ArticlePLoS pathogens2022
Three enigmatic BioH isoenzymes are programmed in the early stage of mycobacterial biotin synthesis, an attractive anti-TB drug target.
Article in PLoS pathogens, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Balanced Expression of the Diiron Oxygenase BioE Is Essential for Biotin Homeostasis in Elizabethkingia meningoseptica.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- A ferritin-like diiron oxygenase BioE initiates bacterial biotin synthesis, a promising antivirulence target.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Confronting the Antimicrobial Resistance Crisis in China: Emerging Superbugs, Genomic Surveillance, and Innovative Countermeasures.China CDC weekly · 2025Article
- A Novel Esterase from Burkholderia sp. YD106 Capable of Hydrolysis of Methyl (R, S)-N-(2, 6-Dimethylphenyl) Alaninate, and Its Mutation for Improving Enantioselectivity.Applied biochemistry and biotechnology · 2025Article
- Structure and catalytic mechanism of exogenous fatty acid recycling by AasS, a versatile acyl-ACP synthetase.Nature structural & molecular biology · 2025Article
- A bacterial methyltransferase that initiates biotin synthesis, an attractive anti-ESKAPE druggable pathway.Science advances · 2024Article
- An inhibitory mechanism of AasS, an exogenous fatty acid scavenger: Implications for re-sensitization of FAS II antimicrobials.PLoS pathogens · 2024Article
- Mycobacterial biotin synthases require an auxiliary protein to convert dethiobiotin into biotin.Nature communications · 2024Article
- Advances in biotin biosynthesis and biotechnological production in microorganisms.World journal of microbiology & biotechnology · 2024Review
- The opportunistic pathogen Pseudomonas aeruginosa exploits bacterial biotin synthesis pathway to benefit its infectivity.PLoS pathogens · 2023Article
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Authors and funding
15 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tuberculosis (TB) is one of the leading infectious diseases of global concern, and one quarter of the world's population are TB carriers. Biotin metabolism appears to be an attractive anti-TB drug target. However, the first-stage of mycobacterial biotin synthesis is fragmentarily understood. Here we report that three evolutionarily-distinct BioH isoenzymes (BioH1 to BioH3) are programmed in biotin synthesis of Mycobacterium smegmatis. Expression of an individual bioH isoform is sufficient to allow the growth of an Escherichia coli ΔbioH mutant on the non-permissive condition lacking biotin. The enzymatic activity in vitro combined with biotin bioassay in vivo reveals that BioH2 and BioH3 are capable of removing methyl moiety from pimeloyl-ACP methyl ester to give pimeloyl-ACP, a cognate precursor for biotin synthesis. In particular, we determine the crystal structure of dimeric BioH3 at 2.27Å, featuring a unique lid domain. Apart from its catalytic triad, we also dissect the substrate recognition of BioH3 by pimeloyl-ACP methyl ester. The removal of triple bioH isoforms (ΔbioH1/2/3) renders M. smegmatis biotin auxotrophic. Along with the newly-identified Tam/BioC, the discovery of three unusual BioH isoforms defines an atypical 'BioC-BioH(3)' paradigm for the first-stage of mycobacterial biotin synthesis. This study solves a long-standing puzzle in mycobacterial nutritional immunity, providing an alternative anti-TB drug target.
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