ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025
Molecular Chain Elongation Mechanism for n-Caproate Biosynthesis by Megasphaera Hexanoica.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Molecular Chain Elongation Mechanism for n-Caproate Biosynthesis by Megasphaera Hexanoica.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
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9 authors.
Funding
Abstract
The microbial production of medium-chain carboxylates has attracted considerable interest owing to their potential applications in biofuels and specialty chemicals; however, the underlying biosynthetic mechanisms remain incompletely understood. The present study evaluates the medium-chain carboxylate-producing microbe Megaspahera hexanoica using genomic analysis, transcriptome analysis, and metabolic engineering. Additionally, the n-caproate synthesis pathway of M. hexanoica is characterized with fructose as an electron donor, and the substrate specificity of the respective proteins is evaluated by constructing an n-caproate biosynthetic pathway in Escherichia coli. Among all r-BOX or RBO genes, thl_1583, which encodes β-ketothiolase (MhTHL), is identified as the most critical enzyme for the carbon chain elongation mechanism in M. hexanoica. Therefore, MhTHL is compared with other well-studied β-ketothiolases (CkTHL from Clostridium kluyveri, ReBktB from Ralstonia eutropha (Cupriavidus necator), EcAtoB from E. coli, and CaTHL from C. acetobutylicum). MhTHL is found to exhibit the highest n-caproate production, as evidenced by the protein crystal structure of MhTHL. Structural comparisons with other thiolases show that MhTHL has a larger substrate-binding pocket than ReBktB. Thiolase mutants generated by site-directed mutagenesis reveal that two residues (Leu87 and Val351) are essential for determining the size of the substrate-binding pocket.
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