Work

Inside Front Cover: Is a Malleable Active Site Loop the Key to High Substrate Promiscuity? Hybrid, Biocatalytic Route to Structurally Diverse Taxoid Side Chains with Remarkable Dual Stereocontrol (Angew. Chem. Int. Ed. 36/2025)

Year: 2025

Type: paratext

Abstract: In their Research Article (e202510889), Berkowitz, Wilson, Grubmueller and co-workers describe the malleable structure of CaADH (Clostridium acetobutylicum alcohol dehydrogenase) and its panoply of loop conformers (top). They deploy CaADH for a dynamic reductive kinetic resolution (DYRKR) entry into new side chains for the Taxotere family of chemotherapeutics. The middle image shows an X-ray crystal structure of a key enzymatic product and Taxotere building block with the proper stereochemistry. Artistic Credit: Ewa Kijowska-Stroes.

Source: Angewandte Chemie International Edition

DOI: 10.1002/anie.202517791

Authors: Gaurav P. Kudalkar, Florian Leidner, Nivesh Kumar, Jared L. Hass, Peter Madzelan, Douglas R. Powell, Victor W. Day, Pierre Le Magueres, Joseph D. Ferrara, Lee M. Daniels, Akihito Yamano, Sho Ito, Wei Niu, Helmut Grubmüller, Mark A. Wilson, David B. Berkowitz

Institutions: University of Nebraska–Lincoln, Max Planck Institute for Multidisciplinary Sciences, University of Oklahoma, University of Kansas, Rigaku (Japan)

Language: English

Topic: Enzyme Catalysis and Immobilization

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

OpenAlex ID: W4413373584

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