Identification of Candida tenuisxylose reductase as highly selective biocatalyst for the synthesis of aromatic α-hydroxyesters and improvement of its efficiency by protein engineering
Literature Information
Regina Kratzer, Bernd Nidetzky
Wild-type Candida tenuisxylose reductase and two Trp-23 mutants thereof catalyze NADH-dependent reduction of a homologous series of aromatic α-keto esters with absolute pseudo re-face stereoselectivity and broad tolerance for the substituent on the aromatic ring, producing the corresponding R-alcohols in high yield.
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Chemical Communications

ChemComm publishes urgent research which is of outstanding significance and interest to experts in the field, while also appealing to the journal’s broad chemistry readership. Our communication format is ideally suited to short, urgent studies that are of such importance that they require accelerated publication. Our scope covers all topics in chemistry, and research at the interface of chemistry and other disciplines (such as materials science, nanoscience, physics, engineering and biology) where there is a significant novelty in the chemistry aspects. Major topic areas covered include: Analytical Chemistry Catalysis Chemical Biology and medicinal chemistry Computational Chemistry and Machine Learning Energy and sustainable chemistry Environmental Chemistry Green Chemistry Inorganic Chemistry Materials Chemistry Nanoscience Organic Chemistry Physical Chemistry Polymer Chemistry Supramolecular Chemistry










![7-Bromo-5-chloro-1H-pyrazolo[4,3-b]pyridine structure 7-Bromo-5-chloro-1H-pyrazolo[4,3-b]pyridine structure](https://static.chemtradehub.com/structs/135/1351813-70-1-a716.webp)



