Die Styroloxid-Isomerase entpuppt sich als multifunktioneller Helfer für die Biotechnologie.

Styrene oxide isomerase is proving to be a multifunctional helper for biotechnology.

TheA is a moderate thermostable flavin-dependent monooxygenase which accepts, besides l-ornithine a number of related molecules for the regio-selective N-hydroxylation. The combination with a NADP+-r...

Chiral epoxides are essential building blocks in the pharmaceutical and chemical industries. This perspective examines both established and emerging enzymatic pathways, highlights recent advancements,...

Nature Communications - Significant process has been made in using one carbon sources toward biomanufacturing. Here, the authors explore how to strength its competitiveness, and highlight latest...

Statt fossilen Rohstoffen wollen Forschende Abfälle aufwerten, um den CO2-Ausstoß einzudämmen.

Artur Maier et al. demonstrate the selective hydroxylation of N moieties of various compounds by means of enzymatic cascades. The so formed N-hydroxy compounds can be isolated and applied in synthesis...

A German-Dutch research group has expanded the toolkit for potential medications.

The nitrogen–nitrogen (N–N) bond motif comprises an important class of compounds for drug discovery. Synthetic methods are primarily based on the modification of N–N or N═N precursors, whereas selecti...

The nitrogen–nitrogen (N–N) bond motif comprises an important class of compounds for drug discovery. Synthetic methods are primarily based on the modification of N–N or N═N precursors, whereas selecti...

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Cytochrome P450 monooxygenases (CYPs) are versatile heme-containing enzymes found across a diverse range of organisms. They play essential roles in hy…

The discovery of enzymes (biocatalysts) can sometimes be challenging. Herein, we describe an approach for connecting phylogenetic information and mult…

Redox enzymes, mostly equipped with metal or organic cofactors, can vary their reactivity with oxygen by orders of magnitude. Understanding how oxygen reactivity is controlled by the protein milieu remains an open issue, with broad implications for mechanistic enzymology and enzyme design. Here, we address this problem by focusing on a widespread group of flavoenzymes that oxidize phenolic compounds derived from microbial lignin degradation, using either oxygen or cytochrome c as an electron acceptor. A comprehensive phylogenetic analysis revealed conserved amino acid motifs in the flavin-binding site. Using a combination of kinetic, mutagenesis, structural, and computational methods, we examined the role of these residues. Our results demonstrate that subtle and localized changes in the flavin environment can drastically impact oxygen reactivity. These effects are afforded through the creation or blockade of pathways for oxygen diffusion. Substrate binding plays a crucial role by potentially obstructing oxygen access to the flavin, thus influencing the enzyme’s reactivity. The switch between oxidase and dehydrogenase functionalities is thereby achieved through targeted, site-specific amino acid replacements that finely tune the microenvironment around the flavin. Our findings explain how very similar enzymes can exhibit distinct functional properties, operating as oxidases or dehydrogenases. They further provide valuable insights for the rational design and engineering of enzymes with tailored functions.