ArticleBiotechnology for biofuels2019
Identification of non-conserved residues essential for improving the hydrocarbon-producing activity of cyanobacterial aldehyde-deformylating oxygenase.
Article in Biotechnology for biofuels, 2019. 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, 35 citations in OpenAlex.
- Combining computer-aided enzyme design and chromosomal integration for plasmid-free biosynthesis of 1,5-pentanediol in Escherichia coli.Microbial cell factories · 2026Article
- Alkane biosynthesis gene expression and its increased production in recombinant cyanobacteria.FEBS open bio · 2025Article
- Codeine 3-O-demethylase catalyzed biotransformation of morphinan alkaloids in Escherichia coli: site directed mutagenesis of terminal residues improves enzyme expression, stability and biotransformation yield.Journal of biological engineering · 2025Article
- The Prokaryotic MicroalgaPolish journal of microbiology · 2023Article
- Biosynthesis pathways of expanding carbon chains for producing advanced biofuels.Biotechnology for biofuels and bioproducts · 2023Review
- Recent advances in the improvement of cyanobacterial enzymes for bioalkane production.Microbial cell factories · 2022Review
- Ferritin-Like Proteins: A Conserved Core for a Myriad of Enzyme Complexes.Sub-cellular biochemistry · 2022Article
- Microbial biotechnological approaches: renewable bioprocessing for the future energy systems.Microbial cell factories · 2021Review
- A novel C-terminal degron identified in bacterial aldehyde decarbonylases using directed evolution.Biotechnology for biofuels · 2020Article
- Improving hydrocarbon production by engineering cyanobacterial acyl-(acyl carrier protein) reductase.Biotechnology for biofuels · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCyanobacteria produce hydrocarbons corresponding to diesel fuels by means of aldehyde-deformylating oxygenase (ADO). ADO catalyzes a difficult and unusual reaction in the conversion of aldehydes to hydrocarbons and has been widely used for biofuel production in metabolic engineering; however, its activity is low. A comparison of the amino acid sequences of highly active and less active ADOs will elucidate non-conserved residues that are essential for improving the hydrocarbon-producing activity of ADOs.
resultsHere, we measured the activities of ADOs from 10 representative cyanobacterial strains by expressing each of them in
conclusionsWe succeeded in identifying non-conserved residues that are essential for improving ADO activity. Our results may be useful for generating combinatorial mutants of ADO that have both higher activity and higher amounts of the soluble protein in vivo, thereby producing higher yields of biohydrocarbons.
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