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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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Journal ArticleDOI

Cytochrome P450-catalyzed regio- and stereoselective phenol coupling of fungal natural products

Laura S. Mazzaferro, +3 more
- 21 Sep 2015 - 
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

Christina Sommer-Kamann, +4 more
- 27 Mar 2017 - 
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

Maryam Beigi, +5 more
- 14 Jan 2013 - 
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, +9 more
- 26 Jan 2016 - 
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, +10 more
- 01 Jul 2019 - 
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 %).