ArticleChembiochem : a European journal of chemical biology2022
Discovery of Two Novel Oxidases Using a High-Throughput Activity Screen.
Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Predicting Functional Diversity Within Enzyme Families: A Practical Perspective.Chembiochem : a European journal of chemical biology · 2026Review
- Green bioconversion of insoluble chitin: chitinase development pathways via multi-strategy synergy.Bioresources and bioprocessing · 2026Review
- Activity assays for flavoprotein oxidases: an overview.Applied microbiology and biotechnology · 2025Review
- Enzymatic reactions towards aldehydes: An overview.Flavour and fragrance journal · 2023Review
- A general model to predict small molecule substrates of enzymes based on machine and deep learning.Nature communications · 2023Article
- Structural Elucidation and Engineering of a Bacterial Carbohydrate Oxidase.Biochemistry · 2023Article
- Discovery of Two Novel Oxidases Using a High-Throughput Activity Screen.Chembiochem : a European journal of chemical biology · 2022Article
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Abstract
Discovery of novel enzymes is a challenging task, yet a crucial one, due to their increasing relevance as chemical catalysts and biotechnological tools. In our work we present a high-throughput screening approach to discovering novel activities. A screen of 96 putative oxidases with 23 substrates led to the discovery of two new enzymes. The first enzyme, N-acetyl-D-hexosamine oxidase (EC 1.1.3.29) from Ralstonia solanacearum, is a vanillyl alcohol oxidase-like flavoprotein displaying the highest activity with N-acetylglucosamine and N-acetylgalactosamine. Before our discovery of the enzyme, its activity was an orphan one - experimentally characterized but lacking the link to amino acid sequence. The second enzyme, from an uncultured marine euryarchaeota, is a long-chain alcohol oxidase (LCAO, EC 1.1.3.20) active with a range of fatty alcohols, with 1-dodecanol being the preferred substrate. The enzyme displays no sequence similarity to previously characterised LCAOs, and thus is a completely novel representative of a protein with such activity.
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