Directed evolution of hybrid enzymes: Evolving enantioselectivity of an achiral Rh-complex anchored to a protein
Literature Information
Manfred T. Reetz, Jérôme J.-P. Peyralans, Andrea Maichele, Yu Fu, Matthias Maywald
The concept of utilizing the methods of directed evolution for tuning the enantioselectivity of synthetic achiral metal–ligand centers anchored to proteins has been implemented experimentally for the first time.
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![L-Threonine, N-[[4,7,10-tris(carboxymethyl)-1,4,7,10-tetraazacyclododec-1-yl]acetyl]-D-phenylalanyl-L-cysteinyl-L-tyrosyl-D-tryptophyl-L-lysyl-L-threonyl-L-cysteinyl-, cyclic (2→7)-disulfide, acetate (salt) (9CI) structure L-Threonine, N-[[4,7,10-tris(carboxymethyl)-1,4,7,10-tetraazacyclododec-1-yl]acetyl]-D-phenylalanyl-L-cysteinyl-L-tyrosyl-D-tryptophyl-L-lysyl-L-threonyl-L-cysteinyl-, cyclic (2→7)-disulfide, acetate (salt) (9CI) structure](https://static.chemtradehub.com/structs/177/177943-89-4-6312.webp)
![4-Nitrophenyl N-{[(2-methyl-2-propanyl)oxy]carbonyl}-L-isoleucinate structure 4-Nitrophenyl N-{[(2-methyl-2-propanyl)oxy]carbonyl}-L-isoleucinate structure](https://static.chemtradehub.com/structs/169/16948-38-2-c88f.webp)