ArticleScientific reports2017
Crucial role of 4-deoxy-L-erythro-5-hexoseulose uronate reductase for alginate utilization revealed by adaptive evolution in engineered Saccharomyces cerevisiae.
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 8 papers.
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8 citing papers in PubMed, 10 citations in OpenAlex.
- Conversion of minimally processed Sargassum to lipids with the yeast Rhodosporidium toruloides.Biotechnology letters · 2026Article
- 4-Deoxy-l-Molecules (Basel, Switzerland) · 2022Review
- Bacteria with a mouth: Discovery and new insights into cell surface structure and macromolecule transport.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2022Article
- Bacterial and fungal gut microbiota of supralittoral talitrid amphipods feeding on brown macroalgae and paper.PloS one · 2022Article
- Structure Characteristics, Biochemical Properties, and Pharmaceutical Applications of Alginate Lyases.Marine drugs · 2021Review
- Bacterial alginate metabolism: an important pathway for bioconversion of brown algae.Biotechnology for biofuels · 2021Review
- Characterization of a New Biofunctional, Exolytic Alginate Lyase fromMarine drugs · 2021Article
- Uncovering the reactive nature of 4-deoxy-L-erythro-5-hexoseulose uronate for the utilization of alginate, a promising marine biopolymer.Scientific reports · 2019Article
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Authors and funding
7 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
In brown macroalgae, alginate and D-mannitol are promising carbohydrates for biorefinery. Saccharomyces cerevisiae is widely used as a microbial cell factory, but this budding yeast is unable to utilize either alginate or D-mannitol. Alginate can be depolymerized by both endo-type and exo-type alginate lyases, yielding a monouronate, 4-deoxy-L-erythro-5-hexoseulose uronate (DEH), a key intermediate in the metabolism of alginate. Here, we constructed engineered two S. cerevisiae strains that are able to utilize both DEH and D-mannitol on two different strain backgrounds, and we also improved their aerobic growth in a DEH liquid medium through adaptive evolution. In both evolved strains, one of the causal mutations was surprisingly identical, a c.50A > G mutation in the codon-optimized NAD(P)H-dependent DEH reductase gene, one of the 4 genes introduced to confer the capacity to utilize DEH. This mutation resulted in an E17G substitution at a loop structure near the coenzyme-binding site of this reductase, and enhanced the reductase activity and aerobic growth in both evolved strains. Thus, the crucial role for this reductase reaction in the metabolism of DEH in the engineered S. cerevisiae is demonstrated, and this finding provides significant information for synthetic construction of a S. cerevisiae strain as a platform for alginate utilization.
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