🥳🥳🥳 Our study on engineering enzymes to break C–F bonds is out in @angewandtechemie.bsky.social. Congrats to the brilliant & dedicated @suzannejansen.bsky.social for taking this step toward the remediation of #PFAS & other contaminating organofluorides!
onlinelibrary.wiley.com/doi/10.1002/...
Overview of ADD-tagging including ADP-ribosyl cyclase (ADPRC)-catalysed dinucleotide substrate generation and two step chemoenzymatic labelling of target proteins with the flavin transferase ApbE, followed by click chemistry-based functional group attachment.
🚨 preprint 2️⃣ this month: our (purely experimental🧪) venture into #ChemBio
We prouldy present: ADD-tagging of proteins (or "ADDing") —a super convenient enzymatic technique to install click chemistry handles on proteins.
Led by superstar @wahyuwidodo.bsky.social
www.biorxiv.org/content/10.1...
A 🧵👇🏽
📢📢📢 PhD Opportunity!
Join our research group at RUG! We're seeking a motivated PhD student for a project on biocatalytic cascade processes combining natural and designer enzymes, supported by machine learning.
Click below to learn more — and feel free to share!
sites.google.com/rug.nl/roelf...
Thank you @francdefel.bsky.social, Andy and Gerard for the great collaboration!
@roelfesgroup.bsky.social @stratinghinst.bsky.social
Last but not least, the simple and straightforward genetic incorporation of aY facilitated the application of the evolved Friedel-Crafts alkylase in whole-cells!
X-ray crystal structures of the parent and evolved mutant (2.2 Å and 1.2 Å!) showed a significant change in the rotameric state of the aY catalytic residue, and a narrowing of the active site cavity.
Directed evolution gave rise to a quadruple mutant that showed increased activity and excellent enantioselectivity (up to 95% ee).
Through genetic incorporation of aY into LmrR, we create an artificial Friedel-Crafts alkylase that is enantiocomplementary to a previous design featuring p-aminophenylalanine as catalytic residue.
We demonstrate the first example of using noncanonical 3-aminotyrosine (aY) as a catalytic residue for iminium activation in a designer enzyme
Very proud to share that one of my main PhD projects has been published in @chemicalscience.rsc.org, and that it has been selected as a #ChemSciPicks of the week paper!
Keep reading below for more details, or check out the full paper for free online: doi.org/10.1039/D5SC...
Thread ⬇️
Grateful to be part of this awesome project lead by @brouwerb.bsky.social. Take a look to our preprint about unlocking iminium ion catalysis when using amino-tyrosine as a genetically encoded amino acid! 🤓
#MSCA @roelfesgroup.bsky.social
Thank you Franco, Andy and Gerard for the great collaboration!
Looking forward to seeing it published soon, keep your eyes peeled!
@roelfesgroup.bsky.social @stratinghinst.bsky.social
Last but not least, the simple and straightforward genetic incorporation of aY facilitated the application of the evolved Friedel-Crafts alkylase in whole-cells!
X-ray crystal structures of the parent and evolved mutant (2.2 Å and 1.2 Å!) showed a significant change in the rotameric state of the aY catalytic residue, and a narrowing of the active site cavity.
Directed evolution gave rise to a quadruple mutant that showed increased activity and excellent enantioselectivity (up to 95% ee).
Through genetic incorporation of aY into LmrR, we create an artificial Friedel-Crafts alkylase that is enantiocomplementary to a previous design featuring p-aminophenylalanine as catalytic residue.
doi.org/10.26434/che...
Check out our latest preprint, in which we demonstrate the first example of using noncanonical 3-aminotyrosine (aY) as a catalytic residue for iminium activation in a designer enzyme!
Thread ⬇️