ArticleThe Journal of biological chemistry2011
Mammalian ACSF3 protein is a malonyl-CoA synthetase that supplies the chain extender units for mitochondrial fatty acid synthesis.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 1 of them a synthesis that pooled it.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
49 citing papers in PubMed, 1 synthesis or guideline pooled it, 74 citations in OpenAlex.
- Pooled it
- Irritable Bowel Disease: Think Malonic and Methylmalonic Aciduria (CMAMMA)!JIMD reports · 2026Article
- Revealing the Shared Genetic Basis of Thermal Adaptation and Abdominal Adiposity in Wenchang Chicken Using Whole-Genome Structural Variation Analysis.Animals : an open access journal from MDPI · 2026Article
- Cells Engage Endogenous Malonate Synthesis to Drive Mitochondrial Metabolism.bioRxiv : the preprint server for biology · 2026Article
- A unified ACSF3-mtFAS model linking mitochondrial energy metabolism to human anthropometric evolution.Cell genomics · 2026Article
- Generation of a novel Dysferlin microdeletion knock-in mouse model mimicking muscular dystrophy-like pathology.Scientific reports · 2026Article
- Malonyl-CoA Decarboxylase: A Spotlight on Brain Aspects.Brain sciences · 2026Review
- Alternative malonyl-CoA pathways for microbial production of diverse products.Applied microbiology and biotechnology · 2026Review
- A Deep Clinical and Biochemical Characterization of a Patient With Combined Malonic and Methylmalonic Aciduria (CMAMMA).JIMD reports · 2025Article
- DCMS analysis revealed differential selection signatures in the transboundary Sahiwal cattle for major economic traits.Scientific reports · 2025Article
- The emerging role of dysregulated propionate metabolism and methylmalonic acid in metabolic disease, aging, and cancer.Cell metabolism · 2025Review
- Airway MMP-12 and DNA methylation in COPD: an integrative approach.Respiratory research · 2025Article
- Chromatin lysine acylation: On the path to chromatin homeostasis and genome integrity.Cancer science · 2024Review
- Identification of genomic-wide genetic links between cutaneous melanoma and obesity-related physical traits via cFDR.Genes & genomics · 2023Article
- Combined Malonic and Methylmalonic Aciduria Diagnosed by Recurrent and Severe Infections Mimicking a Primary Immunodeficiency Disease: A Case Report.Journal of Korean medical science · 2023Article
- Review
- Article
- ZBTB11 dysfunction: spectrum of brain abnormalities, biochemical signature and cellular consequences.Brain : a journal of neurology · 2022Article
- Effects of physical exercise on muscle metabolism and meat quality characteristics of Mongolian sheep.Food science & nutrition · 2022Article
- Novel potential metabolic biomarker panel for early detection of severe COVID-19 using full-spectrum metabolome and whole-transcriptome analyses.Signal transduction and targeted therapy · 2022Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The objective of this study was to identify a source of intramitochondrial malonyl-CoA that could be used for de novo fatty acid synthesis in mammalian mitochondria. Because mammalian mitochondria lack an acetyl-CoA carboxylase capable of generating malonyl-CoA inside mitochondria, the possibility that malonate could act as a precursor was investigated. Although malonyl-CoA synthetases have not been identified previously in animals, interrogation of animal protein sequence databases identified candidates that exhibited sequence similarity to known prokaryotic forms. The human candidate protein ACSF3, which has a predicted N-terminal mitochondrial targeting sequence, was cloned, expressed, and characterized as a 65-kDa acyl-CoA synthetase with extremely high specificity for malonate and methylmalonate. An arginine residue implicated in malonate binding by prokaryotic malonyl-CoA synthetases was found to be positionally conserved in animal ACSF3 enzymes and essential for activity. Subcellular fractionation experiments with HEK293T cells confirmed that human ACSF3 is located exclusively in mitochondria, and RNA interference experiments verified that this enzyme is responsible for most, if not all, of the malonyl-CoA synthetase activity in the mitochondria of these cells. In conclusion, unlike fungi, which have an intramitochondrial acetyl-CoA carboxylase, animals require an alternative source of mitochondrial malonyl-CoA; the mitochondrial ACSF3 enzyme is capable of filling this role by utilizing free malonic acid as substrate.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.