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Artificial Metalloenzymes for Asymmetric Catalysis by Creation of Novel Active Sites in Protein and DNA Scaffolds
Author(s) -
Drienovská Ivana,
Roelfes Gerard
Publication year - 2015
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.201400094
Subject(s) - chemistry , scaffold , combinatorial chemistry , active site , catalysis , dna , dimer , peptide , nanotechnology , optically active , protein engineering , computational biology , biochemistry , enzyme , organic chemistry , database , computer science , materials science , biology
Artificial metalloenzymes have emerged as a promising new approach to asymmetric catalysis. In our group, we are exploring novel artificial metalloenzyme designs involving creation of a new active site in a protein or DNA scaffold that does not have an existing binding pocket. In this review, we give an overview of the developments in the two approaches to artificial metalloenzymes for asymmetric catalysis investigated in our group: creation of a novel active site on a peptide or protein dimer interface and using DNA as a scaffold for artificial metalloenzymes.
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