Cargando…
Identification of promiscuous ene-reductase activity by mining structural databases using active site constellations
The exploitation of catalytic promiscuity and the application of de novo design have recently opened the access to novel, non-natural enzymatic activities. Here we describe a structural bioinformatic method for predicting catalytic activities of enzymes based on three-dimensional constellations of f...
Autores principales: | Steinkellner, Georg, Gruber, Christian C., Pavkov-Keller, Tea, Binter, Alexandra, Steiner, Kerstin, Winkler, Christoph, Łyskowski, Andrzej, Schwamberger, Orsolya, Oberer, Monika, Schwab, Helmut, Faber, Kurt, Macheroux, Peter, Gruber, Karl |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Pub. Group
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4083419/ https://www.ncbi.nlm.nih.gov/pubmed/24954722 http://dx.doi.org/10.1038/ncomms5150 |
Ejemplares similares
-
The Structure of Glycerol Trinitrate Reductase NerA from Agrobacterium radiobacter Reveals the Molecular Reason for Nitro- and Ene-Reductase Activity in OYE Homologues
por: Oberdorfer, Gustav, et al.
Publicado: (2013) -
Asymmetric Reductive Carbocyclization Using Engineered Ene Reductases
por: Heckenbichler, Kathrin, et al.
Publicado: (2018) -
Mechanistic Insights
into the Ene-Reductase-Catalyzed
Promiscuous Reduction of Oximes to Amines
por: Breukelaar, Willem B., et al.
Publicado: (2023) -
Crystal Structure of an (R)-Selective ω-Transaminase from Aspergillus terreus
por: Łyskowski, Andrzej, et al.
Publicado: (2014) -
Regioselective Enzymatic β‐Carboxylation of para‐Hydroxy‐ styrene Derivatives Catalyzed by Phenolic Acid Decarboxylases
por: Wuensch, Christiane, et al.
Publicado: (2015)