| Autor: |
Andorfer MC; Department of Biology and Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA; email: mandorfe@mit.edu., Lewis JC; Department of Chemistry, University of Chicago, Chicago, Illinois 60637, USA; email: jaredlewis@uchicago.edu. |
| Jazyk: |
angličtina |
| Zdroj: |
Annual review of biochemistry [Annu Rev Biochem] 2018 Jun 20; Vol. 87, pp. 159-185. Date of Electronic Publication: 2018 Mar 28. |
| DOI: |
10.1146/annurev-biochem-062917-012042 |
| Abstrakt: |
Flavin-dependent halogenases (FDHs) catalyze the halogenation of organic substrates by coordinating reactions of reduced flavin, molecular oxygen, and chloride. Targeted and random mutagenesis of these enzymes have been used to both understand and alter their reactivity. These studies have led to insights into residues essential for catalysis and FDH variants with improved stability, expanded substrate scope, and altered site selectivity. Mutations throughout FDH structures have contributed to all of these advances. More recent studies have sought to rationalize the impact of these mutations on FDH function and to identify new FDHs to deepen our understanding of this enzyme class and to expand their utility for biocatalytic applications. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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