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Alexander Fries
Researcher at University of Freiburg
Publications - 8
Citations - 185
Alexander Fries is an academic researcher from University of Freiburg. The author has contributed to research in topics: Biocatalysis & Michael reaction. The author has an hindex of 6, co-authored 7 publications receiving 143 citations. Previous affiliations of Alexander Fries include Facultad de Ciencias Exactas y Naturales.
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Cytochrome P450-catalyzed regio- and stereoselective phenol coupling of fungal natural products
TL;DR: The results show that fungi use highly specific cytochrome P450 enzymes for regio- and stereoselective phenol coupling and suggest that bimolecular phenoxy radical couplings in nature can be catalyzed by phenol-coupling P450 heme enzymes, which might also apply to the plant kingdom.
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Asymmetric C‐Alkylation by the S‐Adenosylmethionine‐Dependent Methyltransferase SgvM
TL;DR: It is shown that SgvM from Streptomyces griseoviridis features an extended substrate scope with respect to the nucleophile as well as the electrophile, and could be a valuable tool for asymmetric biocatalytic C-alkylation reactions.
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TCA Cycle Involved Enzymes SucA and Kgd, as well as MenD: Efficient Biocatalysts for Asymmetric C–C Bond Formation
TL;DR: Asymmetric mixed carboligation reactions of α-ketoglutarate with different aldehydes were explored with the thiamine diphosphate dependent enzymes SucA, Kgd and MenD to selectively deliver chiral δ-hydroxy-γ-keto acids with moderate to excellent stereoselectivity.
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25‐Hydroxyvitamin D3 Synthesis by Enzymatic Steroid Side‐Chain Hydroxylation with Water
Markus Warnke,Tobias Jung,Juri Dermer,Karin Hipp,Nico Jehmlich,Martin von Bergen,Sascha Ferlaino,Alexander Fries,Michael Müller,Matthias Boll +9 more
TL;DR: This facile and robust method developed for 25OHVD3 synthesis is a novel example for the concept of substrate-engineered catalysis and offers an attractive alternative to chemical or O2 /electron-donor-dependent enzymatic procedures.
Journal ArticleDOI
Alteration of the Route to Menaquinone towards Isochorismate‐Derived Metabolites
Alexander Fries,Alexander Fries,Laura S. Mazzaferro,Laura S. Mazzaferro,Björn Grüning,Philippe Bisel,Karin Stibal,Patrick C. F. Buchholz,Jürgen Pleiss,Georg A. Sprenger,Michael Müller +10 more
TL;DR: Unexpectedly, as the identified residues such as Arg107 are highly conserved, some of the designed variations can be found in wild‐type SEPHCHC synthases from other bacteria (Arg107Lys, 0.3 %).