I had a great time staying in Jean-Didier Maréchal's lab in 2022, and thanks also for the support in this project. Likewise, thanks again to Gerard Roelfes for support throughout!

Many thanks to everyone involved in this highly collaborative and interdisciplinary study, as well as Ivana Drienovska and Clemens Mayer who originally developed and evolved LmrR_pAF! It's great to see how a curiosity I found in the lab over two years ago lead to this interesting story.

Combined with mutagenesis results, and crystallographic data from Henriette Rozeboom and Andy-Mark Thunnissen, we discovered that the (1) mutations modulate enzyme quaternary structure and (2) unnatural and natural side chains work together to form a new kind of catalytic machinery.

Intrigued by this, I went with a FEBS Short Term fellowship to Jean-Didier Maréchal's lab where Laura Tiessler Sala helped me learned quantum chemistry and molecular dynamics methods.

Evolutionary Specialization of a Promiscuous Designer Enzyme The evolution of a promiscuous enzyme for its various activities often results in catalytically specialized variants. This is an important natural mechanism to ensure the proper functioning of natural...

Very happy to see that our latest paper just appeared online in ACS Catalysis. Two directed evolution campaigns of an artificial enzyme from @roelfesgroup.bsky.social found that just 3 mutations could specialise it towards each of its promiscuous activities.
pubs.acs.org/doi/10.1021/acscatal.4c06409