx, FAHD1 acts antagonistically to pyruvate carboxylase, a key metabolic enzyme. Despite its importance for mitochondrial function, very little is known about the catalytic mechanisms underlying FAHD1 enzymatic activities, and the architecture of its ligated active site is currently ill defined. We present crystallographic data of human FAHD1 that provide new insights into the structure of the catalytic center at high resolution, featuring a flexible 'lid'-like helical region which folds into a helical structure upon binding of the ODx inhibitor oxalate. The oxalate-driven structural transition results in the generation of a potential catalytic triad consisting of E33, H30 and an associated water molecule.
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