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Article

Donor Promiscuity of a Thermostable Transketolase by Directed Evolution: Efficient Complementation of 1-Deoxy-d-xylulose-5-phosphate Synthase Activity.

Angewandte Chemie (International ed. in English) - 2 May 2017

Saravanan Thangavelu, Junker Sebastian, Kickstein Michael, Hein Sascha, Link Marie-Kristin, Ranglack Jan, Witt Samantha, Lorillière Marion, Hecquet Laurence, Fessner Wolf-Dieter

Abstract excerpt

Enzymes catalyzing asymmetric carboligation reactions typically show very high substrate specificity for their nucleophilic donor substrate components. Structure-guided engineering of the thermostable transketolase from Geobacillus stearothermophilus by directed in vitro evolution yielded new enzyme variants that are able to utilize pyruvate and higher aliphatic homologues as nucleophilic components for acyl...

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PMID: 28378514
DOI: 10.1002/anie.201701169

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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