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Verena Gehmayr, Christa Mollay, Lorenz Reith, Prof. Dr. Norbert Müller and Dr. Alexander Jilek Tight Binding of Transition-State Analogues to a Peptidyl-Aminoacyl-L/D-Isomerase from Frog Skin ChemBioChem 12

Version of Record online: 7 JUL 2011 | DOI: 10.1002/cbic.201100203

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Changing hands: In the biosynthesis of bombinin H, an isomerase catalyses the inversion of chirality of an amino acid in peptide linkage through a deprotonation/protonation mechanism. We have synthesized two substrate analogues (1) that are potent inhibitors of the enzyme reaction. Our results strongly support a planar transition state, such as an enolate anion intermediate (2).

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