👨‍💻👨‍🔬 This study shows that the collaboration of dry and wet lab is fundamental to achieve the improvement so sought in biocatalysis.
A big thank you goes to the first author Mahdi, and to all the collaborators at Zymvol that participated in this project.

🧪 Demonstrated on an engineered artificial enzyme based on the Lactococcal multidrug resistance regulator (LmrR) scaffold, the study reveals how distant residues communicate with catalytic regions and their mutation can fine-tune this communication affecting functional properties.

🔗 The pipeline allows to identify distal mutation hotspots—sites distant from the active site, that can still influence enzyme functional properties (e.g. activity and thermostability)

💻 We presented an open‑source computational workflow integrating residue network analysis, allosteric pathway mapping, and a ML-based functional site prediction model.

🌍 This work is the result of a great collaboration between the @roelfesgroup.bsky.social (@stratinghinst.bsky.social) at the @rug.nl and the NMR team at the @utrechtuniversity.bsky.social. Great work everybody!
5/5

💡 We found that the mutations significantly modify the dynamics of the whole protein, promoting a monomeric state (instead of the usual dimer structure) and allowing a novel interaction with the reaction substrates.
4/5

🧪 The wise use of a diamagnetic analogue (Zinc containing) of the cofactor allowed to track the changes in the structure of the enzyme in apo- and bound- state to the cofactor, as well as to the reaction substrates.
3/5

🔬 We used NMR to rationalize the role of two mutations that increase the catalytic activity towards the Friedel-Crafts Alkylation of indoles in an artificial metalloenzyme. The catalyst is based on a copper-phenanthroline complex bound within the hydrophobic pocket of the versatile LmrR protein.
2/5

Still better than default MS excel settings 🤭

Hello! I am a biochemist and protein engineer
pubmed.ncbi.nlm.nih.gov/38836699/