The quest for new robust bacterial monoamine oxidases

• Published in: The FEBS journal Vol. 291; no. 5; pp. 846 - 848
• Main Author: Martins, Lígia O.
• Format: Journal Article
• Language: English
• Published: England Blackwell Publishing Ltd 01.03.2024
• Subjects: alkylamines; Amine oxidase (flavin-containing); biocatalysis; Biotechnology; Drug development; enzyme discovery; Enzymes; flavo‐oxidases; Microorganisms; Structure-function relationships; thermophiles; drug development; thermophiles; flavo-oxidases; alkylamines; enzyme discovery; biocatalysis
• ISSN: 1742-464X; 1742-4658
• DOI: 10.1111/febs.17002

Microbial enzymes are versatile, cost‐effective, and sustainable tools, making them a preferred choice for enzymatic processes. Santema et al. harnessed AlphaFold, a cutting‐edge structure prediction tool, to discover new thermophilic monoamine oxidases (MAO) that could be relevant for drug development and use in biotechnology fields. The new enzyme displays thermal robustness, offering a unique structure‐to‐function profile compared to known MAOs. This bacterial enzyme, paired with recent advancements in enzyme engineering, has the potential to meet the biotech sector's need for customized enzymes. Microbial enzymes are versatile, cost‐effective, and sustainable tools, making them a preferred choice for enzymatic processes. Santema and colleagues harnessed AlphaFold, a cutting‐edge structure prediction tool, to discover new thermophilic monoamine oxidases (MAO) that could be relevant for drug development and use in biotechnology fields. This bacterial enzyme, paired with recent advancements in enzyme engineering, has the potential to meet the biotech sector's need for customized enzymes. Comment on: https://doi.org/10.1111/febs.16973