ArticleNature communications2016
The dynamic organization of fungal acetyl-CoA carboxylase.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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Who cites it
28 citing papers in PubMed.
- Caffeylpyruvate hydrolase from the bioluminescent fungus Neonothopanus gardneri is the key recycling enzyme in the fungal bioluminescence pathway.The FEBS journal · 2026Article
- Optimization of Malonyl Coenzyme A Biosensors in a Reconstituted Cell-Free System for Detecting Acetyl-CoA Carboxylase Activity.ACS synthetic biology · 2025Article
- Structure of the endogenous insect acetyl-coA carboxylase carboxyltransferase domain.The Journal of biological chemistry · 2024Article
- Dataset from a human-in-the-loop approach to identify functionally important protein residues from literature.Scientific data · 2024Article
- Sample optimizations to enable the structure determination of biotin-dependent carboxylases.Methods in enzymology · 2024Article
- Effect of carbon and nitrogen concentrations on lipid accumulation and regulation of acetyl-CoA carboxylase in Papiliotrema laurentii.Antonie van Leeuwenhoek · 2023Article
- Targeting acetyl-CoA carboxylase 1 for cancer therapy.Frontiers in pharmacology · 2023Review
- Plant stress responses compromise mutualisms with Epichloë endophytes.Journal of experimental botany · 2023Article
- Heterobivalent Inhibitors of Acetyl-CoA Carboxylase: Drug Target Residence Time and Time-Dependent Antibacterial Activity.Journal of medicinal chemistry · 2022Article
- Article
- Combining Metabolic Engineering and Multiplexed Screening Methods for 3-Hydroxypropionic Acid Production inFrontiers in bioengineering and biotechnology · 2022Article
- Synthesis of Dolichols inInternational journal of molecular sciences · 2021Article
- Synthetic protein quality control to enhance full-length translation in bacteria.Nature chemical biology · 2021Article
- A Penicillium rubens platform strain for secondary metabolite production.Scientific reports · 2020Article
- Non-Catalytic Subunits Facilitate Quaternary Organization of Plastidic Acetyl-CoA Carboxylase.Plant physiology · 2020Article
- GS-0976 (Firsocostat): an investigational liver-directed acetyl-CoA carboxylase (ACC) inhibitor for the treatment of non-alcoholic steatohepatitis (NASH).Expert opinion on investigational drugs · 2020Review
- A novel multidomain acyl-CoA carboxylase in Saccharopolyspora erythraea provides malonyl-CoA for de novo fatty acid biosynthesis.Scientific reports · 2019Article
- SAXSMoW 2.0: Online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale.Protein science : a publication of the Protein Society · 2019Article
- Constitutive and Chloroplast Targeted Expression of Acetyl-CoA Carboxylase in Oleaginous Microalgae Elevates Fatty Acid Biosynthesis.Marine biotechnology (New York, N.Y.) · 2018Article
- Regulation ofmSphere · 2018Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acetyl-CoA carboxylases (ACCs) catalyse the committed step in fatty-acid biosynthesis: the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. They are important regulatory hubs for metabolic control and relevant drug targets for the treatment of the metabolic syndrome and cancer. Eukaryotic ACCs are single-chain multienzymes characterized by a large, non-catalytic central domain (CD), whose role in ACC regulation remains poorly characterized. Here we report the crystal structure of the yeast ACC CD, revealing a unique four-domain organization. A regulatory loop, which is phosphorylated at the key functional phosphorylation site of fungal ACC, wedges into a crevice between two domains of CD. Combining the yeast CD structure with intermediate and low-resolution data of larger fragments up to intact ACCs provides a comprehensive characterization of the dynamic fungal ACC architecture. In contrast to related carboxylases, large-scale conformational changes are required for substrate turnover, and are mediated by the CD under phosphorylation control.
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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.