Revealing the Structural Basis of Promiscuous Amine Transaminase Activity

Abstract

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. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.