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Fabian Steffen-Munsberg, Dr. Clare Vickers, Ahmad Thontowi, Dr. Sebastian Schätzle, Tina Meinhardt, Dr. Maria Svedendahl Humble, Henrik Land, Prof. Dr. Per Berglund, Prof. Dr. Uwe T. Bornscheuer and Prof. Dr. Matthias Höhne Revealing the Structural Basis of Promiscuous Amine Transaminase Activity ChemCatChem 5

Version of Record online: 8 NOV 2012 | DOI: 10.1002/cctc.201200545

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One lock for different keys: A flexible arginine in the active site allows γ-aminobutyrate:pyruvate transaminases to bind the chemically different substrates L-alanine and γ-aminobutyric acid. Moreover, a flexible arginine residue facilitates the promiscuous conversion of (S)-amines and ketones. The degree of promiscuity can be related to distinct key amino acids lying at the surface of the active site.

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