ArticlePLoS pathogens2015
Characterization of the mycobacterial acyl-CoA carboxylase holo complexes reveals their functional expansion into amino acid catabolism.
Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 47 citations in OpenAlex.
- Article
- Architecture of an asymmetric short chain/long chain hybrid acyl‑CoA carboxylase from Mycobacterium smegmatis.Communications biology · 2026Article
- Structural basis for substrate specificity and MSMEG_0435-0436 binding by the mycobacterial long-chain acyl-CoA carboxylase complex.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Branched-chain amino acid metabolism supports Roseobacteraceae positive interactions in marine biofilms.Applied and environmental microbiology · 2025Article
- Comparative Proteomic Analysis of Cell Wall Proteins of Aminoglycosides Resistant and SensitiveCurrent protein & peptide science · 2025Article
- Polyphosphate kinase-1 regulates bacterial and host metabolic pathways involved in pathogenesis ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Global-scale GWAS associates a subset of SNPs with animal-adapted variants in M. tuberculosis complex.BMC medical genomics · 2023Article
- Biotin-dependent cell envelope remodelling is required for Mycobacterium abscessus survival in lung infection.Nature microbiology · 2023Article
- Clinical strains of Mycobacterium tuberculosis exhibit differential lipid metabolism-associated transcriptome changes in in vitro cholesterol and infection models.Pathogens and disease · 2023Article
- The functional response of human monocyte-derived macrophages to serum amyloid A andFrontiers in immunology · 2023Article
- Combined enhancement of the propionyl-CoA metabolic pathway for efficient androstenedione production in Mycolicibacterium neoaurum.Microbial cell factories · 2022Article
- Commonalities ofFrontiers in immunology · 2022Article
- AccR, a TetR Family Transcriptional Repressor, Coordinates Short-Chain Acyl Coenzyme A Homeostasis inApplied and environmental microbiology · 2020Article
- A GFP-strategy for efficient recombinant protein overexpression and purification inRSC advances · 2018Article
- Article
- Crystal structure of the essential biotin-dependent carboxylase AccA3 fromFEBS open bio · 2017Article
- Functional reconstitution of the Mycobacterium tuberculosis long-chain acyl-CoA carboxylase from multiple acyl-CoA subunits.The FEBS journal · 2017Article
- Emerging Approaches to Tuberculosis Drug Development: At Home in the Metabolome.Trends in pharmacological sciences · 2017Review
- The influence of AccD5 on AccD6 carboxyltransferase essentiality in pathogenic and non-pathogenic Mycobacterium.Scientific reports · 2017Article
- High coverage metabolomics analysis reveals phage-specific alterations to Pseudomonas aeruginosa physiology during infection.The ISME journal · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 7 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biotin-mediated carboxylation of short-chain fatty acid coenzyme A esters is a key step in lipid biosynthesis that is carried out by multienzyme complexes to extend fatty acids by one methylene group. Pathogenic mycobacteria have an unusually high redundancy of carboxyltransferase genes and biotin carboxylase genes, creating multiple combinations of protein/protein complexes of unknown overall composition and functional readout. By combining pull-down assays with mass spectrometry, we identified nine binary protein/protein interactions and four validated holo acyl-coenzyme A carboxylase complexes. We investigated one of these--the AccD1-AccA1 complex from Mycobacterium tuberculosis with hitherto unknown physiological function. Using genetics, metabolomics and biochemistry we found that this complex is involved in branched amino-acid catabolism with methylcrotonyl coenzyme A as the substrate. We then determined its overall architecture by electron microscopy and found it to be a four-layered dodecameric arrangement that matches the overall dimensions of a distantly related methylcrotonyl coenzyme A holo complex. Our data argue in favor of distinct structural requirements for biotin-mediated γ-carboxylation of α-β unsaturated acid esters and will advance the categorization of acyl-coenzyme A carboxylase complexes. Knowledge about the underlying structural/functional relationships will be crucial to make the target category amenable for future biomedical applications.
Indexed as
Identifiers
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.