Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Patrizia Lehwald"'
Publikováno v:
ChemBioChem. 17:1207-1210
Thiamine diphosphate-dependent enzymes catalyze the formation of C-C bonds, thereby generating chiral secondary or tertiary alcohols. By the use of vibrational circular dichroism (VCD) spectroscopy we studied the stereoselectivity of carboligations c
Autor:
Martina Pohl, Michael Müller, Luzia Wiesli, Sabrina Hampel, Michael Richter, Doreen Dobritzsch, Jan Patrick Steitz, Anna Baierl, Patrizia Lehwald, Gunter Schneider, Alexander Fries
Publikováno v:
ChemBioChem
A wide range of thiamine diphosphate (ThDP)‐dependent enzymes catalyze the benzoin‐type carboligation of pyruvate with aldehydes. A few ThDP‐dependent enzymes, such as YerE from Yersinia pseudotuberculosis (YpYerE), are known to accept ketones
Autor:
Finian J. Leeper, Werner Hummel, Susana L. A. Andrade, Volker Brecht, Sabrina Loschonsky, Patrizia Lehwald, Michael Müller, Maryam Beigi
Publikováno v:
Org. Biomol. Chem.. 11:252-256
The thiamine diphosphate (ThDP) dependent MenD catalyzes the reaction of α-ketoglutarate with pyruvate to selectively form 4-hydroxy-5-oxohexanoic acid 2, which seems to be inconsistent with the assumed acyl donor role of the physiological substrate
Publikováno v:
Angewandte Chemie International Edition. 49:2389-2392
Thiamine diphosphate (ThDP)-dependent enzymes are well-established catalysts in the field of asymmetric synthesis.[1] One of the example reactions catalyzed by various types of these enzymes are asymmetric C-C-bond formations of two aldehydes which l
Publikováno v:
Angewandte Chemie. 122:2439-2442
Publikováno v:
ChemInform. 41
The method uses a ThDP-dependent enzyme YerE, the O-antigen of Yersinia pseudotuberculosis O:VI.