Revealing the Structural Basis of Promiscuous Amine Transaminase Activity



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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.