Proteins as diverse, efficient, and evolvable scaffolds for artificial metalloenzymes

By combining synthetic catalysts and biochemical tools, numerous artificial metalloenzymes have been designed to exhibit high catalytic activity and selectivity in diverse chemical transformations. Out of the nearly infinite number of discovered or characterised proteins, however, only a handful of...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2020-08, Vol.56 (67), p.9586-9599
Main Authors: Jeong, Woo Jae, Yu, Jaeseung, Song, Woon Ju
Format: Article
Language:English
Subjects:
Animals
Biochemistry
Catalytic activity
Catalytic Domain
Cellular structure
Cysteine - chemistry
Cysteine - metabolism
Metalloproteins - chemistry
Metalloproteins - metabolism
Metals - chemistry
Muramidase - chemistry
Muramidase - metabolism
Properties (attributes)
Protein Conformation
Protein Stability
Proteins
Scaffolds
Selectivity
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Summary:By combining synthetic catalysts and biochemical tools, numerous artificial metalloenzymes have been designed to exhibit high catalytic activity and selectivity in diverse chemical transformations. Out of the nearly infinite number of discovered or characterised proteins, however, only a handful of proteins have been employed as scaffolds for artificial metalloenzymes, implying that specific proteins are preferred owing to their native structural, functional, or biochemical properties. In the present review, we extract and group the biochemical and structural properties of proteins that are advantageous in the design of artificial metalloenzymes; protein stability, pre-existing metal centre, native binding affinity for small molecules, confined and empty space, well-defined secondary structure, and native cellular location. The desirable properties highlight proteins as the key players in the design of metal-dependent biocatalysts. We also propose rarely considered, yet promising, proteins that could be versatile and unique scaffolds for novel metalloenzymes. We have extracted and categorized the desirable properties of proteins that are adapted as the scaffolds for artificial metalloenzymes.
ISSN:1359-7345
1364-548X
DOI:10.1039/d0cc03137b