microbiotech : The Tischler Lab

The promiscuous N-hydroxylating monooxygenase GorA and its application in cascades 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...

The promiscuous N-hydroxylating monooxygenase GorA and its application in cascades: Cell Reports Physical Science www.cell.com/cell-reports...

A real team work; amazing !!! congrats to our team members and the collaboration partners ;-)

amazing event ... the group is proud and parties ;-)

Big congrats to @danieleggerichs.bsky.social !!! Amazing 😱 You deserve it and we are looking forward to celebrate it together !!!

New Agents with Genome Mining and Mutagenesis A German-Dutch research group has expanded the toolkit for potential medications.

Press Release for our latest publication in @pubs.acs.org ACS Catalysis

news.rub.de/english/pres...

Access to Nitrogen–nitrogen Bond-Containing Heterocycles Through Substrate Promiscuity of Piperazate Synthases 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...

Access to Nitrogen–nitrogen Bond-Containing Heterocycles Through Substrate Promiscuity of Piperazate Synthases | ACS Catalysis pubs.acs.org/doi/10.1021/...

Access to Nitrogen–nitrogen Bond-Containing Heterocycles Through Substrate Promiscuity of Piperazate Synthases 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...

Congrats on this new story:

Access to Nitrogen–nitrogen Bond-Containing Heterocycles Through Substrate Promiscuity of Piperazate Synthases | ACS Catalysis pubs.acs.org/doi/10.1021/...

Spoiler, there will soon be a new book on the shelf with focus on #enzymology #enzyme #application #biocatalysis ... stay tuned as more details I will share on short notice 😊

@dirktischler.bsky.social is opening the @vaam-microbes.bsky.social conference 2025 at @ruhr-uni-bochum.de. Looking forward to three days of presentations, posters, and networking!

Wonderful to see it now in printed version! @danieleggerichs.bsky.social started and we will continue to understand this #enzyme in more detail (more #enzymology to come) as well as to apply it (more #biocatalysis to come)

Congrats from the team!

NextGenBiocat Visit the post for more.

Are you a #youngresearcher working in #biocatalysis? Do you want to share your work with #internationalscientists? Come to the #nextgenbiocat 8-9 of May in Milan!
nextgenbiocat.org

Cytochrome P450 monooxygenases in whole-cell format: Application notes from a biotechnological perspective Cytochrome P450 monooxygenases (CYPs) are versatile heme-containing enzymes found across a diverse range of organisms. They play essential roles in hy…

a book chapter by @carmg.bsky.social from our team moved online; congrats! Cytochrome P450 monooxygenases in whole-cell format: Application notes... www.sciencedirect.com/science/arti...

Sequence-function relation for the prediction of enzyme properties: A case study on flavin-dependent oxidases The discovery of enzymes (biocatalysts) can sometimes be challenging. Herein, we describe an approach for connecting phylogenetic information and mult…

A book chapter from our team was just published; it is about #enzymes #oxidases #screening #phylogeny #predictivebiotechnology #enzymeengineering ... congrats Nils @ et al ;-)

www.sciencedirect.com/science/arti...

" 'Diese [Alkohole] wiederum nutzen wir dann für Bakterien oder isolierte Enzyme als Substrat für die Herstellung verschiedener Zielprodukte, die für Kosmetika oder Kunststoffe genutzt werden können', so Carolin Mügge" news.rub.de/presseinform...

Great to see this online, were @danieleggerichs.bsky.social and @dirktischler.bsky.social contributed !!! #enzymology #biocatalysis for @acs.org catalysis

We move now slowly here :-) our group is interested in #enzymes #biocatalysis #actinobacteria #biotechnology and more we are looking forward to new and old connections!

let's become active #chemsky #enzymesky ... !!!

Dehydrogenase versus Oxidase Function: The Interplay between Substrate Binding and Flavin Microenvironment 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.

Great study on the question what defines an #oxidase vs. a #dehydrogenase... and vice versa #proteinengineering #biocatalysis #flavoprotein #flavin #enzymology

pubs.acs.org/doi/10.1021/...