Metal-binding promiscuity in artificial metalloenzyme design.
Curr Opin Chem Biol
; 25: 124-32, 2015 Apr.
Article
en En
| MEDLINE
| ID: mdl-25603469
ABSTRACT
This review presents recent examples of metal-binding promiscuity in protein scaffolds and highlights the effect of metal variation on catalytic functionality. Naturally evolved binding sites, as well as unnatural amino acids and cofactors can bind a diverse range of metals, including non-biological transition elements. Computational screening and rational design have been successfully used to create promiscuous binding-sites. Incorporation of non-native metals into proteins expands the catalytic range of transformations catalysed by enzymes and enhances their potential for application in chemicals synthesis.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Ingeniería de Proteínas
/
Enzimas
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Metaloproteínas
/
Metales
Idioma:
En
Año:
2015
Tipo del documento:
Article