ArticleMicrobial biotechnology2017
Expansion of the ω-oxidation system AlkBGTL of Pseudomonas putida GPo1 with AlkJ and AlkH results in exclusive mono-esterified dicarboxylic acid production in E. coli.
Article in Microbial biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Engineering membrane-bound alkane monooxygenase from Marinobacter sp. for increased activity in the selective ω-hy-droxylation of linear and branched aliphatic esters.Protein science : a publication of the Protein Society · 2026Article
- A Comprehensive Review on Medium- and Long-Chain Fatty Acid-Derived Metabolites: From Energy Sources to Metabolic Signals.Metabolites · 2026Review
- Engineering of Transmembrane Alkane Monooxygenases to Improve a Key Reaction Step in the Synthesis of Polymer Precursor Tulipalin A.Angewandte Chemie (International ed. in English) · 2025Article
- De novo biosynthesis of nylon 12 monomer ω-aminododecanoic acid.Nature communications · 2025Article
- Cutinase ACut2 fromMicroorganisms · 2022Article
- An Overview of the Electron-Transfer Proteins That Activate Alkane Monooxygenase (AlkB).Frontiers in microbiology · 2022Review
- Investigation of the prevalence and catalytic activity of rubredoxin-fused alkane monooxygenases (AlkBs).Journal of inorganic biochemistry · 2021Article
- Combination of ester biosynthesis and ω-oxidation for production of mono-ethyl dicarboxylic acids and di-ethyl esters in a whole-cell biocatalytic setup with Escherichia coli.Microbial cell factories · 2017Article
- Expansion of the ω-oxidation system AlkBGTL of Pseudomonas putida GPo1 with AlkJ and AlkH results in exclusive mono-esterified dicarboxylic acid production in E. coli.Microbial biotechnology · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The AlkBGTL proteins coded on the alk operon from Pseudomonas putida GPo1 can selectively ω-oxidize ethyl esters of C6 to C10 fatty acids in whole-cell conversions with Escherichia coli. The major product in these conversions is the ω-alcohol. However, AlkB also has the capacity to overoxidize the substrate to the ω-aldehyde and ω-acid. In this study, we show that alcohol dehydrogenase AlkJ and aldehyde dehydrogenase AlkH are able to oxidize ω-alcohols and ω-aldehydes of esterified fatty acids respectively. Resting E. coli expressing AlkBGTHJL enabled exclusive mono-ethyl azelate production from ethyl nonanoate, with an initial specific activity of 61 U g
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