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.
Publication type: Journal
Journal: Chemical Communications
Citation: Chem. Commun.,10.1039.D1CC04664K
Date Published: 2021
Registered Mode: by DOI
Created: 14th Nov 2021 at 14:57
Last updated: 16th Nov 2021 at 13:04