ArticleScientific reports2018
The Thaumarchaeon N. gargensis carries functional bioABD genes and has a promiscuous E. coli ΔbioH-complementing esterase EstN1.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Structural and biochemical insights into the thermostable esterase Ta0887 from Thermoplasma acidophilum.FEBS open bio · 2026Article
- Advances and prospects in microbial production of biotin.Microbial cell factories · 2024Review
- Cloning, Expression, Characterization and Immobilization of a Recombinant Carboxylesterase from the Halophilic Archaeon,Biomolecules · 2024Article
- Cloning, heterologous expression, and characterization of a novel thioesterase from natural sample.Heliyon · 2021Article
- Genomic Insights of "Frontiers in microbiology · 2020Article
- Evolution ofPeerJ · 2020Article
- Phylogenomics suggests oxygen availability as a driving force in Thaumarchaeota evolution.The ISME journal · 2019Article
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4 authors.
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Abstract
Biotin is an essential cofactor required for carboxylation and decarboxylation reactions in all domains of life. While biotin biosynthesis in most Bacteria and Eukarya is well studied, the complete pathway for this vitamer in Archaea is still not known. Detailed genome searches indicated the presence of possible bio gene clusters only in Methanococcales and Thaumarchaeota. Therefore, we analysed the functionality of the predicted genes bioA, bioB, bioD and bioF in the Thaumarchaeon Nitrososphaera gargensis Ga2.9 which are essential for the later steps of biotin synthesis. In complementation tests, the gene cluster-encoded N. gargensis bioABD genes except bioF restored growth of corresponding E. coli Rosetta-gami 2 (DE3) deletion mutants. To find out how biotin biosynthesis is initiated, we searched the genome for a possible bioH analogue encoding a pimeloyl-ACP-methylester carboxylesterase. The respective amino acid sequence of the ORF estN1 showed weak conserved domain similarity to this class of enzymes (e-value 3.70e
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