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

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...