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- Konia, Eleni, et al.
(author)
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Rational engineering of Luminiphilus syltensis(R)-selective amine transaminase for the acceptance of bulky substrates
- 2021
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In: Chemical Communications. - : Royal Society of Chemistry (RSC). - 1359-7345 .- 1364-548X. ; 57:96, s. 12948-12951
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Journal article (peer-reviewed)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 ofLuminiphilus 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.
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