Issue 96, 2021

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

Abstract

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 exhibited 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.

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

Supplementary files

Article information

Article type
Communication
Submitted
21 Aug 2021
Accepted
11 Nov 2021
First published
11 Nov 2021
This article is Open Access
Creative Commons BY license

Chem. Commun., 2021,57, 12948-12951

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

E. Konia, K. Chatzicharalampous, A. Drakonaki, C. Muenke, U. Ermler, G. Tsiotis and I. V. Pavlidis, Chem. Commun., 2021, 57, 12948 DOI: 10.1039/D1CC04664K

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