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


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.

Citation: Chem. Commun.,10.1039.D1CC04664K

Date Published: 2021

Registered Mode: by DOI

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

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Konia, E., Chatzicharalampous, K., Drakonaki, A., Muenke, C., Ermler, U., Tsiotis, G., & Pavlidis, I. V. (2021). Rational engineering of Luminiphilus syltensis (R)-selective amine transaminase for the acceptance of bulky substrates. In Chemical Communications (Vol. 57, Issue 96, pp. 12948–12951). Royal Society of Chemistry (RSC). https://doi.org/10.1039/d1cc04664k

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Created: 14th Nov 2021 at 14:57

Last updated: 16th Nov 2021 at 13:04

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