carba‐Nicotinamid‐Adenin‐Dinukleotid‐Phosphat: Robuster Cofaktor für die Redox‐Biokatalyse

Cofaktoren werden für beinahe die Hälfte aller Enzymreaktionen benötigt. Ihre Funktionen und Bindungspartner sind jedoch auch nach jahrzehntelanger Forschung noch nicht vollständig verstanden. Funktionalisierte Cofaktoren (Analoga), die anstelle des natürlichen Cofaktors binden, können darauf Antworten liefern und den Aktivitätsbereich des jeweiligen Cofaktors aufklären. Mithilfe chemischer Proteomik‐Ansätze wie des aktivitätsbasierten Protein‐Profilings können das Interaktom und die Lokalisierung des nativen Cofaktors in seiner physiologischen Umgebung entschlüsselt und bisher uncharakterisierte Proteine annotiert werden. Darüber hinaus können Cofaktoren, die funktionelle Gruppen an Substrat‐Biomoleküle übertragen, genutzt werden, um als Analoge Enzyme ortsspezifisch zu markieren und die komplexe Biologie der posttranslationalen Proteinmodifikation zu untersuchen. Die vielfältige Aktivität von Cofaktoren hat die Entwicklung von deren Analoga für den Einsatz als Inhibitoren, Antibiotika sowie Chemo‐ und Biosensoren inspiriert. Darüber hinaus haben Cofaktor‐Konjugate die Herstellung neuartiger Enzyme und künstlicher DNA‐Enzyme ermöglicht.

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Funktionalisierte Cofaktor‐Analoga für die Erforschung von Interaktomen und darüber hinaus

Wilkinson

Pfanzelt

Sieber

2022

Angewandte Chemie

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Multienzyme Redox System with Cofactor Regeneration for Cyclic Deracemization of Sulfoxides

et al. 2022

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Optically pure sulfoxides are noteworthy compounds applied in a wide range of industrial fields; however, the biocatalytic deracemization of racemic sulfoxides is challenging. Herein, a high‐enantioselective methionine sulfoxide reductase A (MsrA) was combined with a low‐enantioselective styrene monooxygenase (SMO) for the cyclic deracemization of sulfoxides. Enantiopure sulfoxides were obtained in >90 % yield and with >90 % enantiomeric excess (ee) through dynamic “selective reduction and non‐selective oxidation” cycles. The cofactors of MsrA and SMO were subsequently regenerated by the cascade catalysis of three auxiliary enzymes through the consumption of low‐cost D‐glucose. Moreover, this “one‐pot, one‐step” cyclic deracemization strategy exhibited a wide substrate scope toward various aromatic, heteroaromatic, alkyl and thio‐alkyl sulfoxides. This system proposed an efficient strategy for the green synthesis of chiral sulfoxide.

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Functionalised Cofactor Mimics for Interactome Discovery and Beyond

2022

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Cofactors are required for almost half of all enzyme reactions, but their functions and binding partners are not fully understood even after decades of research. Functionalised cofactor mimics that bind in place of the unmodified cofactor can provide answers, as well as expand the scope of cofactor activity. Through chemical proteomics approaches such as activity-based protein profiling, the interactome and localisation of the native cofactor in its physiological environment can be deciphered and previously uncharacterised proteins annotated. Furthermore, cofactors that supply functional groups to substrate biomolecules can be hijacked by mimics to site-specifically label targets and unravel the complex biology of post-translational protein modification. The diverse activity of cofactors has inspired the design of mimics for use as inhibitors, antibiotic therapeutics, and chemo-and biosensors, and cofactor conjugates have enabled the generation of novel enzymes and artificial DNAzymes.

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carba‐Nicotinamid‐Adenin‐Dinukleotid‐Phosphat: Robuster Cofaktor für die Redox‐Biokatalyse

Cited by 4 publications

References 54 publications

Funktionalisierte Cofaktor‐Analoga für die Erforschung von Interaktomen und darüber hinaus

Funktionalisierte Cofaktor‐Analoga für die Erforschung von Interaktomen und darüber hinaus

Multienzyme Redox System with Cofactor Regeneration for Cyclic Deracemization of Sulfoxides

Functionalised Cofactor Mimics for Interactome Discovery and Beyond

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