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Rational engineerin...
Rational engineering of Luminiphilus syltensis(R)-selective amine transaminase for the acceptance of bulky substrates
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- Konia, Eleni (författare)
- University of Crete
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- Chatzicharalampous, Constantinos (författare)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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- Drakonaki, Athina (författare)
- University of Crete
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- Muenke, Cornelia (författare)
- Max Planck Institute of Biophysics
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- Ermler, Ulrich (författare)
- Max Planck Institute of Biophysics
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- Tsiotis, Georgios (författare)
- University of Crete
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- Pavlidis, Ioannis V. (författare)
- University of Crete
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(creator_code:org_t)
- 2021
- 2021
- Engelska 4 s.
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Ingår i: Chemical Communications. - : Royal Society of Chemistry (RSC). - 1359-7345 .- 1364-548X. ; 57:96, s. 12948-12951
- Relaterad länk:
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http://dx.doi.org/10... (free)
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https://pubs.rsc.org...
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https://lup.lub.lu.s...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Publikations- och innehållstyp
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