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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)
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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.
