ArticleApplied microbiology and biotechnology2021
Identification of key residues for efficient glucose transport by the hexose transporter CgHxt4 in high sugar fermentation yeast Candida glycerinogenes.
Article in Applied microbiology and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Enhancing HAP3 mediated xylose metabolism and acetic acid metabolism promotes lipid production from lignocellulosic hydrolysate fermented by Candida glycerinogenes.Biotechnology letters · 2025Article
- Maltose and Maltotriose Transporters in Brewer'sInternational journal of molecular sciences · 2025Review
- Advances in fungal sugar transporters: unlocking the potential of second-generation bioethanol production.Applied microbiology and biotechnology · 2025Review
- Computational analysis of polymorphic residues in maltose and maltotriose transporters of a wildOpen life sciences · 2025Article
- Key amino acid residues govern the substrate selectivity of the transporter Xltr1p fromEngineering microbiology · 2024Article
- Synthesis of pinene in the industrial strain Candida glycerinogenes by modification of its mevalonate pathway.Journal of microbiology (Seoul, Korea) · 2022Article
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Authors and funding
5 authors at 2 institutions in 1 country.
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Abstract
Efficient hexose transporters are essential for the development of industrial yeast strains with high fermentation performance. We previously identified a hexose transporter, CgHxt4, with excellent sugar uptake performance at ultra-high glucose concentrations (200 g/L) in the high sugar fermenting yeast C. glycerinogenes. To understand the working mechanism of this transporter, we constructed 87 mutants and examined their glucose uptake performance. The results revealed that five residues (N321, N322, F325, G426, and P427) are essential for the efficient glucose transport of CgHxt4. Subsequently, we focused our analysis on the roles of N321 and P427. Specifically, N321 and P427 are likely to play a role in glucose coordination and conformational flexibility, respectively. Our results help to expand the application potential of this transporter and provide insights into the working mechanism of yeast hexose transporter. KEY POINTS: • Five residues, transmembrane segments 7 and 10, were found to be essential for CgHxt4. • N321 and P427 are likely to play a role in glucose coordination and conformational flexibility, respectively. • Chimeric CgHxt5.4TM7 significantly enhanced the performance of CgHxt5.
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