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

By E. Konia, Konstantinos Chatzicharalampous, Athina Drakonaki, Cornelia Muenke, U. Ermler, G. Tsiotis, Ioannis V. Pavlidis. 2021

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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 date, and their substrate scope is limited, apart from a few stellar works in the field. Herein, the structure of Luminiphilus syltensis (R)-selective amine transaminase is elucidated to facilitate engineering towards variants active on bulkier substrates. The V37A variant led to increased activity towards 1-phenylpropylamine and to activity against 1-butylamine. In contrast, the S248 and T249 positions, located on the β-turn in the P-pocket, seem crucial for maintaining the activity of the enzyme.

Subfields: Molecular Biology, Organic Chemistry