Biocatalytic Alkylation Chemistry: Building Molecular Complexity with High Selectivity
Ospina Sánchez F, Schülke KH, Hammer S (2022)
ChemPlusChem 87(1): e202100454.
Zeitschriftenaufsatz
| E-Veröff. vor dem Druck | Englisch
Download
Projekt
DBU PhD Kai Schülke: Deutsche Bundesstiftung Umwelt: Erweiterte Cosubstrat-Biochemie: Enzymatische Synthese und Rezyklierung von SAM-Analoga für hochselektive Alkylierungschemie (Sachmittel Kai Schülke)
Emmy Noether Phase 1: New catalytic reaction development by laboratory evolution of protein-based catalysts (Emmy Noether Research Group Phase 1)
Emmy Noether Phase 1: New catalytic reaction development by laboratory evolution of protein-based catalysts (Emmy Noether Research Group Phase 1)
Abstract / Bemerkung
Biocatalysis has traditionally been viewed as a field that primarily enables access to chiral centers. This includes the synthesis of chiral alcohols, amines and carbonyl compounds, often through functional group interconversion via hydrolytic or oxidation-reduction reactions. This limitation is partly being overcome by the design and evolution of new enzymes. Here, we provide an overview of a recently thriving research field that we summarize as biocatalytic alkylation chemistry. In the past 3-4 years, numerous new enzymes have been developed that catalyze sp3 C-C/N/O/S bond formations. These enzymes utilize different mechanisms to generate molecular complexity by coupling simple fragments with high activity and selectivity. In many cases, the engineered enzymes perform reactions that are difficult or impossible to achieve with current small-molecule catalysts such as organocatalysts and transition-metal complexes. This review further highlights that the design of new enzyme function is particularly successful when off-the-shelf synthetic reagents are utilized to access non-natural reactive intermediates. This underscores how biocatalysis is gradually moving to a field that build molecules through selective bond forming reactions. © 2021 The Authors. ChemPlusChem published by Wiley-VCH GmbH.
Erscheinungsjahr
2022
Zeitschriftentitel
ChemPlusChem
Band
87
Ausgabe
1
Art.-Nr.
e202100454
Urheberrecht / Lizenzen
ISSN
2192-6506
Finanzierungs-Informationen
Open-Access-Publikationskosten wurden durch die Universität Bielefeld im Rahmen des DEAL-Vertrags gefördert.
Page URI
https://pub.uni-bielefeld.de/record/2959615
Zitieren
Ospina Sánchez F, Schülke KH, Hammer S. Biocatalytic Alkylation Chemistry: Building Molecular Complexity with High Selectivity. ChemPlusChem. 2022;87(1): e202100454.
Ospina Sánchez, F., Schülke, K. H., & Hammer, S. (2022). Biocatalytic Alkylation Chemistry: Building Molecular Complexity with High Selectivity. ChemPlusChem, 87(1), e202100454. https://doi.org/10.1002/cplu.202100454
Ospina Sánchez, Felipe, Schülke, Kai Hannes, and Hammer, Stephan. 2022. “Biocatalytic Alkylation Chemistry: Building Molecular Complexity with High Selectivity”. ChemPlusChem 87 (1): e202100454.
Ospina Sánchez, F., Schülke, K. H., and Hammer, S. (2022). Biocatalytic Alkylation Chemistry: Building Molecular Complexity with High Selectivity. ChemPlusChem 87:e202100454.
Ospina Sánchez, F., Schülke, K.H., & Hammer, S., 2022. Biocatalytic Alkylation Chemistry: Building Molecular Complexity with High Selectivity. ChemPlusChem, 87(1): e202100454.
F. Ospina Sánchez, K.H. Schülke, and S. Hammer, “Biocatalytic Alkylation Chemistry: Building Molecular Complexity with High Selectivity”, ChemPlusChem, vol. 87, 2022, : e202100454.
Ospina Sánchez, F., Schülke, K.H., Hammer, S.: Biocatalytic Alkylation Chemistry: Building Molecular Complexity with High Selectivity. ChemPlusChem. 87, : e202100454 (2022).
Ospina Sánchez, Felipe, Schülke, Kai Hannes, and Hammer, Stephan. “Biocatalytic Alkylation Chemistry: Building Molecular Complexity with High Selectivity”. ChemPlusChem 87.1 (2022): e202100454.
Alle Dateien verfügbar unter der/den folgenden Lizenz(en):
Creative Commons Namensnennung - Nicht kommerziell - Keine Bearbeitungen 4.0 International (CC BY-NC-ND 4.0):
Volltext(e)
Access Level
Open Access
Zuletzt Hochgeladen
2022-06-29T07:00:26Z
MD5 Prüfsumme
e044a5c5291421dc4e675de378e7c868
Daten bereitgestellt von European Bioinformatics Institute (EBI)
Zitationen in Europe PMC
Daten bereitgestellt von Europe PubMed Central.
References
Daten bereitgestellt von Europe PubMed Central.
Export
Markieren/ Markierung löschen
Markierte Publikationen
Web of Science
Dieser Datensatz im Web of Science®Quellen
PMID: 34821073
PubMed | Europe PMC
Suchen in