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Rational engineering of Luminiphilus syltensis ( R )-selective amine transaminase for the acceptance of bulky substrates

Abstract (Expand)

Despite the plethora of information on (S)-selective amine transaminases, the (R)-selective ones are still not well-studied; only a few structures are known to the day, and their substrate scope is … limited, apart from a few stellar works on the field. Herein, Luminiphilus syltensis (R)-selective amine transaminase’s structure was elucidated to facilitate the engineering towards variants active on bulkier substrates. V37A variant led to increased activity towards 1-phenylpropylamine and to activity against 1-butylamine. On the contrary, S248 and T249 positions, located on the β-turn in P-pocket, seem crucial for maintaining enzyme’s activity.

Authors: Eleni Konia, Konstantinos Chatzicharalampous, Athina Drakonaki, Cornelia Muenke, Ulrich Ermler, Georgios Tsiotis, Ioannis V. Pavlidis

Date Published: 2021

Publication Type: Journal

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