ArticleScientific reports2017
Expression and Activity of the BioH Esterase of Biotin Synthesis is Independent of Genome Context.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Defining the Enterococcus faecalis Fatty Acid Kinase System of Exogeneous Fatty Acid Utilization.Molecular microbiology · 2025Article
- Engineering controllable alteration of malonyl-CoA levels to enhance polyketide production.Nature chemical biology · 2025Article
- A bacterial methyltransferase that initiates biotin synthesis, an attractive anti-ESKAPE druggable pathway.Science advances · 2024Article
- The opportunistic pathogen Pseudomonas aeruginosa exploits bacterial biotin synthesis pathway to benefit its infectivity.PLoS pathogens · 2023Article
- Three enigmatic BioH isoenzymes are programmed in the early stage of mycobacterial biotin synthesis, an attractive anti-TB drug target.PLoS pathogens · 2022Article
- The Biotin Biosynthetic Pathway in Mycobacterium tuberculosis is a Validated Target for the Development of Antibacterial Agents.Current medicinal chemistry · 2020Review
- The Thaumarchaeon N. gargensis carries functional bioABD genes and has a promiscuous E. coli ΔbioH-complementing esterase EstN1.Scientific reports · 2018Article
- Protein moonlighting elucidates the essential human pathway catalyzing lipoic acid assembly on its cognate enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Development and retention of a primordial moonlighting pathway of protein modification in the absence of selection presents a puzzle.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Transition State Analogue Inhibitors of 5'-Deoxyadenosine/5'-Methylthioadenosine Nucleosidase from Mycobacterium tuberculosis.Biochemistry · 2017Article
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
BioH is an α/β-hydrolase required for synthesis of the pimelate moiety of biotin in diverse bacteria. The bioH gene is found in different genomic contexts. In some cases (e.g., Escherichia coli) the gene is not located within a biotin synthetic operon and its transcription is not coregulated with the other biotin synthesis genes. In other genomes such as Pseudomonas aeruginosa the bioH gene is within a biotin synthesis operon and its transcription is coregulated with the other biotin operon genes. The esterases of pimelate moiety synthesis show remarkable genomic plasticity in that in some biotin operons bioH is replaced by other α/ß hydrolases of diverse sequence. The "wild card" nature of these enzymes led us to compare the paradigm "freestanding" E. coli BioH with the operon-encoded P. aeruginosa BioH. We hypothesized that the operon-encoded BioH might differ in its expression level and/or activity from the freestanding BioH gene. We report this is not the case. The two BioH proteins show remarkably similar hydrolase activities and substrate specificity. Moreover, Pseudomonas aeruginosa BioH is more highly expressed than E. coli BioH. Despite the enzymatic similarities of the two BioH proteins, bioinformatics analysis places the freestanding and operon-encoded BioH proteins into distinct clades.
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