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Search: WFRF:(Muenke Cornelia)

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  • Konia, Eleni, et al. (author)
  • Rational engineering of Luminiphilus syltensis(R)-selective amine transaminase for the acceptance of bulky substrates
  • 2021
  • In: Chemical Communications. - : Royal Society of Chemistry (RSC). - 1359-7345 .- 1364-548X. ; 57:96, s. 12948-12951
  • 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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Type of publication
journal article (1)
Type of content
peer-reviewed (1)
Author/Editor
Konia, Eleni (1)
Chatzicharalampous, ... (1)
Drakonaki, Athina (1)
Muenke, Cornelia (1)
Ermler, Ulrich (1)
Tsiotis, Georgios (1)
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Pavlidis, Ioannis V. (1)
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University
Lund University (1)
Language
English (1)
Research subject (UKÄ/SCB)
Natural sciences (1)
Year
2021 (1)

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