Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Matthias Häckh"'
Autor:
Xavier Lucas, Stefan Günther, Michael Müller, Peter F. Leadlay, Matthias Häckh, Steffen Lüdeke, Marija Marolt
Publikováno v:
ChemBioChem. 20:1150-1154
Enzymes often convert both physiological and non-physiological substrates with high stereoselectivity; yet, for some enzymes, opposite product chirality is observed. A possible explanation is the existence of hidden specificities becoming apparent wh
Autor:
Andriy Luzhetskyy, Steffen Lüdeke, Stefan Günther, Björn Grüning, Michael Müller, Michael Richter, Marta Luzhetska, Marcel Wilde, Andreas Präg, Matthias Häckh
Publikováno v:
Journal of the American Chemical Society. 136:6195-6198
Intermolecular oxidative phenol coupling is the main process in nature for the formation of atroposelective biaryl compounds. Although well defined in plants and fungi, this type of dimerization reaction in bacteria is poorly understood. Therefore, t
Autor:
Marija Marolt, Stefan Günther, Matthias Häckh, Xavier Lucas, Steffen Lüdeke, Michael Müller, Peter F. Leadlay
Publikováno v:
ChemBioChem. 20:1090-1090
Publikováno v:
Chemistry - A European Journal. 19:8922-8928
The stereospecificity of an enzymatic reaction depends on the way in which a substrate and its enantiomer bind to the active site. These binding modes cannot be easily predicted. We have studied the stereospecificity and stereoselectivity of the keto
Autor:
Wolfgang Kroutil, Kirsten Zeitler, Martina Pohl, Dörte Rother, Justyna Kulig, Matthias Häckh, Christopher A. Rose, Steffen Lüdeke, Robert C. Simon, Syed Masood Husain
Publikováno v:
Catalysis Science & Technology 2, 1580-1589 (2012). doi:10.1039/c2cy20120h
Although biotransformations implementing alcohol dehydrogenases (ADHs) are widespread, enzymes which catalyse the reduction and oxidation of sterically demanding substrates, especially 2-hydroxy ketones, are still rare. To fill this gap eight ADHs we